ID EDD1_RAT Reviewed; 920 AA. AC Q62671; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 05-MAR-2002, sequence version 2. DT 20-FEB-2007, entry version 45. DE Ubiquitin-protein ligase EDD1 (EC 6.3.2.-) (Hyperplastic discs protein DE homolog) (100 kDa protein) (Fragment). GN Name=Edd1; Synonyms=Dd5, Edd, Hyd; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Testis; RX MEDLINE=92253337; PubMed=1533713; DOI=10.1093/nar/20.7.1471; RA Mueller D., Rehbein M., Baumeister H., Richter D.; RT "Molecular characterization of a novel rat protein structurally RT related to poly(A) binding proteins and the 70K protein of the U1 RT small nuclear ribonucleoprotein particle (snRNP)."; RL Nucleic Acids Res. 20:1471-1475(1992). RN [2] RP ERRATUM. RA Mueller D., Rehbein M., Baumeister H., Richter D.; RL Nucleic Acids Res. 20:2624-2624(1992). RN [3] RP IDENTIFICATION OF PROBABLE FRAMESHIFT. RX MEDLINE=99153743; PubMed=10030672; DOI=10.1038/sj.onc.1202249; RA Callaghan M.J., Russell A.J., Woollatt E., Sutherland G.R., RA Sutherland R.L., Watts C.K.W.; RT "Identification of a human HECT family protein with homology to the RT Drosophila tumor suppressor gene hyperplastic discs."; RL Oncogene 17:3479-3491(1998). RN [4] RP CHARACTERIZATION. RX PubMed=12239083; DOI=10.1210/en.2002-220262; RA Oughtred R., Bedard N., Adegoke O.A.J., Morales C.R., Trasler J., RA Rajapurohitam V., Wing S.S.; RT "Characterization of rat100, a 300-kilodalton ubiquitin-protein ligase RT induced in germ cells of the rat testis and similar to the Drosophila RT hyperplastic discs gene."; RL Endocrinology 143:3740-3747(2002). CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from CC an E2 ubiquitin-conjugating enzyme in the form of a thioester and CC then directly transfers the ubiquitin to targeted substrates (By CC similarity). May be involved in maturation and/or post- CC transcriptional regulation of mRNA. May play a role in control of CC cell cycle progression. May have tumor suppressor function. CC Regulates DNA topoisomerase II binding protein (TopBP1) for the CC DNA damage response. Plays an essential role in extraembryonic CC development (By similarity). CC -!- SUBUNIT: Binds TOPBP1 (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- TISSUE SPECIFICITY: Highest levels found in testis. Also present CC in liver, kidney, lung and brain. CC -!- DEVELOPMENTAL STAGE: In early post-natal life, expression in the CC testis increases to reach a maximum around day 28. CC -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin- CC thioester formation. CC -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein CC ligase) domain. CC -!- CAUTION: Ref.1 (CAA45756) sequence differs from that shown due to CC a frameshift in position 30. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X64411; CAA45756.1; ALT_FRAME; mRNA. DR UniGene; Rn.54812; -. DR HSSP; O95071; 1I2T. DR SMR; Q62671; 515-575. DR Ensembl; ENSRNOG00000006816; Rattus norvegicus. DR KEGG; rno:117060; -. DR RGD; 621236; Dd5. DR ArrayExpress; Q62671; -. DR GermOnline; ENSRNOG00000006816; Rattus norvegicus. DR InterPro; IPR000569; HECT. DR InterPro; IPR002004; PABP_HYD. DR Pfam; PF00632; HECT; 1. DR Pfam; PF00658; PABP; 1. DR SMART; SM00119; HECTc; 1. DR SMART; SM00517; PolyA; 1. DR PROSITE; PS50237; HECT; 1. KW Ligase; Nuclear protein; Ubl conjugation pathway. FT CHAIN <1 920 Ubiquitin-protein ligase EDD1. FT /FTId=PRO_0000086933. FT DOMAIN 583 920 HECT. FT REGION 515 571 PABP-like. FT COMPBIAS 108 119 Asp/Glu-rich (acidic). FT COMPBIAS 158 181 Pro-rich. FT COMPBIAS 451 470 Arg/Glu-rich (mixed charge). FT COMPBIAS 479 488 Arg/Asp-rich (mixed charge). FT COMPBIAS 610 621 Asp/Glu-rich (acidic). FT COMPBIAS 858 878 Pro-rich. FT ACT_SITE 889 889 Glycyl thioester intermediate (By FT similarity). FT NON_TER 1 1 SQ SEQUENCE 920 AA; 103950 MW; 465771084536C3AA CRC64; ARRERMTARE EASLRTLEGR RRATLLSARQ GMMSARGDFL NYALSLMRSH NDEHSDVLPV LDVCSLKHVA YVFQALIYWI KAMNQQTTLD TPQLERKRTR ELLELGIDNE DSEHENDDDT SQSATLNDKD DESLPAETGQ NHPFFRRSDS MTFLGCIPPN PFEVPLAEAI PLADQPHLLQ PNARKEDLFG RPSQGLYSSS AGSGKCLVEV TMDRNCLEVL PTKMSYAANL KNVMNMQNRQ KKAGEDQSML AEEADSSKPG PSAHDVAAQL KSSLLAEIGL TESEGPPLTS FRPQCSFMGM VISHDMLLGR WRLSLELFGR VFMEDVGAEP GSILTELGGF EVKESKFRRE MEKLRNQQSR DLSLEVDRDR DLLIQQTMRQ LNNHFGRRCA TTPMAVHRVK VTFKDEPGEG SGVARSFYTA IAQAFLSNEK LPNLDCIQNA NKGTHTSLMQ RLRNRGERDR EREREREMRR SSGLRAGSRR DRDRDFRRQL SIDTRPFRPA SEGNPSDDPD PLPAHRQALG ERLYPRVQAM QPAFASKITG MLLELSPAQL LLLLASEDSL RARVEEAMEL IVAHGRENGA DSILDLGLLD SSEKVQENRK RHGSSRSVVD MDLDDTDDGD DNAPLFYQPG KRGFYTPRPG KNTEARLNCF RNIGRILGLC LLQNELCPIT LNRHVIKVLL GRKVNWHDFA FFDPVMYESL RQLILASQSS DADAVFSAMD LAFAVDLCKE EGGGQVELIP NGVNIPVTPQ NVYEYVRKYA EHRMLVVAEQ PLHAMRKGLL DVLPKNSLED LTAEDFRLLV NGCGEVNVQM LISFTSFNDE SGENAEKLLQ FKRWFWSIVE RMSMTERQDL VYFWTSSPSL PASEEGFQPM PSITIRPPDD QHLPTANTCI SRLYVPLYSS KQILKQKLLL AIKTKNFGFV // ID 5HT1D_FUGRU Reviewed; 379 AA. AC P79748; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 20-MAR-2007, entry version 40. DE 5-hydroxytryptamine 1D receptor (5-HT-1D) (Serotonin receptor 1D) DE (5HT1D) (F1D). OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Testis; RX MEDLINE=97361762; PubMed=9218723; DOI=10.1016/S0378-1119(97)00064-4; RA Yamaguchi F., Brenner S.; RT "Molecular cloning of 5-hydroxytryptamine (5-HT) type 1 receptor genes RT from the Japanese puffer fish, Fugu rubripes."; RL Gene 191:219-223(1997). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. The activity of CC this receptor is mediated by G proteins that inhibit adenylate CC cyclase activity (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X83865; CAA58745.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR Ensembl; NEWSINFRUG00000120815; Fugu rubripes. DR InterPro; IPR000505; 5HT1D_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00514; 5HT1DRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 379 5-hydroxytryptamine 1D receptor. FT /FTId=PRO_0000068932. FT TOPO_DOM 1 36 Extracellular (Potential). FT TRANSMEM 37 60 1 (Potential). FT TOPO_DOM 61 73 Cytoplasmic (Potential). FT TRANSMEM 74 96 2 (Potential). FT TOPO_DOM 97 106 Extracellular (Potential). FT TRANSMEM 107 132 3 (Potential). FT TOPO_DOM 133 152 Cytoplasmic (Potential). FT TRANSMEM 153 174 4 (Potential). FT TOPO_DOM 175 192 Extracellular (Potential). FT TRANSMEM 193 216 5 (Potential). FT TOPO_DOM 217 307 Cytoplasmic (Potential). FT TRANSMEM 308 331 6 (Potential). FT TOPO_DOM 332 339 Extracellular (Potential). FT TRANSMEM 340 364 7 (Potential). FT TOPO_DOM 365 379 Cytoplasmic (Potential). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 14 14 N-linked (GlcNAc...) (Potential). FT CARBOHYD 21 21 N-linked (GlcNAc...) (Potential). FT DISULFID 109 186 By similarity. SQ SEQUENCE 379 AA; 42302 MW; 99B6E2C0379EBC78 CRC64; MELDNNSLDY FSSNFTDIPS NTTVAHWTEA TLLGLQISVS VVLAIVTLAT MLSNAFVIAT IFLTRKLHTP ANFLIGSLAV TDMLVSILVM PISIVYTVSK TWSLGQIVCD IWLSSDITFC TASILHLCVI ALDRYWAITD ALEYSKRRTM RRAAVMVAVV WVISISISMP PLFWRQAKAH EELKECMVNT DQISYTLYST FGAFYVPTVL LIILYGRIYV AARSRIFKTP SYSGKRFTTA QLIQTSAGSS LCSLNSASNQ EAHLHSGAGG EGGGSPLFVN SVKVKLADNV LERKRLCAAR ERKATKTLGI ILGAFIICWL PFFVVTLVWA ICKECSFDPL LFDVFTWLGY LNSLINPVIY TVFNDEFKQA FQKLIKFRR // ID ACTB1_FUGRU Reviewed; 375 AA. AC P68142; P53484; DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 20-MAR-2007, entry version 16. DE Actin, cytoplasmic 1 (Beta-actin A). GN Name=ACTB-A; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RX MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347; RA Venkatesh B., Tay B.H., Elgar G., Brenner S.; RT "Isolation, characterization and evolution of nine pufferfish (Fugu RT rubripes) actin genes."; RL J. Mol. Biol. 259:655-665(1996). CC -!- FUNCTION: Actins are highly conserved proteins that are involved CC in various types of cell motility and are ubiquitously expressed CC in all eukaryotic cells. CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a CC structural filament (F-actin) in the form of a two-stranded helix. CC Each actin can bind to 4 others. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Widely distributed. Not expressed in skeletal CC muscle. CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, CC alpha, beta and gamma have been identified. The alpha actins are CC found in muscle tissues and are a major constituent of the CC contractile apparatus. The beta and gamma actins coexist in most CC cell types as components of the cytoskeleton and as mediators of CC internal cell motility. CC -!- MISCELLANEOUS: There are three different beta-cytoplasmic actins CC in Fugu rubripes. CC -!- SIMILARITY: Belongs to the actin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U37499; AAC59889.1; -; Genomic_DNA. DR PIR; S71124; S71124. DR HSSP; P02570; 1HLU. DR SMR; P68142; 4-371. DR Ensembl; NEWSINFRUG00000152503; Fugu rubripes. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR PANTHER; PTHR11937; Actin_like; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Acetylation; ATP-binding; Cytoskeleton; Methylation; KW Nucleotide-binding; Structural protein. FT PROPEP 1 1 Removed in mature form (By similarity). FT /FTId=PRO_0000000808. FT CHAIN 2 375 Actin, cytoplasmic 1. FT /FTId=PRO_0000000809. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 2 2 N-acetylglutamate (By similarity). FT MOD_RES 73 73 Tele-methylhistidine (By similarity). SQ SEQUENCE 375 AA; 41767 MW; 9C505616D33E9495 CRC64; MEDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTYN SIMKCDVDIR KDLYANTVLS GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ EYDESGPSIV HRKCF // ID ACTB_OREMO Reviewed; 375 AA. AC P68143; P53484; DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 20-MAR-2007, entry version 16. DE Actin, cytoplasmic 1 (Beta-actin). GN Name=ACTB; OS Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Labroidei; OC Cichlidae; African cichlids; Pseudocrenilabrinae; Tilapiini; OC Oreochromis. OX NCBI_TaxID=8127; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Gill; RA Takeuchi K.; RT "Cloning of Tilapia actin cDNAs."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Actins are highly conserved proteins that are involved CC in various types of cell motility and are ubiquitously expressed CC in all eukaryotic cells. CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a CC structural filament (F-actin) in the form of a two-stranded helix. CC Each actin can bind to 4 others. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, CC alpha, beta and gamma have been identified. The alpha actins are CC found in muscle tissues and are a major constituent of the CC contractile apparatus. The beta and gamma actins coexist in most CC cell types as components of the cytoskeleton and as mediators of CC internal cell motility. CC -!- SIMILARITY: Belongs to the actin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB037865; BAA90688.1; -; mRNA. DR HSSP; P02570; 1HLU. DR SMR; P68143; 4-371. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR PANTHER; PTHR11937; Actin_like; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Acetylation; ATP-binding; Cytoskeleton; Methylation; KW Nucleotide-binding; Structural protein. FT PROPEP 1 1 Removed in mature form (By similarity). FT /FTId=PRO_0000000802. FT CHAIN 2 375 Actin, cytoplasmic 1. FT /FTId=PRO_0000000803. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 2 2 N-acetylglutamate (By similarity). FT MOD_RES 73 73 Tele-methylhistidine (By similarity). SQ SEQUENCE 375 AA; 41767 MW; 9C505616D33E9495 CRC64; MEDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTYN SIMKCDVDIR KDLYANTVLS GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ EYDESGPSIV HRKCF // ID ACTB2_FUGRU Reviewed; 375 AA. AC P53485; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-MAR-2007, entry version 39. DE Actin, cytoplasmic 2 (Beta-actin B). GN Name=ACTB-B; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347; RA Venkatesh B., Tay B.H., Elgar G., Brenner S.; RT "Isolation, characterization and evolution of nine pufferfish (Fugu RT rubripes) actin genes."; RL J. Mol. Biol. 259:655-665(1996). CC -!- FUNCTION: Actins are highly conserved proteins that are involved CC in various types of cell motility and are ubiquitously expressed CC in all eukaryotic cells. CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a CC structural filament (F-actin) in the form of a two-stranded helix. CC Each actin can bind to 4 others. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, CC alpha, beta and gamma have been identified. The alpha actins are CC found in muscle tissues and are a major constituent of the CC contractile apparatus. The beta and gamma actins coexist in most CC cell types as components of the cytoskeleton and as mediators of CC internal cell motility. CC -!- MISCELLANEOUS: There are three different beta-cytoplasmic actins CC in Fugu rubripes. CC -!- SIMILARITY: Belongs to the actin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U38848; AAC59890.1; -; Genomic_DNA. DR PIR; S71125; S71125. DR HSSP; P02570; 1HLU. DR SMR; P53485; 4-371. DR Ensembl; NEWSINFRUG00000152503; Fugu rubripes. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR PANTHER; PTHR11937; Actin_like; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Acetylation; ATP-binding; Cytoskeleton; Methylation; KW Nucleotide-binding; Structural protein. FT PROPEP 1 1 Removed in mature form (By similarity). FT /FTId=PRO_0000000810. FT CHAIN 2 375 Actin, cytoplasmic 2. FT /FTId=PRO_0000000811. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 2 2 N-acetylaspartate (By similarity). FT MOD_RES 73 73 Tele-methylhistidine (By similarity). SQ SEQUENCE 375 AA; 41767 MW; 1AE990BC0AED0D1C CRC64; MDDEIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMGTA ASSSSLEKSY ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS GGTTMYPGIA DRMQKEITSL APTTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ EYDESGPSIV HRKCF // ID ACTB3_FUGRU Reviewed; 375 AA. AC P53486; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-MAR-2007, entry version 39. DE Actin, cytoplasmic 3 (Beta-actin C). GN Name=ACTB-C; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RX MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347; RA Venkatesh B., Tay B.H., Elgar G., Brenner S.; RT "Isolation, characterization and evolution of nine pufferfish (Fugu RT rubripes) actin genes."; RL J. Mol. Biol. 259:655-665(1996). CC -!- FUNCTION: Actins are highly conserved proteins that are involved CC in various types of cell motility and are ubiquitously expressed CC in all eukaryotic cells. CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a CC structural filament (F-actin) in the form of a two-stranded helix. CC Each actin can bind to 4 others. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Predominantly expressed in gills, kidney and CC skin. CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, CC alpha, beta and gamma have been identified. The alpha actins are CC found in muscle tissues and are a major constituent of the CC contractile apparatus. The beta and gamma actins coexist in most CC cell types as components of the cytoskeleton and as mediators of CC internal cell motility. CC -!- MISCELLANEOUS: There are three different beta-cytoplasmic actins CC in Fugu rubripes. CC -!- SIMILARITY: Belongs to the actin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U38849; AAC59891.1; -; Genomic_DNA. DR PIR; S71126; S71126. DR HSSP; P02570; 2BTF. DR SMR; P53486; 4-371. DR Ensembl; NEWSINFRUG00000152503; Fugu rubripes. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR PANTHER; PTHR11937; Actin_like; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Acetylation; ATP-binding; Cytoskeleton; Methylation; KW Nucleotide-binding; Structural protein. FT PROPEP 1 1 Removed in mature form (By similarity). FT /FTId=PRO_0000000840. FT CHAIN 2 375 Actin, cytoplasmic 3. FT /FTId=PRO_0000000841. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 2 2 N-acetylglutamate (By similarity). FT MOD_RES 73 73 Tele-methylhistidine (By similarity). SQ SEQUENCE 375 AA; 41783 MW; 8B451E0DB3399C0B CRC64; MEDEVASLVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA SSSSSLEKSY ELPDGQVITI GNERFRCPEA LFQPSFLGME SSGIHETTYN SIMKCDVDIR KDLYANTVLS GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ EYDESGPSIV HRKCF // ID ACTC_FUGRU Reviewed; 377 AA. AC P53480; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 03-APR-2007, entry version 42. DE Actin, alpha cardiac. OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RX MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347; RA Venkatesh B., Tay B.H., Elgar G., Brenner S.; RT "Isolation, characterization and evolution of nine pufferfish (Fugu RT rubripes) actin genes."; RL J. Mol. Biol. 259:655-665(1996). CC -!- FUNCTION: Actins are highly conserved proteins that are involved CC in various types of cell motility and are ubiquitously expressed CC in all eukaryotic cells. CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a CC structural filament (F-actin) in the form of a two-stranded helix. CC Each actin can bind to 4 others. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Predominantly expressed in heart. Lower levels CC in skeletal muscle and skin. CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, CC alpha, beta and gamma have been identified. The alpha actins are CC found in muscle tissues and are a major constituent of the CC contractile apparatus. The beta and gamma actins coexist in most CC cell types as components of the cytoskeleton and as mediators of CC internal cell motility. CC -!- MISCELLANEOUS: There are three genes coding for cardiac actin in CC Fugu. CC -!- SIMILARITY: Belongs to the actin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U38959; AAC59894.1; -; Genomic_DNA. DR EMBL; U38960; AAC59895.1; -; Genomic_DNA. DR EMBL; U38961; AAC59896.1; -; Genomic_DNA. DR PIR; S71120; S71120. DR HSSP; P02568; 1MDU. DR SMR; P53480; 6-373. DR Ensembl; NEWSINFRUG00000137636; Fugu rubripes. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR PANTHER; PTHR11937; Actin_like; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Acetylation; ATP-binding; Cytoskeleton; Methylation; Muscle protein; KW Nucleotide-binding; Structural protein. FT PROPEP 1 2 Removed in mature form (By similarity). FT /FTId=PRO_0000000826. FT CHAIN 3 377 Actin, alpha cardiac. FT /FTId=PRO_0000000827. FT MOD_RES 3 3 N-acetylaspartate (By similarity). FT MOD_RES 75 75 Tele-methylhistidine (By similarity). SQ SEQUENCE 377 AA; 41975 MW; 0499A43921D9BBCF CRC64; MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETA YNSIMKCDID IRKDLYANNV LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS KQEYDEAGPS IVHRKCF // ID ACTSA_FUGRU Reviewed; 377 AA. AC P68140; P53481; DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 20-MAR-2007, entry version 16. DE Actin, alpha skeletal muscle A (Alpha-actin-1 A). GN Name=ACTA1-A; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RX MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347; RA Venkatesh B., Tay B.H., Elgar G., Brenner S.; RT "Isolation, characterization and evolution of nine pufferfish (Fugu RT rubripes) actin genes."; RL J. Mol. Biol. 259:655-665(1996). CC -!- FUNCTION: Actins are highly conserved proteins that are involved CC in various types of cell motility and are ubiquitously expressed CC in all eukaryotic cells. CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a CC structural filament (F-actin) in the form of a two-stranded helix. CC Each actin can bind to 4 others. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle. CC Lower levels in heart. CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, CC alpha, beta and gamma have been identified. The alpha actins are CC found in muscle tissues and are a major constituent of the CC contractile apparatus. The beta and gamma actins coexist in most CC cell types as components of the cytoskeleton and as mediators of CC internal cell motility. CC -!- MISCELLANEOUS: There are two different alpha-skeletal actins in CC Fugu rubripes. CC -!- SIMILARITY: Belongs to the actin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U38850; AAC59892.1; -; Genomic_DNA. DR PIR; S71118; S71118. DR HSSP; P02568; 1MDU. DR SMR; P68140; 6-373. DR Ensembl; NEWSINFRUG00000159793; Fugu rubripes. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR PANTHER; PTHR11937; Actin_like; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Acetylation; ATP-binding; Cytoskeleton; Methylation; Muscle protein; KW Nucleotide-binding; Structural protein. FT PROPEP 1 2 Removed in mature form (By similarity). FT /FTId=PRO_0000000862. FT CHAIN 3 377 Actin, alpha skeletal muscle A. FT /FTId=PRO_0000000863. FT MOD_RES 3 3 N-acetylaspartate (By similarity). FT MOD_RES 75 75 Tele-methylhistidine (By similarity). SQ SEQUENCE 377 AA; 41945 MW; 1C7185C0F7C19A26 CRC64; MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDAGDG VTHNVPVYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETA YNSIMKCDID IRKDLYANNV LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS KQEYDEAGPS IVHRKCF // ID ACTS_OREMO Reviewed; 377 AA. AC P68264; P53481; DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2004, sequence version 1. DT 20-MAR-2007, entry version 16. DE Actin, alpha skeletal muscle (Alpha-actin-1). GN Name=ACTA1; OS Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Labroidei; OC Cichlidae; African cichlids; Pseudocrenilabrinae; Tilapiini; OC Oreochromis. OX NCBI_TaxID=8127; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Skeletal muscle; RA Takeuchi K.; RT "Cloning of Tilapia actin cDNAs."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Actins are highly conserved proteins that are involved CC in various types of cell motility and are ubiquitously expressed CC in all eukaryotic cells. CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a CC structural filament (F-actin) in the form of a two-stranded helix. CC Each actin can bind to 4 others. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, CC alpha, beta and gamma have been identified. The alpha actins are CC found in muscle tissues and are a major constituent of the CC contractile apparatus. The beta and gamma actins coexist in most CC cell types as components of the cytoskeleton and as mediators of CC internal cell motility. CC -!- SIMILARITY: Belongs to the actin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB037866; BAA90689.1; -; mRNA. DR HSSP; P02568; 1MDU. DR SMR; P68264; 6-373. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR PANTHER; PTHR11937; Actin_like; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Acetylation; ATP-binding; Cytoskeleton; Methylation; Muscle protein; KW Nucleotide-binding; Structural protein. FT PROPEP 1 2 Removed in mature form (By similarity). FT /FTId=PRO_0000000866. FT CHAIN 3 377 Actin, alpha skeletal muscle. FT /FTId=PRO_0000000867. FT MOD_RES 3 3 N-acetylaspartate (By similarity). FT MOD_RES 75 75 Tele-methylhistidine (By similarity). SQ SEQUENCE 377 AA; 41945 MW; 1C7185C0F7C19A26 CRC64; MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDAGDG VTHNVPVYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETA YNSIMKCDID IRKDLYANNV LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS KQEYDEAGPS IVHRKCF // ID ACTSB_FUGRU Reviewed; 377 AA. AC P53482; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-MAR-2007, entry version 39. DE Actin, alpha skeletal muscle B (Alpha-actin-1 B). GN Name=ACTA1-B; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RX MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347; RA Venkatesh B., Tay B.H., Elgar G., Brenner S.; RT "Isolation, characterization and evolution of nine pufferfish (Fugu RT rubripes) actin genes."; RL J. Mol. Biol. 259:655-665(1996). CC -!- FUNCTION: Actins are highly conserved proteins that are involved CC in various types of cell motility and are ubiquitously expressed CC in all eukaryotic cells. CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a CC structural filament (F-actin) in the form of a two-stranded helix. CC Each actin can bind to 4 others. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle. CC Lower levels in heart, gills and skin. CC -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, CC alpha, beta and gamma have been identified. The alpha actins are CC found in muscle tissues and are a major constituent of the CC contractile apparatus. The beta and gamma actins coexist in most CC cell types as components of the cytoskeleton and as mediators of CC internal cell motility. CC -!- MISCELLANEOUS: There are two different alpha-skeletal actins in CC Fugu rubripes. CC -!- SIMILARITY: Belongs to the actin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U38958; AAC59893.1; -; Genomic_DNA. DR PIR; S71119; S71119. DR HSSP; P02568; 1MDU. DR SMR; P53482; 6-373. DR Ensembl; NEWSINFRUG00000161349; Fugu rubripes. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR PANTHER; PTHR11937; Actin_like; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW Acetylation; ATP-binding; Cytoskeleton; Methylation; Muscle protein; KW Nucleotide-binding; Structural protein. FT PROPEP 1 2 Removed in mature form (By similarity). FT /FTId=PRO_0000000864. FT CHAIN 3 377 Actin, alpha skeletal muscle B. FT /FTId=PRO_0000000865. FT MOD_RES 3 3 N-acetylaspartate (By similarity). FT MOD_RES 75 75 Tele-methylhistidine (By similarity). SQ SEQUENCE 377 AA; 41977 MW; A0973DD7B23B0C82 CRC64; MCDDDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH SFYNELRVAP EEHPTLLTEA PLNPKANREK MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMG TAASSSSLEK SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS KQEYDEAGPS IVHRKCF // ID ACTX_FUGRU Reviewed; 376 AA. AC P53483; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-MAR-2007, entry version 37. DE Actin, alpha anomalous. OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RX MEDLINE=96275651; PubMed=8683572; DOI=10.1006/jmbi.1996.0347; RA Venkatesh B., Tay B.H., Elgar G., Brenner S.; RT "Isolation, characterization and evolution of nine pufferfish (Fugu RT rubripes) actin genes."; RL J. Mol. Biol. 259:655-665(1996). CC -!- FUNCTION: Actins are highly conserved proteins that are involved CC in various types of cell motility and are ubiquitously expressed CC in all eukaryotic cells. CC -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a CC structural filament (F-actin) in the form of a two-stranded helix. CC Each actin can bind to 4 others. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: Predominantly expressed in testis. CC -!- SIMILARITY: Belongs to the actin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U38962; AAC59897.1; -; Genomic_DNA. DR PIR; S71123; S71123. DR HSSP; P02568; 1KXP. DR SMR; P53483; 7-372. DR Ensembl; NEWSINFRUG00000163710; Fugu rubripes. DR InterPro; IPR004001; Actin. DR InterPro; IPR004000; Actin_like. DR PANTHER; PTHR11937; Actin_like; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR PROSITE; PS00406; ACTINS_1; 1. DR PROSITE; PS00432; ACTINS_2; 1. DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1. KW ATP-binding; Cytoskeleton; Nucleotide-binding; Structural protein. FT CHAIN 1 376 Actin, alpha anomalous. FT /FTId=PRO_0000089056. SQ SEQUENCE 376 AA; 41979 MW; DB037F47BA1371D8 CRC64; MSDYDETALV CDNGSGLVKA GFAGDDTPRA VFHAIVGRPR HQDDMDDMGK KGYYVGDEAQ SKRDILSLKH PIERGIITNW DDMEKIWHHT FYNELCVAPE EHPTLLTEAP LNPKANREKM TQIMLETFNM PAMYVSIQAV LSLYASGRTT GIVLDSGEGV THAVPIAEGY ALPPAIMRLN LAGRDLTDYL MKILNERGYS FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKR YELPDGQVIT IGNERFCCPE TLFQPSFMGM ESAGIHEITH SSIMKCDIEI RKDLYANNVL TGGATLFPGI ADRMQKEITA LAPSTMKIQI IAPPERKYSV WIGGSILASL STFQQMWISK QEYEEIGPSI IHCKCF // ID ARF3_FUGRU Reviewed; 181 AA. AC P61207; P16587; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 03-APR-2007, entry version 22. DE ADP-ribosylation factor 3. GN Name=ARF3; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=99177347; PubMed=10077531; RA Gellner K., Brenner S.; RT "Analysis of 148 kb of genomic DNA around the wnt1 locus of Fugu RT rubripes."; RL Genome Res. 9:251-258(1999). CC -!- FUNCTION: GTP-binding protein that functions as an allosteric CC activator of the cholera toxin catalytic subunit, an ADP- CC ribosyltransferase. Involved in protein trafficking; may modulate CC vesicle budding and uncoating within the Golgi apparatus. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF056116; AAC34390.1; -; Genomic_DNA. DR HSSP; P32889; 1RRF. DR SMR; P61207; 2-180. DR Ensembl; NEWSINFRUG00000161195; Fugu rubripes. DR InterPro; IPR006688; ARF. DR InterPro; IPR006689; ARF/SAR. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP_bd. DR PANTHER; PTHR11711; ARF/SAR; 1. DR Pfam; PF00025; Arf; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR PRINTS; PR00328; SAR1GTPBP. DR SMART; SM00177; ARF; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS01019; ARF; 1. KW ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; KW Myristate; Nucleotide-binding; Protein transport; Transport. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 181 ADP-ribosylation factor 3. FT /FTId=PRO_0000207390. FT NP_BIND 24 31 GTP (By similarity). FT NP_BIND 67 71 GTP (By similarity). FT NP_BIND 126 129 GTP (By similarity). FT LIPID 2 2 N-myristoyl glycine (Potential). SQ SEQUENCE 181 AA; 20601 MW; D6FA234DFAED3E5F CRC64; MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK K // ID ARF3_HUMAN Reviewed; 181 AA. AC P61204; P16587; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 29. DE ADP-ribosylation factor 3. GN Name=ARF3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=89345613; PubMed=2474826; RA Bobak D.A., Nightingale M.S., Murtagh J.J. Jr., Price S.R., Moss J., RA Vaughan M.; RT "Molecular cloning, characterization, and expression of human ADP- RT ribosylation factors: two guanine nucleotide-dependent activators of RT cholera toxin."; RL Proc. Natl. Acad. Sci. U.S.A. 86:6101-6105(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92078170; PubMed=1744102; RA Tsai S.C., Haun R.S., Tsuchiya M., Moss J., Vaughan M.; RT "Isolation and characterization of the human gene for ADP-ribosylation RT factor 3, a 20-kDa guanine nucleotide-binding protein activator of RT cholera toxin."; RL J. Biol. Chem. 266:23053-23059(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, Lung, and Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP INTERACTION WITH PRKCABP. RX MEDLINE=20090608; PubMed=10623590; DOI=10.1006/bbrc.1999.1932; RA Takeya R., Takeshige K., Sumimoto H.; RT "Interaction of the PDZ domain of human PICK1 with class I ADP- RT ribosylation factors."; RL Biochem. Biophys. Res. Commun. 267:149-155(2000). CC -!- FUNCTION: GTP-binding protein that functions as an allosteric CC activator of the cholera toxin catalytic subunit, an ADP- CC ribosyltransferase. Involved in protein trafficking; may modulate CC vesicle budding and uncoating within the Golgi apparatus. CC -!- SUBUNIT: Interacts with PRKCABP. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M74493; AAA58359.1; -; Genomic_DNA. DR EMBL; M33384; AAA83931.1; -; mRNA. DR EMBL; M74491; AAB59425.1; -; mRNA. DR EMBL; AF493882; AAM12596.1; -; mRNA. DR EMBL; BT006670; AAP35316.1; -; mRNA. DR EMBL; BC007647; AAH07647.1; -; mRNA. DR EMBL; BC007762; AAH07762.1; -; mRNA. DR EMBL; BC017565; AAH17565.1; -; mRNA. DR EMBL; BC028402; AAH28402.1; -; mRNA. DR PIR; A41570; A41570. DR UniGene; Hs.119177; -. DR HSSP; P32889; 1RRF. DR SMR; P61204; 2-180. DR IntAct; P61204; -. DR OGP; P16587; -. DR Ensembl; ENSG00000134287; Homo sapiens. DR HGNC; HGNC:654; ARF3. DR MIM; 103190; gene. DR ArrayExpress; P61204; -. DR GermOnline; ENSG00000134287; Homo sapiens. DR RZPD-ProtExp; A0201; -. DR RZPD-ProtExp; IOH11881; -. DR RZPD-ProtExp; IOH26585; -. DR RZPD-ProtExp; IOH6999; -. DR RZPD-ProtExp; RZPDo839B12139; -. DR RZPD-ProtExp; RZPDo839B12140; -. DR RZPD-ProtExp; W0762; -. DR GO; GO:0005525; F:GTP binding; TAS:ProtInc. DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc. DR InterPro; IPR006688; ARF. DR InterPro; IPR006689; ARF/SAR. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP_bd. DR PANTHER; PTHR11711; ARF/SAR; 1. DR Pfam; PF00025; Arf; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR PRINTS; PR00328; SAR1GTPBP. DR SMART; SM00177; ARF; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS01019; ARF; 1. KW ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; KW Myristate; Nucleotide-binding; Protein transport; Transport. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 181 ADP-ribosylation factor 3. FT /FTId=PRO_0000207386. FT NP_BIND 24 31 GTP (By similarity). FT NP_BIND 67 71 GTP (By similarity). FT NP_BIND 126 129 GTP (By similarity). FT LIPID 2 2 N-myristoyl glycine (Potential). SQ SEQUENCE 181 AA; 20601 MW; D6FA234DFAED3E5F CRC64; MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK K // ID ARF3_MOUSE Reviewed; 181 AA. AC P61205; P16587; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 33. DE ADP-ribosylation factor 3. GN Name=Arf3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ICR; TISSUE=Brain; RX MEDLINE=97103475; PubMed=8947846; RA Hosaka M., Toda K., Takatsu H., Torii S., Murakami K., Nakayama K.; RT "Structure and intracellular localization of mouse ADP-ribosylation RT factors type 1 to type 6 (ARF1-ARF6)."; RL J. Biochem. 120:813-819(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: GTP-binding protein that functions as an allosteric CC activator of the cholera toxin catalytic subunit, an ADP- CC ribosyltransferase. Involved in protein trafficking; may modulate CC vesicle budding and uncoating within the Golgi apparatus. CC -!- SUBUNIT: Interacts with PRKCABP (By similarity). CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D87900; BAA13492.1; -; mRNA. DR EMBL; BC014778; AAH14778.1; -; mRNA. DR EMBL; BC024935; AAH24935.1; -; mRNA. DR PIR; JC4947; JC4947. DR UniGene; Mm.221298; -. DR UniGene; Mm.393057; -. DR HSSP; P32889; 1RRF. DR SMR; P61205; 2-180. DR Ensembl; ENSMUSG00000051853; Mus musculus. DR KEGG; mmu:11842; -. DR MGI; MGI:99432; Arf3. DR ArrayExpress; P61205; -. DR GermOnline; ENSMUSG00000051853; Mus musculus. DR RZPD-ProtExp; IOM20659; -. DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI. DR GO; GO:0005525; F:GTP binding; TAS:MGI. DR GO; GO:0015031; P:protein transport; TAS:MGI. DR InterPro; IPR006688; ARF. DR InterPro; IPR006689; ARF/SAR. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP_bd. DR PANTHER; PTHR11711; ARF/SAR; 1. DR Pfam; PF00025; Arf; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR PRINTS; PR00328; SAR1GTPBP. DR SMART; SM00177; ARF; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS01019; ARF; 1. KW ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; KW Myristate; Nucleotide-binding; Protein transport; Transport. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 181 ADP-ribosylation factor 3. FT /FTId=PRO_0000207387. FT NP_BIND 24 31 GTP (By similarity). FT NP_BIND 67 71 GTP (By similarity). FT NP_BIND 126 129 GTP (By similarity). FT LIPID 2 2 N-myristoyl glycine (Potential). SQ SEQUENCE 181 AA; 20601 MW; D6FA234DFAED3E5F CRC64; MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK K // ID ARF3_RAT Reviewed; 181 AA. AC P61206; P16587; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 32. DE ADP-ribosylation factor 3 (Liver regeneration-related protein DE LRRG202). GN Name=Arf3; ORFNames=Ac1-253; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX MEDLINE=96408698; PubMed=8813705; RA Price S.R., Nightingale M.S., Tsuchiya M., Moss J., Vaughan M.; RT "Interspecies relationships among ADP-ribosylation factors (ARFs): RT evidence of evolutionary pressure to maintain individual identities."; RL Mol. Cell. Biochem. 159:15-23(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RA Xu C.S., Li W.Q., Li Y.C., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y., RA Yang K.J., Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F., RA Shi J.B., Rahman S., Wang Q.N., Zhang J.B.; RT "Liver regeneration after PH."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: GTP-binding protein that functions as an allosteric CC activator of the cholera toxin catalytic subunit, an ADP- CC ribosyltransferase. Involved in protein trafficking; may modulate CC vesicle budding and uncoating within the Golgi apparatus. CC -!- SUBUNIT: Interacts with PRKCABP (By similarity). CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L12382; AAA40687.1; -; mRNA. DR EMBL; AY325223; AAP92624.1; -; mRNA. DR EMBL; BC088865; AAH88865.1; -; mRNA. DR UniGene; Rn.106440; -. DR HSSP; P32889; 1RRF. DR SMR; P61206; 2-180. DR IntAct; P61206; -. DR Ensembl; ENSRNOG00000033155; Rattus norvegicus. DR KEGG; hsa:377; -. DR KEGG; rno:140940; -. DR RGD; 621273; Arf3. DR ArrayExpress; P61206; -. DR GermOnline; ENSRNOG00000033155; Rattus norvegicus. DR InterPro; IPR006688; ARF. DR InterPro; IPR006689; ARF/SAR. DR InterPro; IPR001806; Ras_trnsfrmng. DR InterPro; IPR005225; Small_GTP_bd. DR PANTHER; PTHR11711; ARF/SAR; 1. DR Pfam; PF00025; Arf; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR PRINTS; PR00328; SAR1GTPBP. DR SMART; SM00177; ARF; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS01019; ARF; 1. KW ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; KW Myristate; Nucleotide-binding; Protein transport; Transport. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 181 ADP-ribosylation factor 3. FT /FTId=PRO_0000207389. FT NP_BIND 24 31 GTP (By similarity). FT NP_BIND 67 71 GTP (By similarity). FT NP_BIND 126 129 GTP (By similarity). FT LIPID 2 2 N-myristoyl glycine (Potential). SQ SEQUENCE 181 AA; 20601 MW; D6FA234DFAED3E5F CRC64; MGNIFGNLLK SLIGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLANQLKNK K // ID CNR1A_FUGRU Reviewed; 468 AA. AC Q98894; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-MAR-2007, entry version 39. DE Cannabinoid receptor type 1A. GN Name=CB1A; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Testis; RX MEDLINE=97001167; PubMed=8812500; DOI=10.1006/geno.1996.0406; RA Yamaguchi F., Macrae A., Brenner S.; RT "Molecular cloning of two cannabinoid type 1-like receptor genes from RT the puffer fish Fugu rubripes."; RL Genomics 35:603-605(1996). CC -!- FUNCTION: Involved in cannabinoid-induced CNS effects (Potential). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X94401; CAA64174.1; -; Genomic_DNA. DR Ensembl; NEWSINFRUG00000135782; Fugu rubripes. DR InterPro; IPR002230; Cnbnoid_rcpt. DR InterPro; IPR000810; Cnoid_rcpt_1. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00522; CANABINOID1R. DR PRINTS; PR00362; CANNABINOIDR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 468 Cannabinoid receptor type 1A. FT /FTId=PRO_0000069320. FT TOPO_DOM 1 115 Extracellular (Potential). FT TRANSMEM 116 141 1 (Potential). FT TOPO_DOM 142 153 Cytoplasmic (Potential). FT TRANSMEM 154 174 2 (Potential). FT TOPO_DOM 175 186 Extracellular (Potential). FT TRANSMEM 187 211 3 (Potential). FT TOPO_DOM 212 231 Cytoplasmic (Potential). FT TRANSMEM 232 254 4 (Potential). FT TOPO_DOM 255 272 Extracellular (Potential). FT TRANSMEM 273 298 5 (Potential). FT TOPO_DOM 299 343 Cytoplasmic (Potential). FT TRANSMEM 344 364 6 (Potential). FT TOPO_DOM 365 376 Extracellular (Potential). FT TRANSMEM 377 398 7 (Potential). FT TOPO_DOM 399 468 Cytoplasmic (Potential). FT CARBOHYD 78 78 N-linked (GlcNAc...) (Potential). FT CARBOHYD 87 87 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 468 AA; 52391 MW; B8628C1B043B42D7 CRC64; MKSVLDGVAD TTFRTITSGL QYLGSNDANY DDPLNDAAFK TGFSLQKPLS AFRSNSFPNK VPADEELIFK GIPFFPTNST DLFGNRNTTR DENSIQCGEN FMDMECFMIL TPSQQLAVAV LSLTLGTFTV LENLVVLCVI FQSRTLRCRP SYHFIGSLAV ADLLGSVIFV YSFLDFHVFH KKDSPNVFLF KLGGVTASFT ASVGSLFLTA IDRYISIHRP LAYRRIVTRT KAVIAFCMMW TISIIIAVLP LLGWNCKRLN SVCSDIFPLI DENYLMFWIG VTSVLVLFII YAYIYILWKA HHHAVRMLSR TSQKSLVVYS AEGTKVQTTR PEQTRMDIRL AKTLVLILAV LVICWGPLLA IMVYDLFWKM DDNIKTVFAF CSMLCLLNST VNPIIYALRS RDLRHAFLSS CHACRGSAQQ LDNSLESDCQ NRNVNISANR AAESCVKTTV KIAKVTMSVS TETSAEAV // ID CNR1B_FUGRU Reviewed; 470 AA. AC Q98895; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-MAR-2007, entry version 39. DE Cannabinoid receptor type 1B. GN Name=CB1B; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Testis; RX MEDLINE=97001167; PubMed=8812500; DOI=10.1006/geno.1996.0406; RA Yamaguchi F., Macrae A., Brenner S.; RT "Molecular cloning of two cannabinoid type 1-like receptor genes from RT the puffer fish Fugu rubripes."; RL Genomics 35:603-605(1996). CC -!- FUNCTION: Involved in cannabinoid-induced CNS effects (Potential). CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X94402; CAA64175.1; -; Genomic_DNA. DR Ensembl; NEWSINFRUG00000147906; Fugu rubripes. DR InterPro; IPR002230; Cnbnoid_rcpt. DR InterPro; IPR000810; Cnoid_rcpt_1. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00522; CANABINOID1R. DR PRINTS; PR00362; CANNABINOIDR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 470 Cannabinoid receptor type 1B. FT /FTId=PRO_0000069321. FT TOPO_DOM 1 113 Extracellular (Potential). FT TRANSMEM 114 139 1 (Potential). FT TOPO_DOM 140 151 Cytoplasmic (Potential). FT TRANSMEM 152 172 2 (Potential). FT TOPO_DOM 173 184 Extracellular (Potential). FT TRANSMEM 185 209 3 (Potential). FT TOPO_DOM 210 229 Cytoplasmic (Potential). FT TRANSMEM 230 252 4 (Potential). FT TOPO_DOM 253 270 Extracellular (Potential). FT TRANSMEM 271 296 5 (Potential). FT TOPO_DOM 297 341 Cytoplasmic (Potential). FT TRANSMEM 342 362 6 (Potential). FT TOPO_DOM 363 374 Extracellular (Potential). FT TRANSMEM 375 396 7 (Potential). FT TOPO_DOM 397 470 Cytoplasmic (Potential). FT CARBOHYD 78 78 N-linked (GlcNAc...) (Potential). FT CARBOHYD 86 86 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 470 AA; 52081 MW; CEE87CD37FDF9192 CRC64; MKLALHRIAG ATMAALTTEV QYLGSNDASY EDPQADAALM KSRFNFEKPY SASSSLHRLI PGNKELIYGG LSTILPTNAS DFPLSNGSGE ATQCGEDIVD NMECFMILTP AQQLVIVILA ITLGTFTVLE NFVVLCVILH SHTLRSRPSY HFIGSLAVAD LIGSIIFVYS FLDFHVLHRK DSPSIFLFKL AGVIASFTAS VGSLFLTAID RYVSIHRPMA YKRIITKTKA VIAFSVMWAI SIEFSLLPLL GWNCKRLHSV CSDIFPLIDE KYLMFWIGMT TVLLLFIIYA YMFILWKSHH HAVRMLSRSS QRSIIVYTSE GTKVQTVRPE QARMDLRLAK TLVLILVALI ICWGPLLAIM VYDLFGRVND FIKTVFAFCS MLCLLNSTIN PVIYAMRSKD LRRAFVNICH MCRGTTQSLD SSAESDWNSR SVRSTGGRAG KDRSVGGKPQ VKVAQVTVSG VTASSPAEAV // ID CO9_FUGRU Reviewed; 586 AA. AC P79755; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 20-MAR-2007, entry version 44. DE Complement component C9 precursor. GN Name=C9; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=98038993; PubMed=9373156; DOI=10.1016/S0378-1119(97)00423-X; RA Yeo G.S.H., Elgar G., Sandford R., Brenner S.; RT "Cloning and sequencing of complement component C9 and its linkage to RT DOC-2 in the pufferfish Fugu rubripes."; RL Gene 200:203-211(1997). CC -!- FUNCTION: C9 is the final component of the complement system to be CC added in the assembly of the membrane attack complex. It is able CC to enter lipid bilayers, forming transmembrane channels (By CC similarity). CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family. CC -!- SIMILARITY: Contains 1 EGF-like domain. CC -!- SIMILARITY: Contains 1 LDL-receptor class A domain. CC -!- SIMILARITY: Contains 1 MACPF domain. CC -!- SIMILARITY: Contains 2 TSP type-1 domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U87241; AAC60288.1; -; Genomic_DNA. DR HSSP; Q07954; 1CR8. DR Ensembl; NEWSINFRUG00000146434; Fugu rubripes. DR InterPro; IPR000742; EGF_3. DR InterPro; IPR013032; EGF_like_reg. DR InterPro; IPR002172; LDL_rcpt_A. DR InterPro; IPR001862; MAC_perforin. DR InterPro; IPR000884; TSP1. DR Pfam; PF00057; Ldl_recept_a; 1. DR Pfam; PF01823; MACPF; 1. DR Pfam; PF00090; TSP_1; 1. DR PRINTS; PR00764; COMPLEMENTC9. DR SMART; SM00192; LDLa; 1. DR SMART; SM00209; TSP1; 1. DR PROSITE; PS00022; EGF_1; 1. DR PROSITE; PS01186; EGF_2; FALSE_NEG. DR PROSITE; PS50026; EGF_3; FALSE_NEG. DR PROSITE; PS01209; LDLRA_1; 1. DR PROSITE; PS50068; LDLRA_2; 1. DR PROSITE; PS00279; MAC_PERFORIN; 1. DR PROSITE; PS50092; TSP1; 2. KW Complement alternate pathway; Complement pathway; Cytolysis; KW EGF-like domain; Glycoprotein; Immune response; Innate immunity; KW Membrane attack complex; Repeat; Signal. FT SIGNAL 1 26 Potential. FT CHAIN 27 586 Complement component C9. FT /FTId=PRO_0000023608. FT DOMAIN 36 89 TSP type-1 1. FT DOMAIN 94 131 LDL-receptor class A. FT DOMAIN 274 487 MACPF. FT DOMAIN 490 524 EGF-like. FT DOMAIN 543 585 TSP type-1 2. FT CARBOHYD 246 246 N-linked (GlcNAc...) (Potential). FT CARBOHYD 274 274 N-linked (GlcNAc...) (Potential). FT CARBOHYD 354 354 N-linked (GlcNAc...) (Potential). FT CARBOHYD 545 545 N-linked (GlcNAc...) (Potential). FT DISULFID 37 72 By similarity. FT DISULFID 48 51 By similarity. FT DISULFID 82 88 By similarity. FT DISULFID 96 108 By similarity. FT DISULFID 103 121 By similarity. FT DISULFID 115 129 By similarity. FT DISULFID 136 175 By similarity. FT DISULFID 363 389 By similarity. FT DISULFID 494 510 By similarity. FT DISULFID 497 512 By similarity. FT DISULFID 514 523 By similarity. SQ SEQUENCE 586 AA; 65198 MW; 8466EB7B8B8FDC18 CRC64; MRTEAALQLG FCALCVMLAL LGEGMGRELP DPPAVNCVWS RWAPWSSCDP CTNTRRRSRG VEVFGQFAGI ACQGSVGDRE YCITNAKCNL PPPRECSDSE FQCESGSCIK LRLKCNGDYD CEDGSDEDCE PLRKTCPPTV LDTNEQGRTA GYGINILGAD PRMNPFNNDF FNGRCDKVRN PNTLQLDRLP WNIGVLNYQT LVEETASREI YEDSYSLLRE MLKEMSIKVD AGLSFKFKST EPSMSNNSLK LDASLEYEKK TMIKDVSELT NIKNKSFMRV KGRLQLSTYR MRSHQLQVAD EFVAHVKSLP LEYEKGIYYA FLEDYGTHYT KNGKSGGEYE LVYVLNQDTI KAKNLTERKI QECLKIGIEA EFATTSVQDG KAHAKLNKCD DVTTKSQGDV EGKAVVDNVM TSVKGGSLES AVTMRAKLNK EGVMDIATYQ NWARTIASAP ALINSEPEPI YMLIPTDIPG ANSRIANLKQ ATADYVAEYN VCKCRPCHNG GTLALLDGKC ICMCSNLFEG LGCQNFKGDK ARVPAARPAV TQEGNWSCWS SWSNCQGQKR SRTRYCNTEG VLGAECRGEI RSEEYC // ID DRD1L_FUGRU Reviewed; 459 AA. AC P53452; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-MAR-2007, entry version 37. DE D(1)-like dopamine receptor. GN Name=D14; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=95309911; PubMed=7789977; DOI=10.1016/0888-7543(95)80044-M; RA Machae A.D., Brenner S.; RT "Analysis of the dopamine receptor family in the compact genome of the RT puffer fish Fugu rubripes."; RL Genomics 25:436-446(1995). CC -!- FUNCTION: Receptor for dopamine. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X80174; CAA56455.1; -; Genomic_DNA. DR PIR; A56849; A56849. DR HSSP; P08913; 1HLL. DR Ensembl; NEWSINFRUG00000145469; Fugu rubripes. DR InterPro; IPR001413; Dopa1A_rcpt. DR InterPro; IPR000929; Dopamine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00565; DOPAMINED1AR. DR PRINTS; PR00242; DOPAMINER. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 459 D(1)-like dopamine receptor. FT /FTId=PRO_0000069382. FT TOPO_DOM 1 23 Extracellular (Potential). FT TRANSMEM 24 49 1 (Potential). FT TOPO_DOM 50 60 Cytoplasmic (Potential). FT TRANSMEM 61 87 2 (Potential). FT TOPO_DOM 88 96 Extracellular (Potential). FT TRANSMEM 97 119 3 (Potential). FT TOPO_DOM 120 138 Cytoplasmic (Potential). FT TRANSMEM 139 164 4 (Potential). FT TOPO_DOM 165 191 Extracellular (Potential). FT TRANSMEM 192 216 5 (Potential). FT TOPO_DOM 217 269 Cytoplasmic (Potential). FT TRANSMEM 270 297 6 (Potential). FT TOPO_DOM 298 311 Extracellular (Potential). FT TRANSMEM 312 333 7 (Potential). FT TOPO_DOM 334 459 Cytoplasmic (Potential). FT CARBOHYD 4 4 N-linked (GlcNAc...) (Potential). FT DISULFID 96 187 By similarity. SQ SEQUENCE 459 AA; 51080 MW; B69857A3A4E4E10B CRC64; MAQNFSTVGD GKQMLLERDS SKRVLTGCFL SLLIFTTLLG NTLVCVAVTK FRHLRSKVTN FFVISLAISD LLVAILVMPW KAATEIMGFW PFGEFCNIWV AFDIMCSTAS ILNLCVISVD RYWAISSPFR YERKMTPKVA CLMISVAWTL SVLISFIPVQ LNWHKAQTAS YVELNGTYAG DLPPDNCDSS LNRTYAISSS LISFYIPVAI MIVTYTRIYR IAQKQIRRIS ALERAAESAQ NRHSSMGNSL SMESECSFKM SFKRETKVLK TLSVIMGVFV CCWLPFFILN CMVPFCEADD TTDFPCISST TFDVFVWFGW ANSSLNPIIY AFNADFRKAF SILLGCHRLC PGNSAIEIVS INNTGAPLSN PSCQYQPKSH IPKEGNHSSS YVIPHSILCQ EEELQKKDGF GGEMEVGLVN NAMEKVSPAI SGNFDSDAAV TLETINPITQ NGQHKSMSC // ID DRD2L_FUGRU Reviewed; 463 AA. AC P53453; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-MAR-2007, entry version 34. DE D(2)-like dopamine receptor. GN Name=D215; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=95309911; PubMed=7789977; DOI=10.1016/0888-7543(95)80044-M; RA Machae A.D., Brenner S.; RT "Analysis of the dopamine receptor family in the compact genome of the RT puffer fish Fugu rubripes."; RL Genomics 25:436-446(1995). CC -!- FUNCTION: Receptor for dopamine. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X80175; CAA56456.1; -; Genomic_DNA. DR HSSP; P08913; 1HLL. DR InterPro; IPR001922; Dopa_D2_rcpt. DR InterPro; IPR000929; Dopamine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00567; DOPAMINED2R. DR PRINTS; PR00242; DOPAMINER. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 463 D(2)-like dopamine receptor. FT /FTId=PRO_0000069392. FT TOPO_DOM 1 35 Extracellular (Potential). FT TRANSMEM 36 58 1 (Potential). FT TOPO_DOM 59 69 Cytoplasmic (Potential). FT TRANSMEM 70 95 2 (Potential). FT TOPO_DOM 96 106 Extracellular (Potential). FT TRANSMEM 107 128 3 (Potential). FT TOPO_DOM 129 149 Cytoplasmic (Potential). FT TRANSMEM 150 172 4 (Potential). FT TOPO_DOM 173 187 Extracellular (Potential). FT TRANSMEM 188 211 5 (Potential). FT TOPO_DOM 212 392 Cytoplasmic (Potential). FT TRANSMEM 393 416 6 (Potential). FT TOPO_DOM 417 425 Extracellular (Potential). FT TRANSMEM 426 449 7 (Potential). FT TOPO_DOM 450 463 Cytoplasmic (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT CARBOHYD 16 16 N-linked (GlcNAc...) (Potential). FT CARBOHYD 22 22 N-linked (GlcNAc...) (Potential). FT DISULFID 105 183 By similarity. SQ SEQUENCE 463 AA; 52120 MW; A54B178D7718AF6B CRC64; MDVFTQYAYN DSIFDNGTWS ANETTKDETH PYNYYAMLLT LLIFVIVFGN VLVCMAVSRE KALQTTTNYL IVSLAVADLL VATLVMPWVV YLEVVGEWRF SKIHCDIFVT LDVMMCTASI LNLCAISIDR YTAVAMPMLY NTRYSSRRRV TVMISVVWVL SFAISCPLLF GLNNTATRDQ SLCFIANPAF VVYSSIVSFY VPFIVTLLVY VQIYVVLRKR RKRVNTKPKQ RLCQAADPDI PTSLKDKCTH PEDVRLCTMI VKSNGSFPVN KKKVIFIKDG VNEVEGLELD ELNYCGGSHK QPPPQQQPRA LGDTPATSHQ LLMSTKANAS PTSTPPTPPE EGQRTEKNGD PTKEAQGNPA PVVALRNGKT QTSLKTLSKR KISQQKEKKA TQMLAIVLGV FIICWLPFFI THILNTHCTR CKVPAEMYNA FTWLGYVNSA VNPIIYTTFN VEFRKAFIKI LHC // ID DRD5L_FUGRU Reviewed; 463 AA. AC P53454; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-MAR-2007, entry version 36. DE D(5)-like dopamine receptor. GN Name=DL; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=95309911; PubMed=7789977; DOI=10.1016/0888-7543(95)80044-M; RA Machae A.D., Brenner S.; RT "Analysis of the dopamine receptor family in the compact genome of the RT puffer fish Fugu rubripes."; RL Genomics 25:436-446(1995). CC -!- FUNCTION: Receptor for dopamine. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X80177; CAA56457.1; -; Genomic_DNA. DR PIR; B56849; B56849. DR HSSP; P08913; 1HLL. DR Ensembl; NEWSINFRUG00000140201; Fugu rubripes. DR InterPro; IPR000929; Dopamine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00242; DOPAMINER. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 463 D(5)-like dopamine receptor. FT /FTId=PRO_0000069409. FT TOPO_DOM 1 39 Extracellular (Potential). FT TRANSMEM 40 65 1 (Potential). FT TOPO_DOM 66 76 Cytoplasmic (Potential). FT TRANSMEM 77 103 2 (Potential). FT TOPO_DOM 104 112 Extracellular (Potential). FT TRANSMEM 113 135 3 (Potential). FT TOPO_DOM 136 154 Cytoplasmic (Potential). FT TRANSMEM 155 180 4 (Potential). FT TOPO_DOM 181 198 Extracellular (Potential). FT TRANSMEM 199 223 5 (Potential). FT TOPO_DOM 224 273 Cytoplasmic (Potential). FT TRANSMEM 274 301 6 (Potential). FT TOPO_DOM 302 315 Extracellular (Potential). FT TRANSMEM 316 337 7 (Potential). FT TOPO_DOM 338 463 Cytoplasmic (Potential). FT CARBOHYD 6 6 N-linked (GlcNAc...) (Potential). FT DISULFID 112 194 By similarity. SQ SEQUENCE 463 AA; 51096 MW; 7FD627F69A699F6B CRC64; MENFYNETEP TEPRGGVDPL RVVTAAEDVP APVGGVSVRA LTGCVLCALI VSTLLGNTLV CAAVIKFRHL RSKVTNAFVV SLAVSDLFVA VLVMPWRAVS EVAGVWLFGR FCDTWVAFDI MCSTASILNL CVISMDRYWA ISNPFRYERR MTRRFAFLMI AVAWTLSVLI SFIPVQLNWH RADNNSSAHE QGDCNASLNR TYAISSSLIS FYIPVLIMVG TYTRIFRIAQ TQIRRISSLE RAAGQRAQNQ SHRASTHDES ALKTSFKRET KVLKTLSVIM GVFVFCWLPF FVLNCVVPFC DVDKVGEPPC VSDTTFNIFV WFGWANSSLN PVIYAFNADF RKAFTTILGC SKFCSSSAVQ AVDFSNELVS YHHDTTLQKE PVPGPGAHRL VAPLPQNRGD AGPNFDKVSV VSDDSRADRN LLLPAILQCD CEAEISLDMV PFGSSGPADS FLIPGQIQDL GDL // ID EI2BB_FUGRU Reviewed; 355 AA. AC Q90511; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-MAR-2007, entry version 27. DE Translation initiation factor eIF-2B subunit beta (eIF-2B GDP-GTP DE exchange factor subunit beta) (S20I15). GN Name=EIF2B2; Synonyms=EIF2BB; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96202283; PubMed=8643637; DOI=10.1073/pnas.93.4.1366; RA Trower M.K., Orton S.M., Purvis I.J., Sanseau P., Riley J., RA Christodoulou C., Burt D., See C.G., Elgar G., Sherrington R., RA Rogaev E.I., St George-Hyslop P.H., Brenner S., Dykes C.W.; RT "Conservation of synteny between the genome of the pufferfish (Fugu RT rubripes) and the region on human chromosome 14 (14q24.3) associated RT with familial Alzheimer disease (AD3 locus)."; RL Proc. Natl. Acad. Sci. U.S.A. 93:1366-1369(1996). CC -!- FUNCTION: Catalyzes the exchange of eukaryotic initiation factor CC 2-bound GDP for GTP (By similarity). CC -!- SUBUNIT: Complex of five different subunits; alpha, beta, gamma, CC delta and epsilon (By similarity). CC -!- SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U40756; AAC59777.1; -; Genomic_DNA. DR Ensembl; NEWSINFRUG00000126267; Fugu rubripes. DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B...; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB. DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB. DR GO; GO:0005515; F:protein binding; ISS:UniProtKB. DR GO; GO:0051716; P:cellular response to stimulus; ISS:UniProtKB. DR GO; GO:0042552; P:myelination; ISS:UniProtKB. DR GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB. DR GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB. DR GO; GO:0006413; P:translational initiation; ISS:UniProtKB. DR InterPro; IPR000649; IF-2B_related. DR PANTHER; PTHR10233; IF-2B; 1. DR Pfam; PF01008; IF-2B; 1. KW Initiation factor; Protein biosynthesis. FT CHAIN 1 355 Translation initiation factor eIF-2B FT subunit beta. FT /FTId=PRO_0000156065. SQ SEQUENCE 355 AA; 39130 MW; 4375743877F6B132 CRC64; MPGADKEVDL TERIEAFLSD LKRGGSGTGP LRGSSETARE TTALLRRITA QARWSSAGDL MEIIRKEGRR LIAAQPSETT VGNMIRRVLK IIREEYARSR GSSEEADQQE SLHKLLTSGG LSEENFRQHF AALRANVIEA INELLTELEG TTDNIAMQAL EHIHSNEVIM TVGRSRTVEA FLKDAARKRK FHVIVAECAP FCQGHKMATS LSTAGIETTV IADAAIFAVM SRVNKVIIGT QTVLANGGLR AVNGTHTLAL AAKHHSTPLI VCAPMFKLSP QFPNEEDTFH KFVSPHEVLP FTEGEILSKV NVHCPVFDYV PPELITLFIS NIGGHAPSYI YRLMSELYHP EDHEL // ID EM55_FUGRU Reviewed; 467 AA. AC P49697; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 20-MAR-2007, entry version 45. DE 55 kDa erythrocyte membrane protein (p55) (Membrane protein, DE palmitoylated 1). GN Name=MPP1; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Testis; RX MEDLINE=96047329; PubMed=7558025; DOI=10.1006/geno.1995.1075; RA Elgar G.S., Rattray F.M., Greystrong J.S., Brenner S.; RT "Genomic structure and nucleotide sequence of the p55 gene of the RT puffer fish Fugu rubripes."; RL Genomics 27:442-446(1995). CC -!- SUBCELLULAR LOCATION: Membrane; peripheral membrane protein (By CC similarity). CC -!- PTM: Extensively palmitoylated (By similarity). CC -!- SIMILARITY: Belongs to the MAGUK family. CC -!- SIMILARITY: Contains 1 guanylate kinase-like domain. CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X81359; CAA57127.1; -; Genomic_DNA. DR PIR; A57627; A57627. DR HSSP; O14936; 1KGD. DR Ensembl; NEWSINFRUG00000131184; Fugu rubripes. DR InterPro; IPR008144; Guanylate_kin. DR InterPro; IPR008145; Guanylt/Ca. DR InterPro; IPR001478; PDZ. DR InterPro; IPR001452; SH3. DR InterPro; IPR011511; SH3_2. DR Pfam; PF00625; Guanylate_kin; 1. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF07653; SH3_2; 1. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD000066; SH3; 1. DR SMART; SM00072; GuKc; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00326; SH3; 1. DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS50106; PDZ; 1. DR PROSITE; PS50002; SH3; 1. KW Lipoprotein; Membrane; Palmitate; SH3 domain. FT CHAIN 1 467 55 kDa erythrocyte membrane protein. FT /FTId=PRO_0000094567. FT DOMAIN 73 154 PDZ. FT DOMAIN 160 230 SH3. FT DOMAIN 283 452 Guanylate kinase-like. SQ SEQUENCE 467 AA; 52609 MW; 48BA1CE3ED524EDC CRC64; MTLKSNKNEP ALILDSVTSV RTALSDLYLE QLLQNKPTDK QAAMQTYENK GAEVFSNGSA GHINGAELSR MREVAFEKNQ SEPLGVTLKL NDKQRCSVAR ILHGGMIHRQ GSLHEGDEIA EINGKSVANQ TVDQLQKILK ETNGVVTMKI IPRPQSRSKP CEMYMRGQFD YDPAMDDLIP CKEAGLKFQT GDIIQIINKQ DPNWWQGRVE NNAANFAGLI PSPELQEWRA ASKSKAREGS QSCSPFGKKK KCKDKYLAKH SSIFDQLDVI SYEEVVRLPA FKRKTLVLIG APGVGRRHIK NVLLTKYPEK FSYPVPHTTR PQRKGDANGE EYFFISNEAM TKCISANELL EYGSFQGYMF GTITETIQKI HEQDKIALLD VEPQTMKVLR TADFGPLMVF IAPTDTAAQT ENLQMIQKES ETILNTYRQY FDVVLVNNDV NESVKIVEEA LEHATTTPQW VPVSWVY // ID FOS_FUGRU Reviewed; 376 AA. AC P53450; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-MAR-2007, entry version 37. DE Proto-oncogene protein c-fos (Cellular oncogene fos). GN Name=FOS; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96202283; PubMed=8643637; DOI=10.1073/pnas.93.4.1366; RA Trower M.K., Orton S.M., Purvis I.J., Sanseau P., Riley J., RA Christodoulou C., Burt D., See C.G., Elgar G., Sherrington R., RA Rogaev E.I., St George-Hyslop P.H., Brenner S., Dykes C.W.; RT "Conservation of synteny between the genome of the pufferfish (Fugu RT rubripes) and the region on human chromosome 14 (14q24.3) associated RT with familial Alzheimer disease (AD3 locus)."; RL Proc. Natl. Acad. Sci. U.S.A. 93:1366-1369(1996). CC -!- FUNCTION: Nuclear phosphoprotein which forms a tight but non- CC covalently linked complex with the JUN/AP-1 transcription factor. CC C-fos has a critical function in regulating the development of CC cells destined to form and maintain the skeleton. It is thought to CC have an important role in signal transduction, cell proliferation CC and differentiation (By similarity). CC -!- SUBUNIT: Heterodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the bZIP family. Fos subfamily. CC -!- SIMILARITY: Contains 1 bZIP domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U40757; AAC59778.1; -; Genomic_DNA. DR HSSP; P01100; 1FOS. DR SMR; P53450; 123-182. DR TRANSFAC; T02205; -. DR Ensembl; NEWSINFRUG00000132419; Fugu rubripes. DR InterPro; IPR011700; bZIP_2. DR InterPro; IPR008917; Euk_TF_DNA_bd. DR InterPro; IPR000837; Leuzip_Fos. DR InterPro; IPR004827; TF_bZIP. DR Pfam; PF07716; bZIP_2; 1. DR PRINTS; PR00042; LEUZIPPRFOS. DR SMART; SM00338; BRLZ; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. KW DNA-binding; Nuclear protein; Phosphorylation; Proto-oncogene. FT CHAIN 1 376 Proto-oncogene protein c-fos. FT /FTId=PRO_0000076473. FT DOMAIN 149 177 Leucine-zipper. FT DNA_BIND 123 144 Basic motif. SQ SEQUENCE 376 AA; 40826 MW; BFC28534431DB491 CRC64; MMFTSFNAEC DSSSRCSASP VGDNLYYPSP AGSYSSMGSP QSQDFTDLTA SSASFIPTVT AISTSPDLQW MVQPLISSVA PSHRAHPYSP SPSYKRTVMR SAASKAHGKR SRVEQTTPEE EEKKRIRRER NKQAAAKCRN RRRELTDTLQ AETDQLEDEK SSLQNDIANL LKEKERLEFI LAAHQPICKI PSQMDTDFSV VSMSPVHACL STTVSTQLQT SIPEATTVTS SHSTFTSTSN SIFSGSSDSL LSTATVSNSV VKMTDLDSSV LEESLDLLAK TEAETARSVP DVNLSNSLFA AQDWEPLHAT ISSSDFEPLC TPVVTCTPAC TTLTSSFVFT FPEAETFPTC GVAHRRRSNS NDQSSDSLSS PTLLAL // ID G6PD_FUGRU Reviewed; 530 AA. AC P54996; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 03-APR-2007, entry version 44. DE Glucose-6-phosphate 1-dehydrogenase (EC 1.1.1.49) (G6PD). GN Name=G6PD; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=95331796; PubMed=7607684; DOI=10.1016/0888-7543(95)80179-P; RA Mason P.J., Stevens D.J., Luzzatto L., Brenner S., Aparicio S.; RT "Genomic structure and sequence of the Fugu rubripes glucose-6- RT phosphate dehydrogenase gene (G6PD)."; RL Genomics 26:587-591(1995). CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate + NADP(+) = D-glucono- CC 1,5-lactone 6-phosphate + NADPH. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): CC step 1/3. CC -!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X83611; CAA58590.2; -; Genomic_DNA. DR PIR; A56841; A56841. DR HSSP; P11413; 1QKI. DR SMR; P54996; 43-530. DR Ensembl; NEWSINFRUG00000135749; Fugu rubripes. DR InterPro; IPR001282; G6PDH. DR Pfam; PF02781; G6PD_C; 1. DR Pfam; PF00479; G6PD_N; 1. DR PIRSF; PIRSF000110; G6PD; 1. DR PRINTS; PR00079; G6PDHDRGNASE. DR ProDom; PD001129; G6PD; 1. DR TIGRFAMs; TIGR00871; zwf; 1. DR PROSITE; PS00069; G6P_DEHYDROGENASE; 1. KW Carbohydrate metabolism; Glucose metabolism; NADP; Oxidoreductase. FT CHAIN 1 530 Glucose-6-phosphate 1-dehydrogenase. FT /FTId=PRO_0000068088. FT ACT_SITE 278 278 Proton acceptor (By similarity). FT BINDING 55 55 NADP (By similarity). FT BINDING 87 87 NADP (By similarity). FT BINDING 216 216 Substrate (By similarity). FT BINDING 220 220 Substrate (By similarity). SQ SEQUENCE 530 AA; 60469 MW; FC73FB53D834EF29 CRC64; MMIILFNCFF CASFREDGQH PTVSLGGVWG AAKELHEDKE FHQSDVHVFI IMGASGDLAK KKIYPTLWWL FRDGLLPEQT YFVGFARSAL TVDAIRTSCM PYLKVTETES DRLSAFFSRN SYISGNYTAG GSFSELNAHI MSLPGASDAN RLFYLALPPT IYHSVTENIK HFCMSAKGWN RVIVEKPFGH DLQSSEELST HLSSLFTEDQ IYRIDHYLGK EMVQNLMVLR FGNRIFGPIW NRDNVACVVL TFKEPFGTQG RGGYFDDFGI IRDVMQNHML QMLCLVAMEK PASTNSDDVR DEKVKVLKCI VPASMSDVVL GQYVGDPEGE GDAKLGYLDD PTVPKGSTQA TFATVVLYVH NERWDGVPFI LRCGKALNER KAEVRLQFTD VPGDIFRNQC YRNELVVRVQ PNEAIYAKMM SKKPGVYFTP EETELDLTYK SRYKDVKLPD AYERLILDVF CGSQMHFVAS DELREAWRIF TPLLHQIEKE KPKPIPYKYG SRGPAEADEL EKRVGFRYEG TYKWVNPHRL // ID HD_FUGRU Reviewed; 3148 AA. AC P51112; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-MAR-2007, entry version 34. DE Huntingtin (Huntington disease protein homolog) (HD protein). GN Name=HD; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=95375788; PubMed=7647794; DOI=10.1038/ng0595-67; RA Baxendale S., Abdulla S., Elgar G., Buck D., Berks M., Micklem G., RA Durbin R., Bates G., Brenner S., Beck S., Lehrach H.; RT "Comparative sequence analysis of the human and pufferfish RT Huntington's disease genes."; RL Nat. Genet. 10:67-76(1995). CC -!- FUNCTION: May play a role in microtubule-mediated transport or CC vesicle function. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- POLYMORPHISM: The poly-Gln region (four residues) does not appear CC to be polymorphic, explaining the absence of a HD-like disorder. CC -!- SIMILARITY: Belongs to the hungtintin family. CC -!- SIMILARITY: Contains 10 HEAT repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X82939; CAA58112.1; -; Genomic_DNA. DR Ensembl; NEWSINFRUG00000144943; Fugu rubripes. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR000357; HEAT. DR InterPro; IPR000091; Huntingtin. DR InterPro; IPR002885; PPR. DR Gene3D; G3DSA:1.25.10.10; ARM-like; 1. DR Pfam; PF02985; HEAT; 4. DR PRINTS; PR00375; HUNTINGTIN. DR TIGRFAMs; TIGR00756; PPR; 1. DR PROSITE; PS50077; HEAT_REPEAT; 1. KW Nuclear protein; Repeat. FT CHAIN 1 3148 Huntingtin. FT /FTId=PRO_0000083941. FT REPEAT 149 186 HEAT 1. FT REPEAT 191 228 HEAT 2. FT REPEAT 760 797 HEAT 3. FT REPEAT 861 898 HEAT 4. FT REPEAT 1419 1456 HEAT 5. FT MOTIF 2398 2407 Nuclear export signal (By similarity). FT COMPBIAS 18 21 Poly-Gln. FT COMPBIAS 679 682 Poly-Ala. FT COMPBIAS 1104 1108 Poly-Ser. SQ SEQUENCE 3148 AA; 348937 MW; D9358676B0345243 CRC64; MATMEKLMKA FESLKSFQQQ QGPPTAEEIV QRQKKEQATT KKDRVSHCLT ICENIVAQSL RTSPEFQKLL GIAMEMFLLC SDDSESDVRM VADECLNRII KALMDSNLPR LQLELYKEIK KNGASRSLRA ALWRFAELAH LIRPQKCRPY LVNLLPCLTR ITKRQEETIQ ETLAAAMPKI MAALGHFAND GEIKMLLKSF VANLKSSSPT IRRTAASSAV SVCQHSRRTS YFYTWLLNVL LGLLVPVDEE HHSHLILGVL LTLRYLMPLL QQQVNTISLK GSFGVMQKEA DVQPAPEQLL QVYELTLHYT QHWDHNVVTA ALELLQQTLR TPPPELLHVL ITAGSIQHAS VFRQDIESRA RSGSILELIA GGGSTCSPLL HRKHRGKMLS GEEDALEDDP EKTDVTTGYF TAVGADNSSA AQVDIITQQP RSSQHTIQPG DSVDLSASSE QGGRGGGASA SDTPESPNDE EDMLSRSSSC GANITPETVE DATPENPAQE GRPVGGSGAY DHSLPPSDSS QTTTEGPDSA VTPSDVAELV LDGSESQYSG MQIGTLQDEE DEGTATSSQE DPPDPFLRSA LALSKPHLFE SRGHNRQGSD SSVDRFIPKD EPPEPEPDNK MSRIKGAIGH YTDRGAEPVV HCVRLLSASF LLTGQKNGLT PDRDVRVSVK ALAVSCVGAA AALHPEAFFN SLYLEPLDGL RAEEQQYISD VLGFIDHGDP QIRGATAILC AAIIQAALSK MRYNIHSWLA SVQSKTGNPL SLVDLVPLLQ KALKDESSVT CKMACSAVRH CIMSLCGSTL SELGLRLVVD LFALKDSSYW LVRTELLETL AEMDFRLVNF LERKSEALHK GEHHYTGRLR LQERVLNDVV IQLLGDDDPR VRHVAASAVS RLVSRLFFDC DQGQADPVVA IARDQSSVYL QLLMHETQPP SQLTVSTITR TYRGFNLSNN VADVTVENNL SRVVTAVSHA FTSSTSRALT FGCCEALCLL AVHFPICTWT TGWHCGHISS QSSFSSRVGR SRGRTLSVSQ SGSTPASSTT SSAVDPERRT LTVGTANMVL SLLSSAWFPL DLSAHQDALL LCGNLLAAVA PKCLRNPWAG EDDSSSSSTN TSGGTHKMEE PWAALSDRAF VAMVEQLFSH LLKVLNICAH VLDDTPPGPP VKATLPSLTN TPSLSPIRRK GKDKDAVDSS SAPLSPKKGN EANTGRPTES TGSTAVHKST TLGSFYHLPP YLKLYDVLKA THANFKVMLD LHSNQEKFGS FLRAALDVLS QLLELATLND INKCVEEILG YLKSCFSREP TMATVCVQQL LKTLFGTNLA SQYEGFLSGP SRSQGKALRL GSSSLRPGLY HYCFMAPYTH FTQALADASL RNMVQAEHEQ DTSGWFDVMQ KTSNQLRSNI ANAARHRGDK NAIHNHIRLF EPLVIKALKQ YTTSTSVALQ RQVLDLLAQL VQLRVNYCLL DSDQVFIGFV LKQFEYIEVG QFRDSEAIIP NIFFFLVLLS YERYHSKQII SIPKIIQLCD GIMASGRKAV THAIPALQPI VHDLFVLRGS NKADAGKELE TQKEVVVSML LRLVQYHQVL EMFILVLQQC HKENEDKWKR LSRQIADVIL PMIAKQQMHL DSPEALGVLN TLFETVAPSS LRPVDMLLKS MFTTPVTMAS VATVQLWVSG ILAVLRVLVS QSTEDIVLSR IHELSLSPHL LSCHTIKRLQ QPNLSPSDQP AGDGQQNQEP NGEAQKSLPE ETFARFLIQL VGVLLDDISS RHVKVDITEQ QHTFYCQQLG TLLMCLIHVF KSGMFRRITV AASRLLKGES GSGHSGIEFY PLEGLNSMVH CLITTHPSLV LLWCQVLLII DYTNYSWWTE VHQTPKGHSL SCTKLLSPHS SGEGEEKPET RLAMINREIV RRGALILFCD YVCQNLHDSE HLTWLIVNHV RDLIDLSHEP PVQDFISAVH RNSAASGLFI QAIQSRCDNL NSPTMLKKTL QCLEGIHLSQ SGSLLMLYVD KLLSTPFRVL ARMVDTLACR RVEMLLAETL QNSVAQLPLE ELHRIQEYLQ TSGLAQRHQR FYSLLDRFRA TVSDTSSPST PVTSHPLDGD PPPAPELVIA DKEWYVALVK SQCCLHGDVS LLETTELLTK LPPADLLSVM SCKEFNLSLL CPCLSLGVQR LLRGQGSLLL ETALQVTLEQ LAGATGLLPV PHHSFIPTSH PQSHWKQLAE VYGDPGFYSR VLSLCRALSQ YLLTVKQLPS SLRIPSDKEH LITTFTCAAT EVVVWHLLQD QLPLSVDLQW ALSCLCLALQ QPCVWNKLST PEYNTHTCSL IYCLHHIILA VAVSPGDQLL HPERKKTKAL RHSDDEDQVD SVHDNHTLEW QACEIMAELV EGLQSVLSLG HHRNTAFPAF LTPTLRNIII SLSRLPLVNS HTRVPPLVWK LGWSPQPGGE FGTTLPEIPV DFLQEKDVFR EFLYRINTLG WSNRTQFEET WATLLGVLVT QPITMDQEEE TQQEEDLERT QLNVLAVQAI TSLVLSAMTL PTAGNPAVSC LEQQPRNKSL KALETRFGRK LAVIRGEVER EIQALVSKRD NVHTYHPYHA WDPVPSLSAA SPGTLISHEK LLLQINTERE LGNMDYKLGQ VSIHSVWLGN NITPLREEEW GEDEDDEADP PAPTSPPLSP INSRKHRAGV DIHSCSQFLL ELYSQWVIPG SPSNRKTPTI LISEVVRSLL AVSDLFTERN QFDMMFSTLM ELQKLHPPED EILNQYLVPA ICKAAAVLGM DKAIAEPVCR LLETTLRSTH LPSRMGALHG VLYVLECDLL DDTAKQLIPT VSEYLLSNLR AIAHCVNLHN QQHVLVMCAV AFYMMENYPL DVGTEFMAGI IQLCGVMVSA SEDSTPSIIY HCVLRGLERL LLSEQLSRVD GEALVKLSVD RVNMPSPHRA MAALGLMLTC MYTGKEKASP AARSAHSDPQ VPDSESIIVA MERVSVLFDR IRKGLPSEAR VVARILPQFL DDFFPPQDIM NKVIGEFLSN QQPYPQFMAT VVYKVFQTLH ATGQSSMVRD WVLLSLSNFT QRTPVAMAMW SLSCFFVSAS TSQWISALLP HVISRMGSSD VVDVNLFCLV AMDFYRHQID EELDRRAFQS VFETVASPGS PYFQLLACLQ SIHQDKSL // ID HIRA_FUGRU Reviewed; 1025 AA. AC O42611; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 20-MAR-2007, entry version 40. DE HIRA protein (TUP1-like enhancer of split protein 1). GN Name=HIRA; Synonyms=TUPLE1; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX MEDLINE=98201624; PubMed=9524281; DOI=10.1016/S0378-1119(98)00010-9; RA Llevadot R., Estivill X., Scambler P., Pritchard M.; RT "Isolation and genomic characterization of the TUPLE1/HIRA gene of the RT pufferfish Fugu rubripes."; RL Gene 208:279-283(1998). CC -!- FUNCTION: Could have a part in mechanisms of transcriptional CC regulation similar to that played by yeast HIR1 and HIR2 together. CC -!- SUBCELLULAR LOCATION: Nucleus (Potential). CC -!- SIMILARITY: Belongs to the WD repeat HIR1 family. CC -!- SIMILARITY: Contains 4 WD repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U94325; AAC60370.1; -; Genomic_DNA. DR EMBL; U94324; AAC60369.1; -; mRNA. DR UniGene; Tru.1844; -. DR HSSP; P16649; 1ERJ. DR Ensembl; NEWSINFRUG00000154061; Fugu rubripes. DR InterPro; IPR011494; Hira. DR InterPro; IPR001680; WD40. DR Pfam; PF07569; Hira; 1. DR Pfam; PF00400; WD40; 4. DR PRINTS; PR00320; GPROTEINBRPT. DR ProDom; PD000018; WD40; 3. DR SMART; SM00320; WD40; 8. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 3. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. KW Nuclear protein; Repeat; Transcription; Transcription regulation; KW WD repeat. FT CHAIN 1 1025 HIRA protein. FT /FTId=PRO_0000051021. FT REPEAT 68 98 WD 1. FT REPEAT 129 159 WD 2. FT REPEAT 172 202 WD 3. FT REPEAT 266 313 WD 4. FT COMPBIAS 673 682 Poly-Ala. FT COMPBIAS 685 688 Poly-Ala. SQ SEQUENCE 1025 AA; 111857 MW; A4212152D75B6A37 CRC64; MKLLKPSWVS HNGKPIFSVD IHPDGTKFAT GGQGEDSGKV MIWNMAPVLK EEDEKNENVP KMLCQMDNHL ACVNCVRWSN NGLYLASGGD DKLVMVWKRA ALIGPSTVFG SSNKLANVEQ WRCVTILRNH TGDVMDVSWS PHDVWLASCS VDNTIVIWNA RKFPEMVTCL RGHTGLVKGL TWDPVGKYIA SQADDHSLRV WRTVDWQMEA NITKPFSECG GTTHVLRLSW SPDGQYLVSA HAMNNSGPTA QIVERDGWRT NMDFVGHRKA VTVVKFNPKI FKKKQKNGGS PKPSCPYCCC AVGSKDRSLS VWLTSLKRPL VVIHDLFDKS IMDISWTLTG LGMLVCSMDG TVAYLDFSLD ELGDPLSEEE KNSIHQNIYG KSLAITNTEP QLSTTIIENP EMLKYQQERR NSTQANSGPG ATGSESATPK LNSVMNGESL EDIRKNLLKK QVETRTPDGR RRITPLCIAQ LDTGDFSPAL FNSAPILPSG SSMSNQLTSQ LSSDSSPGQA PPLGLRPSQD PMLISPPPSS AAKVLEDNKD GVKSCLLLTS ASKIEPMKAL DSRFTERSKA TPGATAAIAS STGLTPSERP KESTPMQKDV KSKEDTSSDS EDKMATINKN LAFNKRKPEL LMDGAEVVEK RKKGRPRKDK MAASIAQPLT QTTSPAEREP SRAAAAGAGA AAPTAAAALK LPTPSIKKAF TLQVSMDPSV VLEVENEVSV VAGSRLSQLR CSRDGRDWNT LLPSSVLTAA GSSDVVAVAS QDRMLSVFSS CGRRLLPAIQ LATPASALHC SAHFVMVLTS GATLSVWDVH KQKALVKNES LLTILSGAAV TVSQSMLTQQ GVPVVGLSNG KSYCFSLSLE TWTLIADTAD SLVQCADFRN CLPNQDAPMS SGPLAAMQGR NFNAGRLASR LSSTPHHLQQ SMTLAFLENQ LASALTLQSA QEYRYWLLIY ARFLVNEGSE YRLRELCKEL LGPVHKSATT SWEPTTLGLR KRDLLREVLP VVGENLRFQR LFTEYQDQLE LLRNK // ID RS24_FUGRU Reviewed; 132 AA. AC O42387; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 20-MAR-2007, entry version 25. DE 40S ribosomal protein S24. GN Name=RPS24; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Crosio C., Cecconi F., Giorgi M., Amaldi F., Mariottini P.; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the ribosomal protein S24e family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ001398; CAA04728.1; -; Genomic_DNA. DR Ensembl; NEWSINFRUG00000143641; Fugu rubripes. DR LinkHub; O42387; -. DR InterPro; IPR001976; Ribosomal_S24E. DR PANTHER; PTHR10496; Ribosomal_S24E; 1. DR Pfam; PF01282; Ribosomal_S24e; 1. DR ProDom; PD006052; Ribosomal_S24E; 1. DR PROSITE; PS00529; RIBOSOMAL_S24E; 1. KW Ribonucleoprotein; Ribosomal protein. FT CHAIN 1 132 40S ribosomal protein S24. FT /FTId=PRO_0000137627. SQ SEQUENCE 132 AA; 15305 MW; DC437F60F20C14F5 CRC64; MNDTVTVRTR KFMTNRLLQR KQMVVDVLHP GKATVPKTEI REKLAKMYKT TPDVVFVFGF RTQFGGGKTT GFAMVYDSLD YAKKNEPKHR LARHGLFEKK KTSRKQRKER KNRMKKVRGT KKASVGASKK KD // ID RS7_FUGRU Reviewed; 194 AA. AC P50894; P53548; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-MAR-2007, entry version 27. DE 40S ribosomal protein S7. GN Name=RPS7; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96371061; PubMed=8774896; DOI=10.1093/nar/24.16.3167; RA Cecconi F., Crosio C., Mariottini P., Cesareni G., Giorgi M., RA Brenner S., Amaldi F.; RT "A functional role for some Fugu introns larger than the typical short RT ones: the example of the gene coding for ribosomal protein S7 and RT snoRNA U17."; RL Nucleic Acids Res. 24:3167-3172(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein S7e family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X94942; CAA64412.1; -; Genomic_DNA. DR Ensembl; NEWSINFRUG00000124260; Fugu rubripes. DR InterPro; IPR000554; Ribosomal_S7E. DR PANTHER; PTHR11278; Ribosomal_S7E; 1. DR Pfam; PF01251; Ribosomal_S7e; 1. DR ProDom; PD006276; Ribosomal_S7E; 2. DR PROSITE; PS00948; RIBOSOMAL_S7E; 1. KW Ribonucleoprotein; Ribosomal protein. FT CHAIN 1 194 40S ribosomal protein S7. FT /FTId=PRO_0000174194. FT COMPBIAS 98 120 Arg/Lys-rich (basic). SQ SEQUENCE 194 AA; 22206 MW; D202501948D47E86 CRC64; MFSTSAKIVK PNGEKPDEFE SGISQALLEL EMNSDLKAQL RELNITAAKE IEVGGSRKAI IIFVPVPQLK SFQKIQVRLV RELEKKFSGK HVVFIAQRRI LPKPTRKSRS KNKQKRPRSR TLTSVHDAIL EDLVFPSEIV GKRIRVKMDS SRLIKVHLDK AQQNNVEHKV ETFSGVYKKL TGKDVVFEFP EFQL // ID SSRL_FUGRU Reviewed; 289 AA. AC O42179; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 20-MAR-2007, entry version 33. DE Somatostatin-like receptor F_48D10.1. GN Name=F_48D10.1; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Hawkins J., Gillam B.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein (By CC similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC -!- CAUTION: Seems to lack the C-terminal part (TM6 and TM7). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF013613; AAB86684.1; -; Genomic_DNA. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001418; Opioid_rcpt. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00384; OPIOIDR. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Transducer; Transmembrane. FT CHAIN 1 289 Somatostatin-like receptor F_48D10.1. FT /FTId=PRO_0000070133. FT TOPO_DOM 1 57 Extracellular (Potential). FT TRANSMEM 58 79 1 (Potential). FT TOPO_DOM 80 89 Cytoplasmic (Potential). FT TRANSMEM 90 110 2 (Potential). FT TOPO_DOM 111 126 Extracellular (Potential). FT TRANSMEM 127 148 3 (Potential). FT TOPO_DOM 149 170 Cytoplasmic (Potential). FT TRANSMEM 171 191 4 (Potential). FT TOPO_DOM 192 240 Extracellular (Potential). FT TRANSMEM 241 261 5 (Potential). FT TOPO_DOM 262 289 Cytoplasmic (Potential). FT CARBOHYD 40 40 N-linked (GlcNAc...) (Potential). FT DISULFID 125 221 By similarity. SQ SEQUENCE 289 AA; 32172 MW; 4F5A1776911D0ADA CRC64; MEPLDQTPGF PLSPEPNYWY ETTPSLLLVS YPHLLDISSN QSTQSVPFQG SSALLTAVIY ITVFVVGLTG NTLAIYVVLR YAGMKTVTNI YILNLAVADE LYIVGLPFLA TQNVLSYWPF GSFLCRVVMT ADSMNQFTSI FCLTVMSIDR YLAVVHPIRS TKWRHPRVAK VVSAAVWAVS FVVVLPVVIF SDVQVRPSRP LQVGTSSKCL VKRVQETFNS CNMIWPEPKN VWSTAFILYT AMVGFFGPLL IICLCYLLIV IKVRHRMSAA QVGAVVSTCP LNICCLSRR // ID SYH_FUGRU Reviewed; 519 AA. AC P70076; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 20-MAR-2007, entry version 41. DE Histidyl-tRNA synthetase (EC 6.1.1.21) (Histidine--tRNA ligase) DE (HisRS). GN Name=HARS; Synonyms=HISS; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Testis; RX MEDLINE=96323249; PubMed=8710896; DOI=10.1073/pnas.93.16.8485; RA Brenner S., Corrochano L.M.; RT "Translocation events in the evolution of aminoacyl-tRNA RT synthetases."; RL Proc. Natl. Acad. Sci. U.S.A. 93:8485-8489(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-histidine + tRNA(His) = AMP + CC diphosphate + L-histidyl-tRNA(His). CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z54243; CAA91012.1; -; Genomic_DNA. DR Ensembl; NEWSINFRUG00000150159; Fugu rubripes. DR InterPro; IPR004154; Anticodon_bd. DR InterPro; IPR004516; HisS. DR InterPro; IPR009068; S15_NS1_RNA_bd. DR InterPro; IPR002314; tRNA-synt_2b. DR InterPro; IPR006195; tRNA_ligase_II. DR Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PIRSF; PIRSF001549; His-tRNA_synth; 1. DR TIGRFAMs; TIGR00442; hisS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding; KW Protein biosynthesis. FT CHAIN 1 519 Histidyl-tRNA synthetase. FT /FTId=PRO_0000136337. SQ SEQUENCE 519 AA; 57913 MW; A1CBF5752070759E CRC64; MLAMHCARVC SVLMGCRTTT RALSIRSFPG VTLAQIDEEV AKLLELKAHL GGDDGKHQFV LKTAKGTRDY NPKQMAIREK VFNTIVSCFK RHGAETIDTP VFELKETLTG KYGEDSKLIY DLKDQGGELL SLRYDLTVPF ARYLAMNKIT NIKRYHIAKV YRRDNPAMTR GRYREFYQCD FDIAGQYDAM IPDAECLKIV HEILSELDLG DFRIKVNDRR ILDGMFAVCG VPDNMFRTIC STVDKLDKLP WEAVKNEMVN EKGLSEEAAD QIGVYVGMQG GMDLAERLLQ DQKMCQSTQA CAGLTDIKLL FSYLQLFQVT DKVVFDLSLA RGLDYYTGII YEAILTQAGV APVAPETSNE APTEECVTVG SVAGGGRYDG LVGMFDPKGR KVPCVGVSIG IERIFSIMEQ KAEASTEKIR TTEVQVMVAA AQKNLLEERL RLITELWNAG IKAELMYKKS PKLLSQLQHC EESGIPLVAI LGEQELKNGV VKLRNVATRD EVDISRADLI AEIKKRTSA // ID SYV_FUGRU Reviewed; 1217 AA. AC P49696; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 20-MAR-2007, entry version 40. DE Valyl-tRNA synthetase (EC 6.1.1.9) (Valine--tRNA ligase) (ValRS). GN Name=VARS; Synonyms=VARS1; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=97396021; PubMed=9254008; RA Lim E.H., Corrochano L.M., Elgar G., Brenner S.; RT "Genomic structure and sequence analysis of the valyl-tRNA synthetase RT gene of the Japanese pufferfish, Fugu rubripes."; RL DNA Seq. 7:141-151(1997). CC -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate CC + L-valyl-tRNA(Val). CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. CC -!- SIMILARITY: Contains 1 GST-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X91856; CAA62967.1; -; Genomic_DNA. DR HSSP; P96142; 1IVS. DR Ensembl; NEWSINFRUG00000142988; Fugu rubripes. DR InterPro; IPR013155; Anticodon_V_L_bd. DR InterPro; IPR004046; GST_C. DR InterPro; IPR010987; GST_C_like. DR InterPro; IPR002300; tRNA-synt_1a. DR InterPro; IPR001412; tRNA-synt_I. DR InterPro; IPR002303; tRNA-synt_val. DR InterPro; IPR010978; tRNA_bd_arm. DR InterPro; IPR009080; tRNAsyn_1a_bd. DR InterPro; IPR009008; ValRS_IleRS_edit. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR PRINTS; PR00986; TRNASYNTHVAL. DR TIGRFAMs; TIGR00422; valS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding; KW Protein biosynthesis. FT CHAIN 1 1217 Valyl-tRNA synthetase. FT /FTId=PRO_0000106256. FT DOMAIN 1 ? GST-like. FT MOTIF 293 303 "HIGH" region. FT MOTIF 809 813 "KMSKS" region. FT BINDING 812 812 ATP (By similarity). SQ SEQUENCE 1217 AA; 138218 MW; 5E08AF24B5C8A7A1 CRC64; MATLYVSPHL DDFRSLLALV AAEYCGNAKQ QSQVWQWLSF ADNELTPVSC AVVFPLMGMT GLDKKIQQNS RVELMRVLKV LDQALEPRTF LVGESITLAD MAVAMAVLLP FKYVLEPSDR NVLMNVTRWF TTCINQPEFL KVLGKISLCE KMVPVTAKTS TEEAAAVHPD AAALNGPPKT EAQLKKEAKK REKLEKFQQK KEMEAKKKMQ PVAEKKAKPE KRELGVITYD IPTPSGEKKD VVSPLPDSYS PQYVEAAWYP WWEKQGFFKP EFGRKSIGEQ NPRGIFMMCI PPPNVTGSLH LGHALTNAIQ DTLTRWHRMR GETTLWNPGC DHAGIATQVV VEKKLMREKG TSRHDLGREK FIEEVWKWKN EKGDRIYHQL KKLGSSLDWD RACFTMDPKL SYAVQEAFIR MHDEGVIYRS KRLVNWSCSL NSAISDIEVD KNELSGRTLL PVPGYKEKVE FGVLVSFAYK VDGSDEEVVV ATTRIETMLG DTAVAVHPSD SRYQHLKGKT VLHPFCDRKI PVVFDDFVDM SFGTGAVKIT PAHDHNDYEV GVRHNLAFIN ILDENGFVIN VPPPFLGMKR FDARKAVLQA LKDRDQFKEI KDNPMVVPVC SRSKDIVEPL MKPQWYVSCS DMGKQAADAV REGRLKIIPD HHSQTWFNWM DNIRDWCISR QLWWGHRIPA YFITVSDPSV KPGEDMDGHY RVSGRTPEEA REKAAKRFNV SPDKIALRQD EDVLDTWFSS GINPFSILGW PNETEDLNVF YPGTLLETGH DILFFWVARM VMMGLKLTGK LPFKEVYHCA VVRDAHGRKM SKSLGNVIDP LDDHIGIALE GLHAQLMDTN LDPLEVEKPK KVQKADYPNC IPECGTDALR FALCAYTSQG RDINLDVNRI LGYRHFCNKL WNAVKFAMRT LGDQFVPADT SPAEREESVS DRWILSRLST AVAQCDAAFR TYDFPAITTA IYNFWLYELC DVYLESVKPV FIKAKEDGSC ERPAAVCRQT LYTCLEVGLR LLAPLMPFVT EELYQRLPRR RPQSDPPSIC VTPYPDAAEF CWQCEDVDRD IDFIMGVVRT IRSLRSDYKL TKTAADCYLQ CTDAATVSLV QKYSLQIQTL SYSQAIVPLM APQPAPEGCA VAIASDRCTV NMMLKGLIDV EKEVPKLMGK KTDLEKQIEK LSEKISKGDY KEKVPVKVQE QDTEKLRQSQ TELEKVKEAM DNFQKMM // ID TCPD_FUGRU Reviewed; 536 AA. AC P53451; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 20-MAR-2007, entry version 39. DE T-complex protein 1 subunit delta (TCP-1-delta) (CCT-delta). GN Name=CCT4; Synonyms=CCTD; OS Fugu rubripes (Japanese pufferfish) (Takifugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; OC Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; OC Tetradontoidea; Tetraodontidae; Takifugu. OX NCBI_TaxID=31033; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC TISSUE=Testis; RX MEDLINE=96125198; PubMed=8543170; DOI=10.1016/0378-1119(95)00604-4; RA Yoda T., Morita T., Kawatsu K., Sueki K., Shibata T., Hamano Y.; RT "Cloning and sequencing of the chaperonin-encoding Cctd gene from Fugu RT rubripes rubripes."; RL Gene 166:249-253(1995). CC -!- FUNCTION: Molecular chaperone; assist the folding of proteins upon CC ATP hydrolysis. Known to play a role, in vitro, in the folding of CC actin and tubulin. CC -!- SUBUNIT: Hetero-oligomeric complex of about 850 to 900 kDa that CC forms two stacked rings, 12 to 16 nm in diameter. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D49483; BAA08447.1; -; mRNA. DR EMBL; D49484; BAA18913.1; -; Genomic_DNA. DR UniGene; Tru.1843; -. DR HSSP; P48424; 1A6D. DR Ensembl; NEWSINFRUG00000131796; Fugu rubripes. DR InterPro; IPR012717; Chap_CCT_delta. DR InterPro; IPR002194; Chaperonin_TCP-1. DR InterPro; IPR001844; Chaprnin_Cpn60. DR InterPro; IPR002423; Cpn60/TCP-1. DR InterPro; IPR008950; GroEL-ATPase. DR PANTHER; PTHR11353; Cpn60/TCP-1; 1. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00298; CHAPERONIN60. DR PRINTS; PR00304; TCOMPLEXTCP1. DR TIGRFAMs; TIGR02342; chap_CCT_delta; 1. DR PROSITE; PS00750; TCP1_1; 1. DR PROSITE; PS00751; TCP1_2; 1. DR PROSITE; PS00995; TCP1_3; 1. KW ATP-binding; Chaperone; Nucleotide-binding. FT CHAIN 1 536 T-complex protein 1 subunit delta. FT /FTId=PRO_0000128336. SQ SEQUENCE 536 AA; 57716 MW; B3ED3285FAC18D07 CRC64; MPEGKATSSA SNTGKNKGGA YQDRDKPAQI RYSNISAAKA VADAVRTSLG PKGMDKMIQD EKGDVTITND GATILKQMQV LHPSAKMLVE LSKAQDIEAG DGTTSVVVIA GALLDSCNRL LQRGIHPTII SESFQKAVDK GVEVLTAMSQ PVQLGDRETL LNSATTSLCS KVVSQYSSLL APMSVDAVMR VIDPATATSV DLHDIKIIKK LGGTIDDCEL VEGLVLTQRV ANSSVSRVEK AKIGLIQFCL SPPKTDMDNQ IVVSDYTQMD RVLREERAYI LNMVKQIKKA GCNVLFIQKS ILRDALSDLA LHFLNKMKIM VVKDIEREDI EFICKTIGTK PIAHIDHFTP EMLGTAELAE EVSLDGSGKL VKITGCASPG KTVSIVVRGS NKLVIEEAER SIHDALCVIR CLVKKRALIA GGGAPEIELA VRLAEYSRTL GGMEAYCVRA YSDALEVIPS TLAENAGLNP ISTVTELRNR HAQGDKMAGI NVRKGGISNI MEELVVQPLL VSISALTLAT ETVRSILKID DVVNAR // ID ACH2_DROME Reviewed; 576 AA. AC P17644; Q9VC73; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 03-APR-2007, entry version 78. DE Acetylcholine receptor subunit alpha-like 2 precursor. GN Name=nAcR-alpha-96Ab; Synonyms=Acr96Ab, AcrE, sad; ORFNames=CG6844; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Head; RX MEDLINE=90301489; PubMed=2114015; DOI=10.1093/nar/18.12.3640; RA Baumann A., Jonas P., Gundelfinger E.D.; RT "Sequence of D alpha 2, a novel alpha-like subunit of Drosophila RT nicotinic acetylcholine receptors."; RL Nucleic Acids Res. 18:3640-3640(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Head; RX MEDLINE=90353591; PubMed=2117557; DOI=10.1016/0014-5793(90)81170-S; RA Jonas P., Baumann A., Merz B., Gundelfinger E.D.; RT "Structure and developmental expression of the D alpha 2 gene encoding RT a novel nicotinic acetylcholine receptor protein of Drosophila RT melanogaster."; RL FEBS Lett. 269:264-268(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90360975; PubMed=1697262; RA Sawruk E., Schloss P., Betz H., Schmitt B.; RT "Heterogeneity of Drosophila nicotinic acetylcholine receptors: SAD, a RT novel developmentally regulated alpha-subunit."; RL EMBO J. 9:2671-2677(1990). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: After binding acetylcholine, the AChR responds by an CC extensive change in conformation that affects all subunits and CC leads to opening of an ion-conducting channel across the plasma CC membrane. CC -!- INTERACTION: CC Q9VHK6:CG9836; NbExp=1; IntAct=EBI-93751, EBI-141585; CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: CNS in embryos. CC -!- DEVELOPMENTAL STAGE: Late embryonic and late pupal stages. CC -!- SIMILARITY: Belongs to the ligand-gated ionic channel (TC 1.A.9) CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X52274; CAA36517.1; -; mRNA. DR EMBL; X53583; CAA37652.1; -; mRNA. DR EMBL; AE003748; AAF56303.1; -; Genomic_DNA. DR EMBL; AY058446; AAL13675.1; -; mRNA. DR PIR; S11679; ACFFA2. DR UniGene; Dm.2363; -. DR DIP; DIP:22674N; -. DR IntAct; P17644; -. DR Ensembl; CG6844; Drosophila melanogaster. DR KEGG; dme:Dmel_CG6844; -. DR FlyBase; FBgn0000039; nAcR-alpha-96Ab. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-013190-MONOMER; -. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-013191-MONOMER; -. DR GermOnline; CG6844; Drosophila melanogaster. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR006029; Neu_channel_TM. DR InterPro; IPR006202; Neur_chan_lig_bd. DR InterPro; IPR006201; Neur_channel. DR InterPro; IPR002394; Nic_ach_rcpt. DR Gene3D; G3DSA:3.30.1100.20; Neur_chan_lig_bd; 1. DR PANTHER; PTHR18945; Neur_channel; 2. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR00254; NICOTINICR. DR PRINTS; PR00252; NRIONCHANNEL. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. KW Complete proteome; Glycoprotein; Ion transport; Ionic channel; KW Membrane; Postsynaptic membrane; Receptor; Signal; Transmembrane; KW Transport. FT SIGNAL 1 21 Probable. FT CHAIN 22 576 Acetylcholine receptor subunit alpha-like FT 2. FT /FTId=PRO_0000000300. FT TOPO_DOM 22 261 Extracellular (Potential). FT TRANSMEM 262 285 Potential. FT TRANSMEM 293 311 Potential. FT TRANSMEM 327 346 Potential. FT TOPO_DOM 347 526 Cytoplasmic (Potential). FT TRANSMEM 527 545 Potential. FT CARBOHYD 65 65 N-linked (GlcNAc...) (Potential). FT CARBOHYD 254 254 N-linked (GlcNAc...) (Potential). FT CARBOHYD 570 570 N-linked (GlcNAc...) (Potential). FT DISULFID 169 183 By similarity. FT DISULFID 243 244 Associated with receptor activation (By FT similarity). SQ SEQUENCE 576 AA; 65506 MW; 97D6A46CADC3F42F CRC64; MAPGCCTTRP RPIALLAHIW RHCKPLCLLL VLLLLCETVQ ANPDAKRLYD DLLSNYNRLI RPVSNNTDTV LVKLGLRLSQ LIDLNLKDQI LTTNVWLEHE WQDHKFKWDP SEYGGVTELY VPSEHIWLPD IVLYNNADGE YVVTTMTKAI LHYTGKVVWT PPAIFKSSCE IDVRYFPFDQ QTCFMKFGSW TYDGDQIDLK HISQKNDKDN KVEIGIDLRE YYPSVEWDIL GVPAERHEKY YPCCAEPYPD IFFNITLRRK TLFYTVNLII PCVGISYLSV LVFYLPADSG EKIALCISIL LSQTMFFLLI SEIIPSTSLA LPLLGKYLLF TMLLVGLSVV ITIIILNIHY RKPSTHKMRP WIRSFFIKRL PKLLLMRVPK DLLRDLAANK INYGLKFSKT KFGQALMDEM QMNSGGSSPD SLRRMQGRVG AGGCNGMHVT TATNRFSGLV GALGGGLSTL SGYNGLPSVL SGLDDSLSDV AARKKYPFEL EKAIHNVMFI QHHMQRQDEF NAEDQDWGFV AMVMDRLFLW LFMIASLVGT FVILGEAPSL YDDTKAIDVQ LSDVAKQIYN LTEKKN // ID HBA_HUMAN Reviewed; 142 AA. AC P69905; P01922; Q96KF1; Q9NYR7; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 03-APR-2007, entry version 41. DE Hemoglobin subunit alpha (Hemoglobin alpha chain) (Alpha-globin). GN Name=HBA1; GN and GN Name=HBA2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1). RX MEDLINE=81088339; PubMed=7448866; DOI=10.1016/0092-8674(80)90347-5; RA Michelson A.M., Orkin S.H.; RT "The 3' untranslated regions of the duplicated human alpha-globin RT genes are unexpectedly divergent."; RL Cell 22:371-377(1980). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (HBA2). RX MEDLINE=80137531; PubMed=6244294; RA Wilson J.T., Wilson L.B., Reddy V.B., Cavallesco C., Ghosh P.K., RA Deriel J.K., Forget B.G., Weissman S.M.; RT "Nucleotide sequence of the coding portion of human alpha globin RT messenger RNA."; RL J. Biol. Chem. 255:2807-2815(1980). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2). RX MEDLINE=81175088; PubMed=6452630; RA Liebhaber S.A., Goossens M.J., Kan Y.W.; RT "Cloning and complete nucleotide sequence of human 5'-alpha-globin RT gene."; RL Proc. Natl. Acad. Sci. U.S.A. 77:7054-7058(1980). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6946451; RA Orkin S.H., Goff S.C., Hechtman R.L.; RT "Mutation in an intervening sequence splice junction in man."; RL Proc. Natl. Acad. Sci. U.S.A. 78:5041-5045(1981). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-32. RX MEDLINE=21303311; PubMed=11410421; RA Zhao Y., Xu X.; RT "Alpha2(CD31 AGG-->AAG, Arg-->Lys) causing non-deletional alpha- RT thalassemia in a Chinese family with HbH disease."; RL Haematologica 86:541-542(2001). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1). RX MEDLINE=21295668; PubMed=11402454; RA Zhao Y., Zhong M., Liu Z., Xu X.; RT "Rapid detection of the common alpha-thalassemia-2 determinants by PCR RT assay."; RL Zhonghua Yi Xue Yi Chuan Xue Za Zhi 18:216-218(2001). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (HBA2). RC TISSUE=Blood; RA Kutlar F., Leithner C., Kutlar A.; RT "Rapid sequencing of mRNA of the human alpha two globin, directly RT isolated from reticulocytes in whole blood."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (HBA1). RC TISSUE=Blood; RA Kutlar F., Leithner C., Kutlar A.; RT "cDNA sequencing of human alpha one globin mRNA, the 3'untranslated RT region is different than alpha two globin."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Blood; RA Kutlar F., Holley L., Leithner C., Kutlar A.; RT "An alpha chain variant 'Hemoglobin J-Toronto (Cd.5 /Ala to Asp)' RT mutation was detected on the alpha-1 globin mRNA by sequencing of RT cDNA."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA2), AND VARIANT EVANS MET-63. RC TISSUE=Blood; RA Kutlar F., Elam D., Hoff J.V., Holley L., Kutlar A.; RT "Unstable Hb 'Evans' (GTG->ATG/Val 62 Met) was detected on the alpha-2 RT globin gene of an Hispanic girl."; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HBA1 AND HBA2). RX MEDLINE=21096910; PubMed=11157797; DOI=10.1093/hmg/10.4.339; RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., RA Higgs D.R.; RT "Sequence, structure and pathology of the fully annotated terminal 2 RT Mb of the short arm of human chromosome 16."; RL Hum. Mol. Genet. 10:339-352(2001). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALPHA-2). RC TISSUE=Bone marrow, Brain, Lung, and Spleen; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [14] RP PROTEIN SEQUENCE OF 2-142. RX PubMed=13872627; RA Braunitzer G., Gehring-Muller R., Hilschmann N., Hilse K., Hobom G., RA Rudloff V., Wittmann-Liebold B.; RT "The constitution of normal adult human haemoglobin."; RL Hoppe-Seyler's Z. Physiol. Chem. 325:283-286(1961). RN [15] RP PROTEIN SEQUENCE OF 2-142. RX PubMed=13954546; RA Hill R.J., Konigsberg W.; RT "The structure of human hemoglobin: IV. The chymotryptic digestion of RT the alpha chain of human hemoglobin."; RL J. Biol. Chem. 237:3151-3156(1962). RN [16] RP PROTEIN SEQUENCE OF 2-142. RX PubMed=14093912; DOI=10.1021/bi00906a030; RA Schroeder W.A., Shelton J.R., Shelton J.B., Cormick J.; RT "The amino acid sequence of the alpha chain of human fetal RT hemoglobin."; RL Biochemistry 2:1353-1357(1963). RN [17] RP PROTEIN SEQUENCE OF 2-32. RC TISSUE=Platelet; RX MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN. RX MEDLINE=76027820; PubMed=1177322; DOI=10.1016/S0022-2836(75)80037-4; RA Fermi G.; RT "Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2.5- RT A resolution: refinement of the atomic model."; RL J. Mol. Biol. 97:237-256(1975). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). RX PubMed=7373648; DOI=10.1016/0022-2836(80)90308-3; RA Baldwin J.M.; RT "The structure of human carbonmonoxy haemoglobin at 2.7-A RT resolution."; RL J. Mol. Biol. 136:103-128(1980). RN [20] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF LIGANDED R2 STATE. RX MEDLINE=92381041; PubMed=1512262; RA Silva M.M., Rogers P.H., Arnone A.; RT "A third quaternary structure of human hemoglobin A at 1.7-A RT resolution."; RL J. Biol. Chem. 267:17248-17256(1992). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF HB GOWER-2. RX MEDLINE=98332748; PubMed=9665850; DOI=10.1006/jmbi.1998.1868; RA Sutherland-Smith A.J., Baker H.M., Hofmann O.M., Brittain T., RA Baker E.N.; RT "Crystal structure of a human embryonic haemoglobin: the carbonmonoxy RT form of Gower II (alpha2 epsilon2) haemoglobin at 2.9-A resolution."; RL J. Mol. Biol. 280:475-484(1998). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF VARIANT HB CATONSVILLE GLU-38 RP INS. RX MEDLINE=93192190; PubMed=8448109; DOI=10.1021/bi00061a007; RA Kavanaugh J.S., Moo-Penn W.F., Arnone A.; RT "Accommodation of insertions in helices: the mutation in hemoglobin RT Catonsville (Pro 37 alpha-Glu-Thr 38 alpha) generates a 3(10)-->alpha RT bulge."; RL Biochemistry 32:2509-2513(1993). RN [23] RP VARIANT AL-AIN ABU DHABI ASP-19. RX MEDLINE=93053723; PubMed=1428941; RA Abbes S., M'Rad A., Fitzgerald P.A., Dormer P., Blouquit Y., RA Kister J., Galacteros F., Wajcman H.; RT "HB Al-Ain Abu Dhabi [alpha 18(A16)Gly-->Asp]: a new hemoglobin RT variant discovered in an Emiratee family."; RL Hemoglobin 16:355-362(1992). RN [24] RP VARIANT ATAGO TYR-86. RX MEDLINE=72030550; PubMed=5115619; RA Fujiwara N., Maekawa T., Matsuda G.; RT "Hemoglobin Atago (alpha2-85 Tyr beta-2) a new abnormal human RT hemoglobin found in Nagasaki. Biochemical studies on hemoglobins and RT myoglobins. VI."; RL Int. J. Protein Res. 3:35-39(1971). RN [25] RP VARIANT AUCKLAND ASN-88. RX MEDLINE=97463291; PubMed=9322075; RA Brennan S.O., Matthews J.R.; RT "Hb Auckland [alpha 87(F8) His-->Asn]: a new mutation of the proximal RT histidine identified by electrospray mass spectrometry."; RL Hemoglobin 21:393-403(1997). RN [26] RP VARIANTS J-BUDA ASN-62 AND G-PEST ASN-75. RA Brimhall B.J., Duerst M., Hollan S.R., Stenzel P., Szelenyi J., RA Jones R.T.; RT "Structural characterizations of hemoglobins J-Buda (alpha 61 (E10) RT Lys-to-Asn) and G-Pest (alpha 74 (EF3) Asp-to-Asn)."; RL Biochim. Biophys. Acta 336:344-360(1974). RN [27] RP VARIANT CEMENELUM TRP-93. RX PubMed=8148419; RA Wajcman H., Kister J., M'Rad A., Soummer A.M., Galacteros F.; RT "Hb Cemenelum [alpha 92 (FG4) Arg-->Trp]: a hemoglobin variant of the RT alpha 1/beta 2 interface that displays a moderate increase in oxygen RT affinity."; RL Ann. Hematol. 68:73-76(1994). RN [28] RP VARIANTS CHONGQING ARG-3 AND HARBIN MET-17. RX MEDLINE=85130255; PubMed=6526652; RA Zeng Y.-T., Huang S.-Z., Qiu X.-K., Cheng G.-C., Ren Z.-R., Jin Q.-C., RA Chen C.-Y., Jiao C.-T., Tang Z.-G., Liu R.-H., Bao X.-H., Zeng L.-Z., RA Duan Y.-Q., Zhang G.-Y.; RT "Hemoglobin Chongqing [alpha 2(NA2)Leu-->Arg] and hemoglobin Harbin RT [alpha 16(A14)Lys-->Met] found in China."; RL Hemoglobin 8:569-581(1984). RN [29] RP VARIANT CLINIC LYS-61 DEL. RX PubMed=10206681; RX DOI=10.1002/(SICI)1098-1004(1998)11:5<412::AID-HUMU14>3.3.CO;2-I; RA Ayala S., Colomer D., Gelpi J.L., Corron J.L.V.; RT "Alpha-thalassaemia due to a single codon deletion in the alpha 1- RT globin gene. Computational structural analysis of the new alpha-chain RT variant."; RL Hum. Mutat. 11:412-412(1998). RN [30] RP VARIANT DAVENPORT HIS-79. RX MEDLINE=91331854; PubMed=2101836; RA Wilson J.B., Webber B.B., Plaseska D., de Alarcon P.A., McMillan S.K., RA Huisman T.H.J.; RT "Hb Davenport or alpha 2(78)(EF7)Asn-->His beta 2."; RL Hemoglobin 14:599-605(1990). RN [31] RP VARIANT EVANS MET-63. RX MEDLINE=90109650; PubMed=2606724; RA Wilson J.B., Webber B.B., Kutlar A., Reese A.L., McKie V.C., RA Lutcher C.L., Felice A.E., Huisman T.H.J.; RT "Hb Evans or alpha 262(E11)Val-->Met beta 2; an unstable hemoglobin RT causing a mild hemolytic anemia."; RL Hemoglobin 13:557-566(1989). RN [32] RP VARIANTS SPANISH TOWN VAL-28 AND FORT DE FRANCE ARG-46. RX MEDLINE=89323437; PubMed=2752146; RA Cash F.E., Monplaisir N., Goossens M., Liebhaber S.A.; RT "Locus assignment of two alpha-globin structural mutants from the RT Caribbean basin: alpha Fort de France (alpha 45 Arg) and alpha Spanish RT Town (alpha 27 Val)."; RL Blood 74:833-835(1989). RN [33] RP VARIANT GODAVARI THR-96. RX MEDLINE=98153063; PubMed=9494044; RA Wajcman H., Kister J., Riou J., Galacteros F., Girot R., RA Maier-Redelsperger M., Nayudu N.V.S., Giordano P.C.; RT "Hb Godavari [alpha 95(G2)Pro-->Thr]: a neutral amino acid RT substitution in the alpha 1 beta 2 interface that modifies the RT electrophoretic mobility of hemoglobin."; RL Hemoglobin 22:11-22(1998). RN [34] RP VARIANT GRADY GLU-PHE-THR-119 INS. RX MEDLINE=75010592; PubMed=4528583; RA Huisman T.H.J., Wilson J.B., Gravely M., Hubbard M.; RT "Hemoglobin Grady: the first example of a variant with elongated RT chains due to an insertion of residues."; RL Proc. Natl. Acad. Sci. U.S.A. 71:3270-3273(1974). RN [35] RP VARIANT HANAMAKI GLU-140. RX MEDLINE=92340291; PubMed=1634363; RA Orisaka M., Tajima T., Harano T., Harano K., Kushida Y., Imai K.; RT "A new alpha chain variant, Hb Hanamaki or alpha 2(139)(HC1)Lys-->Glu RT beta 2, found in a Japanese family."; RL Hemoglobin 16:67-71(1992). RN [36] RP VARIANT HANDA MET-91. RX MEDLINE=83056269; PubMed=6815131; RA Harano T., Harano K., Shibata S., Ueda S., Imai K., Seki M.; RT "HB Handa [alpha 90 (FG 2) Lys replaced by Met]: structure and RT biosynthesis of a new slightly higher oxygen affinity variant."; RL Hemoglobin 6:379-389(1982). RN [37] RP VARIANT HASHARON HIS-48. RX MEDLINE=69165810; PubMed=5780195; RA Charache S., Mondzac A.M., Gessner U.; RT "Hemoglobin Hasharon (alpha-2-47 his(CD5)beta-2): a hemoglobin found RT in low concentration."; RL J. Clin. Invest. 48:834-847(1969). RN [38] RP VARIANT HOBART ARG-21. RX MEDLINE=88006902; PubMed=3654264; RA Fleming P.J., Sumner D.R., Wyatt K., Hughes W.G., Melrose W.D., RA Jupe D.M.D., Baikie M.J.; RT "Hemoglobin Hobart or alpha 20(Bl)His-->Arg: a new alpha chain RT hemoglobin variant."; RL Hemoglobin 11:211-220(1987). RN [39] RP VARIANT INKSTER VAL-86. RX MEDLINE=74302151; PubMed=4212045; RA Reed R.E., Winter W.P., Rucknagel D.L.; RT "Haemoglobin inkster (alpha2 85aspartic acid leads to valine beta2) RT coexisting with beta-thalassaemia in a Caucasian family."; RL Br. J. Haematol. 26:475-484(1974). RN [40] RP VARIANT KANAGAWA MET-41. RX MEDLINE=92340282; PubMed=1634355; RA Miyashita H., Hashimoto K., Mohri H., Ohokubo T., Harano T., RA Harano K., Imai K.; RT "Hb Kanagawa [alpha 40(C5)Lys-->Met]: a new alpha chain variant with RT an increased oxygen affinity."; RL Hemoglobin 16:1-10(1992). RN [41] RP VARIANT KURDISTAN TYR-48. RX MEDLINE=94252883; PubMed=8195005; RA Giordano P.C., Harteveld C.L., Streng H., Oosterwijk J.C., RA Heister J.G.A.M., Amons R., Bernini L.F.; RT "Hb Kurdistan [alpha 47(CE5)Asp-->Tyr], a new alpha chain variant in RT combination with beta (0)-thalassemia."; RL Hemoglobin 18:11-18(1994). RN [42] RP VARIANT KUROSAKI GLU-8. RX MEDLINE=96031515; PubMed=7558876; RA Harano T., Harano K., Imai K., Murakami T., Matsubara H.; RT "Hb Kurosaki [alpha 7(A5)Lys-->Glu]: a new alpha chain variant found RT in a Japanese woman."; RL Hemoglobin 19:197-201(1995). RN [43] RP VARIANT J-MEERUT/J-BIRMINGHAM GLU-121. RX MEDLINE=95229430; PubMed=7713747; RA Yalcin A., Avcu F., Beyan C., Guergey A., Ural A.U.; RT "A case of HB J-Meerut (or Hb J-Birmingham) [alpha RT 120(H3)Ala-->Glu]."; RL Hemoglobin 18:433-435(1994). RN [44] RP VARIANT MELUSINE SER-115. RX MEDLINE=94124250; PubMed=8294199; RA Wacjman H., Klames G., Groff P., Prome D., Riou J., Galacteros F.; RT "Hb Melusine [alpha 114(GH2)Pro-->Ser]: a new neutral hemoglobin RT variant."; RL Hemoglobin 17:397-405(1993). RN [45] RP VARIANT MONTGOMERY ARG-49. RX MEDLINE=75109326; PubMed=1115799; RA Brimhall B., Jones R.T., Schneider R.G., Hosty T.S., Tomlin G., RA Atkins R.; RT "Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys) RT and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg)."; RL Biochim. Biophys. Acta 379:28-32(1975). RN [46] RP VARIANT PETAH TIKVA ASP-111. RX MEDLINE=81134478; PubMed=7470621; RA Honig G.R., Shamsuddin M., Zaizov R., Steinherz M., Solar I., RA Kirschman C.; RT "Hemoglobin Petah Tikva (alpha 110 Ala replaced by Asp): a new RT unstable variant with alpha-thalassemia-like expression."; RL Blood 57:705-711(1981). RN [47] RP VARIANT PHNOM PENH ILE-118 INS. RX MEDLINE=98112407; PubMed=9452028; RA Wajcman H., Prehu M.O., Prehu C., Blouquit Y., Prome D., RA Galacteros F.; RT "Hemoglobin Phnom Penh [alpha117Phe(H1)-Ile-alpha118Thr(H2)]; evidence RT for a hotspot for insertion of residues in the third exon of the RT alpha1-globin gene."; RL Hum. Mutat. Suppl. 1:S20-S22(1998). RN [48] RP VARIANT PORT HURON ARG-57. RX MEDLINE=92202056; PubMed=1802882; RA Zwerdling T., Williams S., Nasr S.A., Rucknagel D.L.; RT "Hb Port Huron [alpha 56 (E5)Lys-->Arg]: a new alpha chain variant."; RL Hemoglobin 15:381-391(1991). RN [49] RP VARIANT SAWARA ALA-7. RX MEDLINE=74008827; PubMed=4744335; RA Sumida I., Ohta Y., Imamura T., Yanase T.; RT "Hemoglobin Sawara: alpha 6(A4) aspartic acid leads to alanine."; RL Biochim. Biophys. Acta 322:23-26(1973). RN [50] RP VARIANT SHENYANG GLU-27. RX MEDLINE=83135048; PubMed=7161109; RA Zeng Y.-T., Huang S.-Z., Zhou X., Qiu X.-K., Dong Q., Li M., Bai J.; RT "Hb Shenyang (alpha 26 (B7) Ala replaced by Glu): a new unstable RT variant found in China."; RL Hemoglobin 6:625-628(1982). RN [51] RP VARIANT SUAN-DOK ARG-110. RX MEDLINE=80006169; PubMed=478977; RA Sanguansermsri T., Matragoon S., Changloah L., Flatz G.; RT "Hemoglobin Suan-Dok (alpha 2 109 (G16) Leu replaced by Arg beta 2): RT an unstable variant associated with alpha-thalassemia."; RL Hemoglobin 3:161-174(1979). RN [52] RP VARIANT SUN PRAIRIE PRO-131. RX MEDLINE=91177710; PubMed=2079430; RA Harkness M., Harkness D.R., Kutlar F., Kutlar A., Wilson J.B., RA Webber B.B., Codrington J.F., Huisman T.H.J.; RT "Hb Sun Prairie or alpha(2)130(H13)Ala-->Pro beta 2, a new unstable RT variant occurring in low quantities."; RL Hemoglobin 14:479-489(1990). RN [53] RP VARIANT SWAN RIVER GLY-7. RX MEDLINE=96351655; PubMed=8745434; RA Harano T., Harano K., Imai K., Terunuma S.; RT "HB Swan River [alpha 6(A4)Asp-->Gly] observed in a Japanese man."; RL Hemoglobin 20:75-78(1996). RN [54] RP VARIANT THIONVILLE GLU-2. RX MEDLINE=92316953; PubMed=1618774; RA Vasseur C., Blouquit Y., Kister J., Prome D., Kavanaugh J.S., RA Rogers P.H., Guillemin C., Arnone A., Galacteros F., Poyart C., RA Rosa J., Wajcman H.; RT "Hemoglobin Thionville. An alpha-chain variant with a substitution of RT a glutamate for valine at NA-1 and having an acetylated methionine NH2 RT terminus."; RL J. Biol. Chem. 267:12682-12691(1992). RN [55] RP VARIANT TUNIS-BIZERTE PRO-130. RX MEDLINE=95306384; PubMed=7786798; RA Darbellay R., Mach-Pascual S., Rose K., Graf J., Beris P.; RT "Haemoglobin Tunis-Bizerte: a new alpha 1 globin 129 Leu-->Pro RT unstable variant with thalassaemic phenotype."; RL Br. J. Haematol. 90:71-76(1995). RN [56] RP VARIANT TURRIFF GLU-100. RX MEDLINE=92340284; PubMed=1634357; RA Langdown J.V., Davidson R.J., Williamson D.; RT "A new alpha chain variant, Hb Turriff [alpha 99(G6)Lys-->Glu]: the RT interference of abnormal hemoglobins in Hb A1c determination."; RL Hemoglobin 16:11-17(1992). RN [57] RP VARIANT VAL DE MARNE ARG-134. RX MEDLINE=94124251; PubMed=8294200; RA Wacjman H., Kister J., M'Rad A., Marden M.C., Riou J., Galacteros F.; RT "Hb Val de Marne [alpha 133(H16)Ser-->Arg]: a new hemoglobin variant RT with moderate increase in oxygen affinity."; RL Hemoglobin 17:407-417(1993). RN [58] RP VARIANT WESTMEAD GLN-123. RX MEDLINE=92155975; PubMed=1686260; RA Jiang N.H., Liang S., Wen X.J., Liang R., Su C., Tang Z.; RT "Hb Westmead: an alpha 2-globin gene mutation detected by polymerase RT chain reaction and Stu I cleavage."; RL Hemoglobin 15:291-295(1991). RN [59] RP VARIANT WOODVILLE TYR-7. RX MEDLINE=86167529; PubMed=3754246; RA Como P.F., Barber S., Sage R.E., Kronenberg H.; RT "Hemoglobin Woodville: alpha (2)6(A4) aspartic acid-->tyrosine."; RL Hemoglobin 10:135-141(1986). RN [60] RP VARIANT YUDA ASP-131. RX MEDLINE=93053734; PubMed=1428950; RA Fujisawa K., Hattori Y., Ohba Y., Ando S.; RT "Hb Yuda or alpha 130(H13)Ala-->Asp; a new alpha chain variant with RT low oxygen affinity."; RL Hemoglobin 16:435-439(1992). RN [61] RP VARIANT ZAIRE HIS-LEU-PRO-ALA-GLU-117 INS. RX MEDLINE=92380658; PubMed=1511986; DOI=10.1007/BF00221961; RA Wajcman H., Blouquit Y., Vasseur C., le Querrec A., Laniece M., RA Melevendi C., Rasore A., Galacteros F.; RT "Two new human hemoglobin variants caused by unusual mutational RT events: Hb Zaire contains a five residue repetition within the alpha- RT chain and Hb Duino has two residues substituted in the beta-chain."; RL Hum. Genet. 89:676-680(1992). RN [62] RP VARIANT BOGHE GLN-59, AND VARIANT CHAROLLES TYR-104. RX PubMed=10569723; RA Lacan P., Francina A., Souillet G., Aubry M., Couprie N., RA Dementhon L., Becchi M.; RT "Two new alpha chain variants: Hb Boghe [alpha58(E7)His-->Gln, RT alpha2], a variant on the distal histidine, and Hb CHarolles RT [alpha103(G10)His-Tyr, alpha1]."; RL Hemoglobin 23:345-352(1999). RN [63] RP VARIANT CAMPINAS VAL-27, AND VARIANT WEST ONE GLY-127. RX PubMed=14576901; DOI=10.1590/S0100-879X2003001100004; RA Jorge S.B., Melo M.B., Costa F.F., Sonati M.F.; RT "Screening for mutations in human alpha-globin genes by nonradioactive RT single-strand conformation polymorphism."; RL Braz. J. Med. Biol. Res. 36:1471-1474(2003). RN [64] RP VARIANT BASSETT ALA-95, AND CHARACTERIZATION OF VARIANT BASSETT RP ALA-95. RX PubMed=15495251; DOI=10.1002/ajh.20184; RA Abdulmalik O., Safo M.K., Lerner N.B., Ochotorena J., Daikhin E., RA Lakka V., Santacroce R., Abraham D.J., Asakura T.; RT "Characterization of hemoglobin bassett (alpha94Asp-->Ala), a variant RT with very low oxygen affinity."; RL Am. J. Hematol. 77:268-276(2004). RN [65] RP VARIANT PLASENCIA ARG-126. RX PubMed=15921163; RA Martin G., Villegas A., Gonzalez F.A., Ropero P., Hojas R., Polo M., RA Mateo M., Salvador M., Benavente C.; RT "A novel mutation of the alpha2-globin causing alpha(+)-thalassemia: RT Hb Plasencia [alpha125(H8)Leu-->Arg (alpha2)."; RL Hemoglobin 29:113-117(2005). CC -!- FUNCTION: Involved in oxygen transport from the lung to the CC various peripheral tissues. CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in CC adult hemoglobin A (HbA); two alpha chains and two delta chains in CC adult hemoglobin A2 (HbA2); two alpha chains and two epsilon CC chains in early embryonic hemoglobin Gower-2; two alpha chains and CC two gamma chains in fetal hemoglobin F (HbF). CC -!- INTERACTION: CC Q9NZD4:AHSP; NbExp=1; IntAct=EBI-714680, EBI-720250; CC P68871:HBB; NbExp=1; IntAct=EBI-714680, EBI-715554; CC -!- TISSUE SPECIFICITY: Red blood cells. CC -!- PTM: The initiator Met is not cleaved in variant Thionville and is CC acetylated. CC -!- DISEASE: Defects in HBA1/HBA2 are the cause of alpha-thalassemia CC [MIM:141800]. The thalassemias are the most common monogenic CC diseases and occur mostly in Mediterranean and Southeast Asian CC populations. The hallmark of alpha-thalassemia is an imbalance in CC globin-chain production in the adult HbA molecule. The level of CC alpha chain production can range from none to very nearly normal CC levels. Deletion of both copies of each of the two alpha-globin CC genes causes alpha(0)-thalassemia, also known as homozygous alpha- CC thalassemia. Due to the complete absence of alpha chains, the CC predominant fetal hemoglobin is a tetramer of gamma-chains (Bart CC hemoglobin) that has essentially no oxygen carrying capacity. This CC causes oxygen starvation in the fetal tissues and leads to hydrops CC fetalis, prenatal lethality or early neonatal death. The loss of CC three alpha genes results in high levels of a tetramer of four CC beta chains (hemoglobin H), causing a severe and life-threatening CC anemia known as hemoglobin H disease. Untreated, most patients die CC in childhood or early adolescence. The loss of two alpha genes CC results in mild alpha-thalassemia, also known as heterozygous CC alpha-thalassemia. Affected individuals have small red cells and a CC mild anemia (microcytosis). If three of the four alpha-globin CC genes are functional, individuals are completely asymptomatic. CC Some rare forms of alpha-thalassemia are due to point mutations CC (non-deletional alpha-thalassemia). The thalassemic phenotype is CC due to unstable globin alpha chains that are rapidly catabolized CC prior to formation of the alpha-beta heterotetramers. CC -!- MISCELLANEOUS: Gives blood its red color. CC -!- SIMILARITY: Belongs to the globin family. CC -!- WEB RESOURCE: NAME=HbVar; CC NOTE=Human hemoglobin variants and thalassemias; CC URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBA1". CC -!- WEB RESOURCE: NAME=HbVar; CC NOTE=Human hemoglobin variants and thalassemias; CC URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBA2". CC -!- WEB RESOURCE: NAME=GeneReviews; CC URL="http://www.genetests.org/query?gene=HBA1". CC -!- WEB RESOURCE: NAME=GeneReviews; CC URL="http://www.genetests.org/query?gene=HBA2". CC -!- WEB RESOURCE: NAME=SHMPD; CC NOTE=The Singapore human mutation and polymorphism database; CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HBA1". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J00153; AAB59407.1; -; Genomic_DNA. DR EMBL; J00153; AAB59408.1; -; Genomic_DNA. DR EMBL; V00491; CAA23750.1; -; Genomic_DNA. DR EMBL; V00493; CAA23752.1; -; mRNA. DR EMBL; V00488; CAA23748.1; -; Genomic_DNA. DR EMBL; V00516; CAA23774.1; -; Genomic_DNA. DR EMBL; AF230076; AAF72612.1; -; Genomic_DNA. DR EMBL; AF525460; AAM83102.1; -; Genomic_DNA. DR EMBL; AF097635; AAC72839.1; -; mRNA. DR EMBL; AF105974; AAC97373.1; -; mRNA. DR EMBL; AF349571; AAK37554.1; -; mRNA. DR EMBL; AF536204; AAN04486.1; -; Genomic_DNA. DR EMBL; AE006462; AAK61215.1; -; Genomic_DNA. DR EMBL; AE006462; AAK61216.1; -; Genomic_DNA. DR EMBL; Z84721; CAB06554.1; -; Genomic_DNA. DR EMBL; Z84721; CAB06555.1; -; Genomic_DNA. DR EMBL; BC005931; AAH05931.1; -; mRNA. DR EMBL; BC008572; AAH08572.1; -; mRNA. DR EMBL; BC032122; AAH32122.1; -; mRNA. DR EMBL; BC050661; AAH50661.1; -; mRNA. DR PIR; A90807; HAHU. DR PIR; C93303; HACZP. DR PIR; I58217; HACZ. DR UniGene; Hs.449630; -. DR PDB; 1A00; X-ray; A/C=1-142. DR PDB; 1A01; X-ray; A/C=1-142. DR PDB; 1A0U; X-ray; A/C=1-142. DR PDB; 1A0Z; X-ray; A/C=1-142. DR PDB; 1A3N; X-ray; A/C=1-142. DR PDB; 1A3O; X-ray; A/C=1-142. DR PDB; 1A9W; X-ray; A/C=1-142. DR PDB; 1ABW; X-ray; A=1-142. DR PDB; 1ABY; X-ray; A=1-142. DR PDB; 1AJ9; X-ray; A=1-142. DR PDB; 1B86; X-ray; A/C=1-142. DR PDB; 1BAB; X-ray; A/C=3-142. DR PDB; 1BBB; X-ray; A/C=1-142. DR PDB; 1BIJ; X-ray; A/C=1-142. DR PDB; 1BUW; X-ray; A=1-142, C=-. DR PDB; 1BZ0; X-ray; A/C=1-142. DR PDB; 1BZ1; X-ray; A/C=1-142. DR PDB; 1BZZ; X-ray; A/C=3-142. DR PDB; 1C7B; X-ray; A/C=3-142. DR PDB; 1C7C; X-ray; A=1-142. DR PDB; 1C7D; X-ray; A=1-142. DR PDB; 1CLS; X-ray; A/C=1-142. DR PDB; 1CMY; X-ray; A/C=1-142. DR PDB; 1COH; X-ray; A/C=1-142. DR PDB; 1DKE; X-ray; A/C=1-142. DR PDB; 1DXT; X-ray; A/C=1-142. DR PDB; 1DXU; X-ray; A/C=1-142. DR PDB; 1DXV; X-ray; A/C=1-142. DR PDB; 1FDH; X-ray; A=1-142. DR PDB; 1FN3; X-ray; A/C=1-142. DR PDB; 1G9V; X-ray; A/C=1-142. DR PDB; 1GBU; X-ray; A/C=1-142. DR PDB; 1GBV; X-ray; A/C=1-142. DR PDB; 1GLI; X-ray; A/C=3-142. DR PDB; 1GZX; X-ray; A/C=1-142. DR PDB; 1HAB; X-ray; A/C=1-142. DR PDB; 1HAC; X-ray; A/C=1-142. DR PDB; 1HBA; X-ray; A/C=1-142. DR PDB; 1HBB; X-ray; A/C=1-142. DR PDB; 1HBS; X-ray; A/C/E/G=1-142. DR PDB; 1HCO; X-ray; A=1-142. DR PDB; 1HDB; X-ray; A/C=1-142. DR PDB; 1HGA; X-ray; A/C=1-142. DR PDB; 1HGB; X-ray; A/C=1-142. DR PDB; 1HGC; X-ray; A/C=1-142. DR PDB; 1HHO; X-ray; A=1-142. DR PDB; 1IRD; X-ray; A=1-142. DR PDB; 1J3Y; X-ray; A/C/E/G=1-142. DR PDB; 1J3Z; X-ray; A/C/E/G=1-142. DR PDB; 1J40; X-ray; A/C/E/G=1-142. DR PDB; 1J41; X-ray; A/C/E/G=1-142. DR PDB; 1J7S; X-ray; A/C=3-142. DR PDB; 1J7W; X-ray; A/C=3-142. DR PDB; 1J7Y; X-ray; A/C=3-142. DR PDB; 1JY7; X-ray; A/C/P/R/U/W=1-142. DR PDB; 1K0Y; X-ray; A/C=1-142. DR PDB; 1K1K; X-ray; A=1-142. DR PDB; 1KD2; X-ray; A/C=1-142. DR PDB; 1LFL; X-ray; A/C/P/R=-. DR PDB; 1LFQ; X-ray; A=-. DR PDB; 1LFT; X-ray; A=-. DR PDB; 1LFV; X-ray; A=-. DR PDB; 1LFY; X-ray; A=-. DR PDB; 1LFZ; X-ray; A=-. DR PDB; 1LJW; X-ray; A=1-142. DR PDB; 1M9P; X-ray; A/C=1-142. DR PDB; 1MKO; X-ray; A/C=1-142. DR PDB; 1NEJ; X-ray; A/C=1-142. DR PDB; 1NIH; X-ray; A/C=1-142. DR PDB; 1NQP; X-ray; A/C=1-142. DR PDB; 1O1I; X-ray; A=1-142. DR PDB; 1O1J; X-ray; A=1-142. DR PDB; 1O1K; X-ray; A/C=3-142. DR PDB; 1O1L; X-ray; A=1-142. DR PDB; 1O1M; X-ray; A=1-142. DR PDB; 1O1N; X-ray; A=1-142. DR PDB; 1O1O; X-ray; A/C=1-142. DR PDB; 1O1P; X-ray; A=1-142. DR PDB; 1QI8; X-ray; A/C=3-142. DR PDB; 1QSH; X-ray; A/C=1-142. DR PDB; 1QSI; X-ray; A/C=1-142. DR PDB; 1QXD; X-ray; A/C=1-142. DR PDB; 1QXE; X-ray; A/C=1-142. DR PDB; 1R1X; X-ray; A=1-142. DR PDB; 1R1Y; X-ray; A/C=1-142. DR PDB; 1RPS; X-ray; A/C=1-142. DR PDB; 1RQ3; X-ray; A/C=1-142. DR PDB; 1RQ4; X-ray; A/C=1-142. DR PDB; 1RQA; X-ray; A/C=1-142. DR PDB; 1RVW; X-ray; A=1-142. DR PDB; 1SDK; X-ray; A/C=1-142. DR PDB; 1SDL; X-ray; A/C=1-142. DR PDB; 1SHR; X-ray; A/C=1-142. DR PDB; 1SI4; X-ray; A/C=1-142. DR PDB; 1THB; X-ray; A/C=1-142. DR PDB; 1UIW; X-ray; A/C/E/G=1-142. DR PDB; 1VWT; X-ray; A/C=1-142. DR PDB; 1XXT; X-ray; A/C=1-142. DR PDB; 1XY0; X-ray; A/C=3-142. DR PDB; 1XYE; X-ray; A/C=3-142. DR PDB; 1XZ2; X-ray; A/C=1-142. DR PDB; 1XZ4; X-ray; A/C=3-142. DR PDB; 1XZ5; X-ray; A/C=3-142. DR PDB; 1XZ7; X-ray; A/C=3-142. DR PDB; 1XZU; X-ray; A/C=3-142. DR PDB; 1XZV; X-ray; A/C=3-142. DR PDB; 1Y01; X-ray; B=1-142. DR PDB; 1Y09; X-ray; A/C=3-142. DR PDB; 1Y0A; X-ray; A/C=3-142. DR PDB; 1Y0C; X-ray; A/C=3-142. DR PDB; 1Y0D; X-ray; A/C=1-141. DR PDB; 1Y0T; X-ray; A/C=1-142. DR PDB; 1Y0W; X-ray; A/C=1-142. DR PDB; 1Y22; X-ray; A/C=1-142. DR PDB; 1Y2Z; X-ray; A/C=1-142. DR PDB; 1Y31; X-ray; A/C=1-142. DR PDB; 1Y35; X-ray; A/C=1-142. DR PDB; 1Y45; X-ray; A/C=1-142. DR PDB; 1Y46; X-ray; A/C=1-142. DR PDB; 1Y4B; X-ray; A/C=1-142. DR PDB; 1Y4F; X-ray; A/C=1-142. DR PDB; 1Y4G; X-ray; A/C=1-142. DR PDB; 1Y4P; X-ray; A/C=1-142. DR PDB; 1Y4Q; X-ray; A/C=1-142. DR PDB; 1Y4R; X-ray; A/C=1-142. DR PDB; 1Y4V; X-ray; A/C=1-142. DR PDB; 1Y5F; X-ray; A/C=1-142. DR PDB; 1Y5J; X-ray; A/C=1-142. DR PDB; 1Y5K; X-ray; A/C=1-142. DR PDB; 1Y7C; X-ray; A/C=1-142. DR PDB; 1Y7D; X-ray; A/C=1-142. DR PDB; 1Y7G; X-ray; A/C=1-142. DR PDB; 1Y7Z; X-ray; A/C=1-142. DR PDB; 1Y83; X-ray; A/C=1-142. DR PDB; 1Y85; X-ray; A/C=1-142. DR PDB; 1Y8W; X-ray; A/C=3-142. DR PDB; 1YDZ; X-ray; A/C=3-142. DR PDB; 1YE0; X-ray; A/C=1-142. DR PDB; 1YE1; X-ray; A/C=1-142. DR PDB; 1YE2; X-ray; A/C=1-142. DR PDB; 1YEN; X-ray; A/C=1-142. DR PDB; 1YEO; X-ray; A/C=1-142. DR PDB; 1YEQ; X-ray; A/C=1-142. DR PDB; 1YEU; X-ray; A/C=1-142. DR PDB; 1YEV; X-ray; A/C=1-142. DR PDB; 1YFF; X-ray; A/C/E/G=1-142. DR PDB; 1YG5; X-ray; A/C=1-142. DR PDB; 1YGD; X-ray; A/C=1-142. DR PDB; 1YGF; X-ray; A/C=1-142. DR PDB; 1YH9; X-ray; A/C=1-142. DR PDB; 1YHE; X-ray; A/C=1-142. DR PDB; 1YHR; X-ray; A/C=1-142. DR PDB; 1YIE; X-ray; A/C=1-142. DR PDB; 1YIH; X-ray; A/C=1-142. DR PDB; 1YVQ; X-ray; A/C=1-142. DR PDB; 1YVT; X-ray; A=1-142. DR PDB; 1YZI; X-ray; A=1-142. DR PDB; 1Z8U; X-ray; B/D=1-142. DR PDB; 2D5Z; X-ray; A/C=1-142. DR PDB; 2D60; X-ray; A/C=1-142. DR PDB; 2DN1; X-ray; A=1-142. DR PDB; 2DN2; X-ray; A/C=1-142. DR PDB; 2DN3; X-ray; A=1-142. DR PDB; 2H35; NMR; A=1-142, C=-. DR PDB; 2HBC; X-ray; A=1-142. DR PDB; 2HBD; X-ray; A=1-142. DR PDB; 2HBE; X-ray; A=1-142. DR PDB; 2HBF; X-ray; A=1-142. DR PDB; 2HBS; X-ray; A/C/E/G=1-142. DR PDB; 2HCO; X-ray; A=1-142. DR PDB; 2HHD; X-ray; A/C=1-142. DR PDB; 2HHE; X-ray; A/C=1-142. DR PDB; 4HHB; X-ray; A/C=1-142. DR PDB; 6HBW; X-ray; A/C=1-142. DR IntAct; P69905; -. DR SWISS-2DPAGE; P69905; HUMAN. DR DOSAC-COBS-2DPAGE; P01922; HUMAN. DR DOSAC-COBS-2DPAGE; P69905; HUMAN. DR REPRODUCTION-2DPAGE; P69905; HUMAN. DR Siena-2DPAGE; P69905; -. DR Ensembl; ENSG00000188536; Homo sapiens. DR H-InvDB; HIX0023258; -. DR HGNC; HGNC:4823; HBA1. DR HGNC; HGNC:4824; HBA2. DR MIM; 141800; gene+phenotype. DR MIM; 141850; gene. DR MIM; 141860; gene. DR DrugBank; APRD00796; Amodiaquine. DR DrugBank; APRD00468; Chloroquine. DR DrugBank; APRD01053; Iron Dextran. DR DrugBank; APRD00300; Mefloquine. DR DrugBank; APRD00604; Primaquine. DR DrugBank; APRD00563; Quinine. DR LinkHub; P69905; -. DR GermOnline; ENSG00000188536; Homo sapiens. DR GermOnline; ENSG00000206172; Homo sapiens. DR RZPD-ProtExp; IOH7452; -. DR RZPD-ProtExp; M0373; -. DR RZPD-ProtExp; RZPDo834G076; -. DR RZPD-ProtExp; S0333; -. DR GO; GO:0005833; C:hemoglobin complex; TAS:UniProtKB. DR GO; GO:0005515; F:protein binding; TAS:UniProtKB. DR GO; GO:0015671; P:oxygen transport; TAS:UniProtKB. DR InterPro; IPR002338; Alpha_haem. DR InterPro; IPR000971; Globin. DR InterPro; IPR009050; Globin_like. DR InterPro; IPR012292; Globin_related. DR InterPro; IPR002339; Pi_haem. DR Gene3D; G3DSA:1.10.490.10; Globin_related; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00612; ALPHAHAEM. DR PRINTS; PR00815; PIHAEM. DR PROSITE; PS01033; GLOBIN; 1. KW 3D-structure; Acetylation; Direct protein sequencing; KW Disease mutation; Heme; Iron; Metal-binding; Oxygen transport; KW Polymorphism; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 142 Hemoglobin subunit alpha. FT /FTId=PRO_0000052653. FT METAL 59 59 Iron (heme distal ligand). FT METAL 88 88 Iron (heme proximal ligand). FT VARIANT 2 2 V -> E (in Thionville; O(2) affinity FT down). FT /FTId=VAR_002719. FT VARIANT 3 3 L -> R (in ChongQing; O(2) affinity up). FT /FTId=VAR_002720. FT VARIANT 6 6 A -> D (in J-Toronto). FT /FTId=VAR_002721. FT VARIANT 6 6 A -> P (in Karachi). FT /FTId=VAR_002722. FT VARIANT 7 7 D -> A (in Sawara; O(2) affinity up). FT /FTId=VAR_002723. FT VARIANT 7 7 D -> G (in Swan River). FT /FTId=VAR_002724. FT VARIANT 7 7 D -> N (in Dunn; O(2) affinity up). FT /FTId=VAR_002725. FT VARIANT 7 7 D -> V (in Ferndown; O(2) affinity up). FT /FTId=VAR_002726. FT VARIANT 7 7 D -> Y (in Woodville; O(2) affinity up). FT /FTId=VAR_002727. FT VARIANT 8 8 K -> E (in Kurosaki). FT /FTId=VAR_002728. FT VARIANT 11 11 V -> F (in dbSNP:rs1799896). FT /FTId=VAR_014605. FT VARIANT 12 12 K -> E (in Anantharaj). FT /FTId=VAR_002729. FT VARIANT 13 13 A -> D (in J-Paris 1/J-Aljezur). FT /FTId=VAR_002730. FT VARIANT 15 15 W -> R (in Evanston; O(2) affinity up). FT /FTId=VAR_002731. FT VARIANT 16 16 G -> R (in Ottawa/Siam). FT /FTId=VAR_002732. FT VARIANT 17 17 K -> M (in Harbin; slightly unstable). FT /FTId=VAR_002733. FT VARIANT 17 17 K -> N (in Beijing). FT /FTId=VAR_002734. FT VARIANT 19 19 G -> D (in Al-Ain Abu Dhabi). FT /FTId=VAR_002735. FT VARIANT 19 19 G -> R (in Handsworth). FT /FTId=VAR_002736. FT VARIANT 20 20 A -> D (in J-Kurosh). FT /FTId=VAR_002737. FT VARIANT 20 20 A -> E (in J-Tashikuergan). FT /FTId=VAR_002738. FT VARIANT 21 21 H -> Q (in Le Lamentin). FT /FTId=VAR_002739. FT VARIANT 21 21 H -> R (in Hobart). FT /FTId=VAR_002740. FT VARIANT 22 22 A -> D (in J-Nyanza). FT /FTId=VAR_002741. FT VARIANT 22 22 A -> P (in Fontainebleau). FT /FTId=VAR_002742. FT VARIANT 23 23 G -> D (in J-Medellin). FT /FTId=VAR_002743. FT VARIANT 24 24 E -> G (in Reims; slightly unstable). FT /FTId=VAR_002744. FT VARIANT 24 24 E -> K (in Chad). FT /FTId=VAR_002745. FT VARIANT 25 25 Y -> H (in Luxembourg; unstable). FT /FTId=VAR_002746. FT VARIANT 27 27 A -> E (in Shenyang; unstable). FT /FTId=VAR_002747. FT VARIANT 27 27 A -> V (in Campinas). FT /FTId=VAR_025387. FT VARIANT 28 28 E -> D (in Hekinan). FT /FTId=VAR_002748. FT VARIANT 28 28 E -> G (in Fort Worth). FT /FTId=VAR_002749. FT VARIANT 28 28 E -> V (in Spanish town). FT /FTId=VAR_002750. FT VARIANT 31 31 E -> K (in O-Padova). FT /FTId=VAR_002751. FT VARIANT 32 32 R -> K (causes alpha-thalassemia). FT /FTId=VAR_025002. FT VARIANT 32 32 R -> S (in Prato; unstable). FT /FTId=VAR_002752. FT VARIANT 35 35 L -> R (in Queens/Ogi). FT /FTId=VAR_002753. FT VARIANT 38 38 P -> PE (in Catonsville). FT /FTId=VAR_002755. FT VARIANT 38 38 P -> R (in Bourmedes). FT /FTId=VAR_002754. FT VARIANT 41 41 K -> M (in Kanagawa; O(2) affinity up). FT /FTId=VAR_002756. FT VARIANT 42 42 T -> S (in Miyano; O(2) affinity up). FT /FTId=VAR_002757. FT VARIANT 44 44 F -> L (in Hirosaki; unstable). FT /FTId=VAR_002758. FT VARIANT 45 45 P -> L (in Milledgeville; O(2) affinity FT up). FT /FTId=VAR_002759. FT VARIANT 45 45 P -> R (in Kawachi; O(2) affinity up). FT /FTId=VAR_002760. FT VARIANT 46 46 H -> Q (in Bari). FT /FTId=VAR_002761. FT VARIANT 46 46 H -> R (in Fort de France; O(2) affinity FT up). FT /FTId=VAR_002762. FT VARIANT 48 48 D -> A (in Cordele; unstable). FT /FTId=VAR_002763. FT VARIANT 48 48 D -> G (in Umi/Michigan; unstable). FT /FTId=VAR_002764. FT VARIANT 48 48 D -> H (in Hasharon/Sinai; unstable). FT /FTId=VAR_002765. FT VARIANT 48 48 D -> Y (in Kurdistan). FT /FTId=VAR_002766. FT VARIANT 49 49 L -> R (in Montgomery). FT /FTId=VAR_002767. FT VARIANT 50 50 S -> R (in Savaria). FT /FTId=VAR_002768. FT VARIANT 51 51 H -> R (in Aichi; slightly unstable). FT /FTId=VAR_002769. FT VARIANT 52 52 G -> D (in J-Abidjan). FT /FTId=VAR_002770. FT VARIANT 52 52 G -> R (in Russ). FT /FTId=VAR_002771. FT VARIANT 54 54 A -> D (in J-Rovigo; unstable). FT /FTId=VAR_002772. FT VARIANT 55 55 Q -> R (in Hikoshima/Shimonoseki). FT /FTId=VAR_002773. FT VARIANT 57 57 K -> R (in Port Huron). FT /FTId=VAR_002774. FT VARIANT 57 57 K -> T (in Thailand). FT /FTId=VAR_002775. FT VARIANT 58 58 G -> R (in L-Persian Gulf). FT /FTId=VAR_002776. FT VARIANT 59 59 H -> Q (in Boghe). FT /FTId=VAR_025388. FT VARIANT 59 59 H -> Y (in M-Boston/M-Osaka; O(2) FT affinity down). FT /FTId=VAR_002777. FT VARIANT 60 60 G -> D (in Adana; unstable; causes alpha- FT thalassemia; dbSNP:rs28928878). FT /FTId=VAR_002778. FT VARIANT 60 60 G -> V (in Tottori; unstable). FT /FTId=VAR_002779. FT VARIANT 61 61 K -> N (in Zambia; dbSNP:rs28928887). FT /FTId=VAR_002780. FT VARIANT 61 61 Missing (in Clinic; unstable; causes FT alpha-thalassemia). FT /FTId=VAR_002781. FT VARIANT 62 62 K -> N (in J-Buda). FT /FTId=VAR_002782. FT VARIANT 62 62 K -> T (in J-Anatolia). FT /FTId=VAR_002783. FT VARIANT 63 63 V -> M (in Evans; unstable). FT /FTId=VAR_002784. FT VARIANT 64 64 A -> D (in Pontoise; unstable). FT /FTId=VAR_002785. FT VARIANT 65 65 D -> Y (in Persepolis). FT /FTId=VAR_002786. FT VARIANT 69 69 N -> K (in G-Philadelphia; FT dbSNP:rs1060339). FT /FTId=VAR_002787. FT VARIANT 72 72 A -> E (in J-Habana). FT /FTId=VAR_002788. FT VARIANT 72 72 A -> V (in Ozieri). FT /FTId=VAR_002789. FT VARIANT 73 73 H -> R (in Daneskgah-Teheran). FT /FTId=VAR_002790. FT VARIANT 75 75 D -> A (in Lille). FT /FTId=VAR_002791. FT VARIANT 75 75 D -> G (in Chapel Hill). FT /FTId=VAR_002792. FT VARIANT 75 75 D -> N (in G-Pest). FT /FTId=VAR_002793. FT VARIANT 76 76 D -> A (in Duan). FT /FTId=VAR_002794. FT VARIANT 76 76 D -> H (in Q-Iran). FT /FTId=VAR_002795. FT VARIANT 77 77 M -> K (in Noko). FT /FTId=VAR_002796. FT VARIANT 77 77 M -> T (in Aztec). FT /FTId=VAR_002797. FT VARIANT 78 78 P -> R (in Guizhou). FT /FTId=VAR_002798. FT VARIANT 79 79 N -> H (in Davenport). FT /FTId=VAR_002799. FT VARIANT 79 79 N -> K (in Stanleyville-2). FT /FTId=VAR_002800. FT VARIANT 80 80 A -> G (in Singapore). FT /FTId=VAR_012662. FT VARIANT 81 81 L -> R (in Ann Arbor; unstable). FT /FTId=VAR_002801. FT VARIANT 82 82 S -> C (in Nigeria). FT /FTId=VAR_002802. FT VARIANT 83 83 A -> D (in Garden State). FT /FTId=VAR_002803. FT VARIANT 85 85 S -> R (in Etobicoke; O(2) affinity up). FT /FTId=VAR_002804. FT VARIANT 86 86 D -> V (in Inkster; O(2) affinity up). FT /FTId=VAR_002805. FT VARIANT 86 86 D -> Y (in Atago; O(2) affinity up). FT /FTId=VAR_002806. FT VARIANT 87 87 L -> R (in Moabit; unstable). FT /FTId=VAR_002807. FT VARIANT 88 88 H -> N (in Auckland; unstable). FT /FTId=VAR_002808. FT VARIANT 88 88 H -> R (in Iwata; unstable). FT /FTId=VAR_002809. FT VARIANT 89 89 A -> S (in Loire; O(2) affinity up). FT /FTId=VAR_002810. FT VARIANT 91 91 K -> M (in Handa; O(2) affinity up). FT /FTId=VAR_002811. FT VARIANT 92 92 L -> P (in Port Phillip; unstable; FT dbSNP:rs17407508). FT /FTId=VAR_002812. FT VARIANT 93 93 R -> Q (in J-Cape Town; O(2) affinity FT up). FT /FTId=VAR_002813. FT VARIANT 93 93 R -> W (in Cemenelum; O(2) affinity up). FT /FTId=VAR_020775. FT VARIANT 95 95 D -> A (in Bassett; markedly reduced FT oxygen affinity). FT /FTId=VAR_025389. FT VARIANT 95 95 D -> Y (in Setif; unstable). FT /FTId=VAR_002814. FT VARIANT 96 96 P -> A (in Denmark Hill; O(2) affinity FT up). FT /FTId=VAR_002815. FT VARIANT 96 96 P -> T (in Godavari; O(2) affinity up). FT /FTId=VAR_002816. FT VARIANT 98 98 N -> K (in Dallas; O(2) affinity up). FT /FTId=VAR_002817. FT VARIANT 100 100 K -> E (in Turriff). FT /FTId=VAR_002818. FT VARIANT 103 103 S -> R (in Manitoba; slightly unstable). FT /FTId=VAR_002819. FT VARIANT 104 104 H -> R (in Contaldo; unstable). FT /FTId=VAR_002820. FT VARIANT 104 104 H -> Y (in Charolles). FT /FTId=VAR_025390. FT VARIANT 110 110 L -> R (in Suan-Dok; unstable; causes FT alpha-thalassemia). FT /FTId=VAR_002821. FT VARIANT 111 111 A -> D (in Petah Tikva; unstable; causes FT alpha-thalassemia). FT /FTId=VAR_002822. FT VARIANT 113 113 H -> D (in Hopkins-II; unstable). FT /FTId=VAR_002823. FT VARIANT 114 114 L -> H (in Twin Peaks). FT /FTId=VAR_002824. FT VARIANT 115 115 P -> L (in Nouakchott). FT /FTId=VAR_002825. FT VARIANT 115 115 P -> R (in Chiapas). FT /FTId=VAR_002826. FT VARIANT 115 115 P -> S (in Melusine). FT /FTId=VAR_002827. FT VARIANT 116 116 A -> D (in J-Tongariki). FT /FTId=VAR_002828. FT VARIANT 117 117 E -> A (in Ube-4). FT /FTId=VAR_002829. FT VARIANT 117 117 E -> EHLPAE (in Zaire). FT /FTId=VAR_002830. FT VARIANT 118 118 F -> FI (in Phnom Penh). FT /FTId=VAR_002831. FT VARIANT 119 119 T -> TEFT (in Grady). FT /FTId=VAR_002832. FT VARIANT 121 121 A -> E (in J-Meerut/J-Birmingham). FT /FTId=VAR_002833. FT VARIANT 122 122 V -> M (in Owari). FT /FTId=VAR_002834. FT VARIANT 123 123 H -> Q (in Westmead). FT /FTId=VAR_002835. FT VARIANT 126 126 L -> P (in Quong Sze; causes alpha- FT thalassemia). FT /FTId=VAR_002836. FT VARIANT 126 126 L -> R (in Plasencia; family with FT moderate microcytosis and hypochromia). FT /FTId=VAR_025391. FT VARIANT 127 127 D -> G (in West One). FT /FTId=VAR_025392. FT VARIANT 127 127 D -> V (in Fukutomi; O(2) affinity up). FT /FTId=VAR_002837. FT VARIANT 127 127 D -> Y (in Monteriore; O(2) affinity up). FT /FTId=VAR_002838. FT VARIANT 128 128 K -> N (in Jackson). FT /FTId=VAR_002839. FT VARIANT 130 130 L -> P (in Tunis-Bizerte; unstable; FT causes alpha-thalassemia). FT /FTId=VAR_002840. FT VARIANT 131 131 A -> D (in Yuda; O(2) affinity down). FT /FTId=VAR_002842. FT VARIANT 131 131 A -> P (in Sun Prairie; unstable). FT /FTId=VAR_002841. FT VARIANT 132 132 S -> P (in Questembert; highly unstable; FT causes alpha-thalassemia). FT /FTId=VAR_002843. FT VARIANT 134 134 S -> R (in Val de Marne; O(2) affinity FT up). FT /FTId=VAR_002844. FT VARIANT 136 136 V -> E (in Pavie). FT /FTId=VAR_002845. FT VARIANT 137 137 L -> M (in Chicago). FT /FTId=VAR_002846. FT VARIANT 137 137 L -> P (in Bibba; unstable; causes alpha- FT thalassemia). FT /FTId=VAR_002847. FT VARIANT 139 139 S -> P (in Attleboro; O(2) affinity up). FT /FTId=VAR_002848. FT VARIANT 140 140 K -> E (in Hanamaki; O(2) affinity up). FT /FTId=VAR_002849. FT VARIANT 140 140 K -> T (in Tokoname; O(2) affinity up). FT /FTId=VAR_002850. FT VARIANT 141 141 Y -> H (in Rouen; O(2) affinity up). FT /FTId=VAR_002851. FT VARIANT 142 142 R -> C (in Nunobiki; O(2) affinity up). FT /FTId=VAR_002852. FT VARIANT 142 142 R -> H (in Suresnes; O(2) affinity up). FT /FTId=VAR_002854. FT VARIANT 142 142 R -> L (in Legnano; O(2) affinity up). FT /FTId=VAR_002853. FT VARIANT 142 142 R -> P (in Singapore). FT /FTId=VAR_002855. FT HELIX 4 15 FT HELIX 16 20 FT HELIX 21 35 FT HELIX 37 42 FT HELIX 53 71 FT HELIX 73 75 FT HELIX 76 79 FT HELIX 81 89 FT HELIX 96 112 FT TURN 114 116 FT HELIX 119 136 FT TURN 137 139 SQ SEQUENCE 142 AA; 15258 MW; 15E13666573BBBAE CRC64; MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP AVHASLDKFL ASVSTVLTSK YR // ID HBA_PANPA Reviewed; 142 AA. AC P69906; P01922; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 20. DE Hemoglobin subunit alpha (Hemoglobin alpha chain) (Alpha-globin). GN Name=HBA1; GN and GN Name=HBA2; OS Pan paniscus (Pygmy chimpanzee) (Bonobo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9597; RN [1] RP PROTEIN SEQUENCE OF 2-142. RX MEDLINE=83219265; PubMed=6406908; DOI=10.1038/303546a0; RA Goodman M., Braunitzer G., Stangl A., Schrank B.; RT "Evidence on human origins from haemoglobins of African apes."; RL Nature 303:546-548(1983). CC -!- FUNCTION: Involved in oxygen transport from the lung to the CC various peripheral tissues. CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in CC adult hemoglobin A (HbA); two alpha chains and two delta chains in CC adult hemoglobin A2 (HbA2); two alpha chains and two epsilon CC chains in early embryonic hemoglobin Gower-2; two alpha chains and CC two gamma chains in fetal hemoglobin F (HbF). CC -!- TISSUE SPECIFICITY: Red blood cells. CC -!- MISCELLANEOUS: Gives blood its red color. CC -!- SIMILARITY: Belongs to the globin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; C93303; HACZP. DR SMR; P69906; 2-142. DR InterPro; IPR002338; Alpha_haem. DR InterPro; IPR000971; Globin. DR InterPro; IPR009050; Globin_like. DR InterPro; IPR012292; Globin_related. DR InterPro; IPR002339; Pi_haem. DR Gene3D; G3DSA:1.10.490.10; Globin_related; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00612; ALPHAHAEM. DR PRINTS; PR00815; PIHAEM. DR PROSITE; PS01033; GLOBIN; 1. KW Direct protein sequencing; Heme; Iron; Metal-binding; KW Oxygen transport; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 142 Hemoglobin subunit alpha. FT /FTId=PRO_0000052717. FT METAL 59 59 Iron (heme distal ligand). FT METAL 88 88 Iron (heme proximal ligand). SQ SEQUENCE 142 AA; 15258 MW; 15E13666573BBBAE CRC64; MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP AVHASLDKFL ASVSTVLTSK YR // ID HBA_PANTR Reviewed; 142 AA. AC P69907; P01922; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 20-FEB-2007, entry version 25. DE Hemoglobin subunit alpha (Hemoglobin alpha chain) (Alpha-globin). GN Name=HBA1; GN and GN Name=HBA2; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=84169526; PubMed=6689503; DOI=10.1093/nar/11.24.8915; RA Liebhaber S.A., Begley K.A.; RT "Structural and evolutionary analysis of the two chimpanzee alpha- RT globin mRNAs."; RL Nucleic Acids Res. 11:8915-8929(1983). RN [2] RP PROTEIN SEQUENCE OF 2-142. RX MEDLINE=66071496; PubMed=5855051; RA Rifkin D.B., Konigsberg W.; RT "The characterization of the tryptic peptides from the hemoglobin of RT the chimpanzee (Pan troglodytes)."; RL Biochim. Biophys. Acta 104:457-461(1965). RN [3] RP PROTEIN SEQUENCE OF 2-142. RX MEDLINE=83219265; PubMed=6406908; DOI=10.1038/303546a0; RA Goodman M., Braunitzer G., Stangl A., Schrank B.; RT "Evidence on human origins from haemoglobins of African apes."; RL Nature 303:546-548(1983). CC -!- FUNCTION: Involved in oxygen transport from the lung to the CC various peripheral tissues. CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in CC adult hemoglobin A (HbA); two alpha chains and two delta chains in CC adult hemoglobin A2 (HbA2); two alpha chains and two epsilon CC chains in early embryonic hemoglobin Gower-2; two alpha chains and CC two gamma chains in fetal hemoglobin F (HbF). CC -!- TISSUE SPECIFICITY: Red blood cells. CC -!- MISCELLANEOUS: Gives blood its red color. CC -!- SIMILARITY: Belongs to the globin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X00226; CAA25044.1; -; mRNA. DR EMBL; X00227; CAA25045.1; -; mRNA. DR PIR; I58217; HACZ. DR SMR; P69907; 2-142. DR KEGG; hsa:3039; -. DR KEGG; hsa:3040; -. DR InterPro; IPR002338; Alpha_haem. DR InterPro; IPR000971; Globin. DR InterPro; IPR009050; Globin_like. DR InterPro; IPR012292; Globin_related. DR InterPro; IPR002339; Pi_haem. DR Gene3D; G3DSA:1.10.490.10; Globin_related; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00612; ALPHAHAEM. DR PRINTS; PR00815; PIHAEM. DR PROSITE; PS01033; GLOBIN; 1. KW Direct protein sequencing; Heme; Iron; Metal-binding; KW Oxygen transport; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 142 Hemoglobin subunit alpha. FT /FTId=PRO_0000052720. FT METAL 59 59 Iron (heme distal ligand). FT METAL 88 88 Iron (heme proximal ligand). SQ SEQUENCE 142 AA; 15258 MW; 15E13666573BBBAE CRC64; MVLSPADKTN VKAAWGKVGA HAGEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG KKVADALTNA VAHVDDMPNA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL AAHLPAEFTP AVHASLDKFL ASVSTVLTSK YR // ID HBB_HUMAN Reviewed; 147 AA. AC P68871; P02023; Q13852; Q14481; Q14510; Q45KT0; Q6FI08; Q8IZI1; AC Q9BX96; Q9UCP8; Q9UCP9; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 20-MAR-2007, entry version 43. DE Hemoglobin subunit beta (Hemoglobin beta chain) (Beta-globin). GN Name=HBB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=81064667; PubMed=6254664; DOI=10.1016/0092-8674(80)90428-6; RA Lawn R.M., Efstratiadis A., O'Connell C., Maniatis T.; RT "The nucleotide sequence of the human beta-globin gene."; RL Cell 21:647-651(1980). RN [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=77126403; PubMed=1019344; RA Marotta C., Forget B., Cohen-Solal M., Weissman S.M.; RT "Nucleotide sequence analysis of coding and noncoding regions of human RT beta-globin mRNA."; RL Prog. Nucleic Acid Res. Mol. Biol. 19:165-175(1976). RN [3] RP NUCLEOTIDE SEQUENCE. RA Lu L., Hu Z.H., Du C.S., Fu Y.S.; RT "DNA sequence of the human beta-globin gene isolated from a healthy RT Chinese."; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE, AND VARIANT DURHAM-N.C. PRO-115. RC TISSUE=Blood; RA Kutlar F., Abboud M., Leithner C., Holley L., Brisco J., Kutlar A.; RT "Electrophoretically silent, very unstable, thalassemic mutation at RT codon 114 of beta globin (hemoglobin Durham-N.C.) detected by cDNA RT sequencing of mRNA, from a Russian women."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE, AND VARIANT LOUISVILLE LEU-43. RC TISSUE=Blood; RA Kutlar F., Harbin J., Brisco J., Kutlar A.; RT "Rapid detection of electrophoretically silent, unstable human RT hemoglobin 'Louisville', (Beta; Phe 42 Leu/TTT to CTT) by cDNA RT sequencing of mRNA."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE, AND VARIANT TY GARD GLN-125. RC TISSUE=Blood; RA Kutlar F., Holley L., Leithner C., Kutlar A.; RT "A rare beta chain variant 'Hemoglobin Ty Gard:Pro 124 Gln' found in a RT Caucasian female with erythrocytosis."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kutlar A., Vercellotti G.M., Glendenning M., Holley L., Elam D., RA Kutlar F.; RT "Heterozygote C->A beta-thalassemia mutation at the intron-2/848 RT nucleotide of beta globin gene was detected on a Northern European RT (Caucasian) individual."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-7 AND SER-140. RC TISSUE=Blood; RA Kutlar F., Lallinger R.R., Holley L., Glendenning M., Kutlar A.; RT "A new hemoglobin, beta chain variant 'Hb S-Wake' confirmed to be on RT the same chromosome with hemoglobin S mutation, detected in an RT African-American family."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE, AND VARIANT O-ARAB. RC TISSUE=Blood; RA Kutlar F., Elam D., Glendenning M., Kutlar A., Dincol G.; RT "Coexistence of the hemoglobin O-Arab (Glu 121 Lys) and beta- RT thalassemia (intron-2; nucleotide 745 C->G) was detected in a Turkish RT patient."; RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Li W.J.; RT "Thalassaemic trait cause by C-T substitution at position -90 in RT proximal CACCC box of beta-globin gene in China family."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-7. RX PubMed=16175509; DOI=10.1086/491748; RA Wood E.T., Stover D.A., Slatkin M., Nachman M.W., Hammer M.F.; RT "The beta-globin recombinational hotspot reduces the effects of strong RT selection around HbC, a recently arisen mutation providing resistance RT to malaria."; RL Am. J. Hum. Genet. 77:637-642(2005). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., RA Korn B., Zuo D., Hu Y., LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [14] RP PROTEIN SEQUENCE OF 2-147. RX PubMed=13872627; RA Braunitzer G., Gehring-Muller R., Hilschmann N., Hilse K., Hobom G., RA Rudloff V., Wittmann-Liebold B.; RT "The constitution of normal adult human haemoglobin."; RL Hoppe-Seyler's Z. Physiol. Chem. 325:283-286(1961). RN [15] RP NUCLEOTIDE SEQUENCE OF 122-147. RX MEDLINE=85205333; PubMed=2581851; DOI=10.1016/0378-1119(85)90093-9; RA Lang K.M., Spritz R.A.; RT "Cloning specific complete polyadenylylated 3'-terminal cDNA RT segments."; RL Gene 33:191-196(1985). RN [16] RP ACETYLATION AT LYS-145. RX PubMed=4531009; RA Shamsuddin M., Mason R.G., Ritchey J.M., Honig G.R., Klotz I.M.; RT "Sites of acetylation of sickle cell hemoglobin by aspirin."; RL Proc. Natl. Acad. Sci. U.S.A. 71:4693-4697(1974). RN [17] RP INTERACTION WITH HAPTOGLOBIN. RX MEDLINE=86242088; PubMed=3718478; RA Yoshioka N., Atassi M.Z.; RT "Haemoglobin binding with haptoglobin. Localization of the RT haptoglobin-binding sites on the beta-chain of human haemoglobin by RT synthetic overlapping peptides encompassing the entire chain."; RL Biochem. J. 234:453-456(1986). RN [18] RP GLYCATION AT VAL-2. RX MEDLINE=78138698; PubMed=635569; RA Bunn H.F., Gabbay K.H., Gallop P.M.; RT "The glycosylation of hemoglobin: relevance to diabetes mellitus."; RL Science 200:21-27(1978). RN [19] RP NITRIC OXIDE-BINDING. RX MEDLINE=20056222; PubMed=10588683; DOI=10.1073/pnas.96.25.14206; RA Durner J., Gow A.J., Stamler J.S., Glazebrook J.; RT "Ancient origins of nitric oxide signaling in biological systems."; RL Proc. Natl. Acad. Sci. U.S.A. 96:14206-14207(1999). RN [20] RP S-NITROSYLATION AT CYS-94. RX MEDLINE=99060083; PubMed=9843411; DOI=10.1021/bi9816711; RA Chan N.L., Rogers P.H., Arnone A.; RT "Crystal structure of the S-nitroso form of liganded human RT hemoglobin."; RL Biochemistry 37:16459-16464(1998). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-145, AND MASS SPECTROMETRY. RX PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026; RA Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., RA Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; RT "Substrate and functional diversity of lysine acetylation revealed by RT a proteomics survey."; RL Mol. Cell 23:607-618(2006). RN [22] RP ELECTRON MICROSCOPY OF SICKLE-CELL HEMOGLOBIN FIBERS. RX PubMed=4123689; RA Finch J.T., Perutz M.F., Bertles J.F., Doebler J.; RT "Structure of sickled erythrocytes and of sickle-cell hemoglobin RT fibers."; RL Proc. Natl. Acad. Sci. U.S.A. 70:718-722(1973). RN [23] RP X-RAY CRYSTALLOGRAPHY (5 ANGSTROMS) OF MUTANT VAL-7. RX PubMed=1195378; DOI=10.1016/S0022-2836(75)80108-2; RA Wishner B.C., Ward K.B., Lattman E.E., Love W.E.; RT "Crystal structure of sickle-cell deoxyhemoglobin at 5 A resolution."; RL J. Mol. Biol. 98:179-194(1975). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF DEOXYHEMOGLOBIN. RX MEDLINE=76027820; PubMed=1177322; DOI=10.1016/S0022-2836(75)80037-4; RA Fermi G.; RT "Three-dimensional fourier synthesis of human deoxyhaemoglobin at 2.5- RT A resolution: refinement of the atomic model."; RL J. Mol. Biol. 97:237-256(1975). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF CARBONMONOXY HEMOGLOBIN. RX PubMed=7373648; DOI=10.1016/0022-2836(80)90308-3; RA Baldwin J.M.; RT "The structure of human carbonmonoxy haemoglobin at 2.7-A RT resolution."; RL J. Mol. Biol. 136:103-128(1980). RN [26] RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF DEOXYHEMOGLOBIN. RX PubMed=6726807; DOI=10.1016/0022-2836(84)90472-8; RA Fermi G., Perutz M.F., Shaanan B., Fourme R.; RT "The crystal structure of human deoxyhaemoglobin at 1.74 A RT resolution."; RL J. Mol. Biol. 175:159-174(1984). RN [27] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT ROTHSCHILD ARG-38. RX MEDLINE=92232710; PubMed=1567857; DOI=10.1021/bi00131a030; RA Kavanaugh J.S., Rogers P.H., Case D.A., Arnone A.; RT "High-resolution X-ray study of deoxyhemoglobin Rothschild 37 beta RT Trp-->Arg: a mutation that creates an intersubunit chloride-binding RT site."; RL Biochemistry 31:4111-4121(1992). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ARG-75. RX PubMed=1507231; DOI=10.1016/0022-2836(92)90638-Z; RA Fermi G., Perutz M.F., Williamson D., Stein P., Shih D.T.; RT "Structure-function relationships in the low-affinity mutant RT haemoglobin Aalborg (Gly74 (E18)beta-->Arg)."; RL J. Mol. Biol. 226:883-888(1992). RN [29] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX PubMed=8642597; DOI=10.1006/jmbi.1996.0124; RA Paoli M., Liddington R., Tame J., Wilkinson A., Dodson G.; RT "Crystal structure of T state haemoglobin with oxygen bound at all RT four haems."; RL J. Mol. Biol. 256:775-792(1996). RN [30] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS ALA-38; GLU-38; RP GLY-38 AND TYR-38. RX PubMed=9521756; DOI=10.1021/bi9708702; RA Kavanaugh J.S., Weydert J.A., Rogers P.H., Arnone A.; RT "High-resolution crystal structures of human hemoglobin with mutations RT at tryptophan 37beta: structural basis for a high-affinity T-state."; RL Biochemistry 37:4358-4373(1998). RN [31] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT TRP-7. RX PubMed=9830011; DOI=10.1074/jbc.273.49.32690; RA Harrington D.J., Adachi K., Royer W.E. Jr.; RT "Crystal structure of deoxy-human hemoglobin beta6 Glu-->Trp. RT Implications for the structure and formation of the sickle cell RT fiber."; RL J. Biol. Chem. 273:32690-32696(1998). RN [32] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT LYS-7. RX PubMed=12454462; DOI=10.1107/S0907444902016426; RA Dewan J.C., Feeling-Taylor A., Puius Y.A., Patskovska L., RA Patskovsky Y., Nagel R.L., Almo S.C., Hirsch R.E.; RT "Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A RT resolution."; RL Acta Crystallogr. D 58:2038-2042(2002). RN [33] RP VARIANT ALABAMA LYS-40. RX MEDLINE=75109326; PubMed=1115799; RA Brimhall B., Jones R.T., Schneider R.G., Hosty T.S., Tomlin G., RA Atkins R.; RT "Two new hemoglobins. Hemoglobin Alabama (beta39(C5)Gln leads to Lys) RT and hemoglobin Montgomery (alpha 48(CD 6) Leu leads to Arg)."; RL Biochim. Biophys. Acta 379:28-32(1975). RN [34] RP VARIANT ALESHA MET-68. RX MEDLINE=93322192; PubMed=8330974; RA Molchanova T.P., Postnikov Y.V., Pobedimskaya D.D., Smetanina N.S., RA Moschan A.A., Kazanetz E.G., Tokarev Y.N., Huisman T.H.J.; RT "Hb Alesha or alpha 2 beta (2)67(E11)Val-->Met: a new unstable RT hemoglobin variant identified through sequencing of amplified DNA."; RL Hemoglobin 17:217-225(1993). RN [35] RP VARIANT J-ALTGELDS GARDENS ASP-93. RX MEDLINE=79067354; PubMed=721609; RA Adams J.G. III, Przywara K.P., Heller P., Shamsuddin M.; RT "Hemoglobin J Altgeld Gardens. A hemoglobin variant with a RT substitution of the proximal histidine of the beta-chain."; RL Hemoglobin 2:403-415(1978). RN [36] RP VARIANT ANKARA ASP-11. RX MEDLINE=74297498; PubMed=4850241; DOI=10.1016/0014-5793(74)80766-0; RA Arcasoy A., Casey R., Lehmann H., Cavdar A.O., Berki A.; RT "A new haemoglobin J from Turkey -- Hb Ankara (beta10 (A7) Ala-Asp)."; RL FEBS Lett. 42:121-123(1974). RN [37] RP VARIANTS J-ANTAKYA MET-66 AND COMPLUTENSE GLU-128. RX MEDLINE=86216227; PubMed=3707969; DOI=10.1016/0167-4838(86)90178-0; RA Huisman T.H.J., Wilson J.B., Kutlar A., Yang K.-G., Chen S.-S., RA Webber B.B., Altay C., Martinez A.V.; RT "Hb J-Antakya or alpha 2 beta (2)65(E9)Lys-->Met in a Turkish family RT and Hb complutense or alpha 2 beta (2)127(H5)Gln-->Glu in a Spanish RT family; correction of a previously published identification."; RL Biochim. Biophys. Acta 871:229-231(1986). RN [38] RP VARIANT J-AUCKLAND ASP-26. RX MEDLINE=88006903; PubMed=3654265; RA Williamson D., Wells R.M.G., Anderson R., Matthews J.; RT "A new unstable and low oxygen affinity hemoglobin variant: Hb J- RT Auckland [beta 25(B7)Gly-->Asp]."; RL Hemoglobin 11:221-230(1987). RN [39] RP VARIANT AURORA TYR-140. RX MEDLINE=96352910; PubMed=8718692; RA Lafferty J., Ali M., Matthew K., Eng B., Patterson M., Waye J.S.; RT "Identification of a new high oxygen affinity hemoglobin variant: Hb RT Aurora [beta 139(H17) Asn-->Tyr]."; RL Hemoglobin 19:335-341(1995). RN [40] RP VARIANT BREST LYS-128. RX MEDLINE=88256755; PubMed=3384710; RA Baudin-Chich V., Wajcman H., Gombaud-Saintonge G., Arous N., Riou J., RA Briere J., Galacteros F.; RT "Hemoglobin Brest [beta 127 (H5)Gln-->Lys] a new unstable human RT hemoglobin variant located at the alpha 1 beta 1 interface with RT specific electrophoretic behavior."; RL Hemoglobin 12:179-188(1988). RN [41] RP VARIANT BRISBANE HIS-69. RX MEDLINE=81239159; PubMed=6166590; RA Brennan S.O., Wells R.M., Smith H., Carrell R.W.; RT "Hemoglobin Brisbane: beta68 Leu replaced by His. A new high oxygen RT affinity variant."; RL Hemoglobin 5:325-335(1981). RN [42] RP VARIANT BUNBURY ASN-95. RX MEDLINE=84031649; PubMed=6629823; RA Como P.F., Kennett D., Wilkinson T., Kronenberg H.; RT "A new hemoglobin with high oxygen affinity -- hemoglobin Bunbury: RT alpha 2 beta 2 [94 (FG1) Asp replaced by Asn]."; RL Hemoglobin 7:413-421(1983). RN [43] RP VARIANT J-CAIRO GLN-66. RX MEDLINE=76114933; PubMed=1247583; RA Garel M.-C., Hassan W., Coquelet M.T., Goossens M., Rosa J., Arous N.; RT "Hemoglobin J Cairo: beta 65 (E9) Lys leads to Gln, A new hemoglobin RT variant discovered in an Egyptian family."; RL Biochim. Biophys. Acta 420:97-104(1976). RN [44] RP VARIANT CAMPERDOWN SER-105. RX MEDLINE=75184109; PubMed=1138922; RA Wilkinson T., Chua C.G., Carrell R.W., Robin H., Exner T., Lee K.M., RA Kronenberg H.; RT "A new haemoglobin variant, haemoglobin Camperdown (beta 104 (G6) RT arginine->serine)."; RL Biochim. Biophys. Acta 393:195-200(1975). RN [45] RP VARIANT CARIBBEAN ARG-92. RX MEDLINE=77048866; PubMed=992050; DOI=10.1016/0014-5793(76)80662-X; RA Ahern E., Ahern V., Hilton T., Serjeant G.R., Serjeant B.E., RA Seakins M., Lang A., Middleton A., Lehmann H.; RT "Haemoglobin caribbean beta91 (F7) Leu replaced by Arg: a mildly RT haemoglobin with a low oxygen affinity."; RL FEBS Lett. 69:99-102(1976). RN [46] RP VARIANT CITY OF HOPE SER-70. RX MEDLINE=85006311; PubMed=6434492; RA Rahbar S., Asmerom Y., Blume K.G.; RT "A silent hemoglobin variant detected by HPLC: hemoglobin City of Hope RT beta 69 (E13) Gly-->Ser."; RL Hemoglobin 8:333-342(1984). RN [47] RP VARIANT COIMBRA GLU-100. RX MEDLINE=92267852; PubMed=1814856; RA Tamagnini G.P., Ribeiro M.L., Valente V., Ramachandran M., RA Wilson J.B., Baysal E., Gu L.H., Huisman T.H.J.; RT "Hb Coimbra or alpha 2 beta (2)99(G1)Asp-->Glu, a newly discovered RT high oxygen affinity variant."; RL Hemoglobin 15:487-496(1991). RN [48] RP VARIANT COSTA RICA ARG-78. RX MEDLINE=96235282; PubMed=8641705; DOI=10.1007/s004390050145; RA Romero W.E.R., Castillo M., Chaves M.A., Saenz G.F., Gu L.-H., RA Wilson J.B., Baysal E., Smetanina N.S., Leonova J.Y., Huisman T.H.J.; RT "Hb Costa Rica or alpha 2 beta 2 77(EF1)His-->Arg: the first example RT of a somatic cell mutation in a globin gene."; RL Hum. Genet. 97:829-833(1996). RN [49] RP VARIANT DEBROUSSE PRO-97. RX MEDLINE=96180033; PubMed=8602627; RA Lacan P., Kister J., Francina A., Souillet G., Galacteros F., RA Delaunay J., Wajcman H.; RT "Hemoglobin Debrousse (beta 96[FG3]Leu-->Pro): a new unstable RT hemoglobin with twofold increased oxygen affinity."; RL Am. J. Hematol. 51:276-281(1996). RN [50] RP VARIANT DHONBURI GLY-127. RX MEDLINE=90379198; PubMed=2399911; RA Bardakdjian-Michau J., Fucharoen S., Delanoe-Garin J., Kister J., RA Lacombe C., Winichagoon P., Blouquit Y., Riou J., Wasi P., RA Galacteros F.; RT "Hemoglobin Dhonburi alpha 2 beta 2 126 (H4) Val-->Gly: a new unstable RT beta variant producing a beta-thalassemia intermedia phenotype in RT association with beta zero-thalassemia."; RL Am. J. Hematol. 35:96-99(1990). RN [51] RP VARIANTS NEWCASTLE PRO-93 AND CAMPERDOWN SER-105, AND DESCRIPTION OF RP VARIANT DUINO. RX MEDLINE=92380658; PubMed=1511986; DOI=10.1007/BF00221961; RA Wajcman H., Blouquit Y., Vasseur C., le Querrec A., Laniece M., RA Melevendi C., Rasore A., Galacteros F.; RT "Two new human hemoglobin variants caused by unusual mutational RT events: Hb Zaire contains a five residue repetition within the alpha- RT chain and Hb Duino has two residues substituted in the beta-chain."; RL Hum. Genet. 89:676-680(1992). RN [52] RP VARIANT DURHAM-N.C. PRO-115. RX MEDLINE=93244842; PubMed=1301199; RA Murru S., Poddie D., Sciarratta G.V., Agosti S., Baffico M., RA Melevendi C., Pirastu M., Cao A.; RT "A novel beta-globin structural mutant, Hb Brescia (beta 114 Leu-Pro), RT causing a severe beta-thalassemia intermedia phenotype."; RL Hum. Mutat. 1:124-128(1992). RN [53] RP VARIANT DURHAM-N.C. PRO-115. RX MEDLINE=94154273; PubMed=8111050; RA de Castro C.M., Devlin B., Fleenor D.E., Lee M.E., Kaufman R.E.; RT "A novel beta-globin mutation, beta Durham-NC [beta 114 Leu-->Pro], RT produces a dominant thalassemia-like phenotype."; RL Blood 83:1109-1116(1994). RN [54] RP VARIANT J-EUROPA ASP-63. RX MEDLINE=96407264; PubMed=8811317; RA Kiger L., Kister J., Groff P., Kalmes G., Prome D., Galacteros F., RA Wajcman H.; RT "Hb J-Europa [beta 62(E6)Ala-->Asp]: normal oxygen binding properties RT in a new variant involving a residue located distal to the heme."; RL Hemoglobin 20:135-140(1996). RN [55] RP VARIANT GEELONG ASP-140. RX MEDLINE=92010939; PubMed=1917539; RA Como P.F., Hocking D.R., Swinton G.W., Trent R.J., Holland R.A.B., RA Tibben E.A., Wilkinson T., Kronenberg H.; RT "Hb Geelong [beta 139(H17)Asn-->Asp]."; RL Hemoglobin 15:85-95(1991). RN [56] RP VARIANT GRANGE-BLANCHE VAL-28. RX MEDLINE=88030044; PubMed=3666141; DOI=10.1016/0014-5793(87)80509-4; RA Baklouti F., Giraud Y., Francina A., Richard G., Perier C., RA Geyssant A., Jaubert J., Brizard C., Delaunay J.; RT "Hemoglobin Grange-Blanche [beta 27(B9) Ala-->Val], a new variant with RT normal expression and increased affinity for oxygen."; RL FEBS Lett. 223:59-62(1987). RN [57] RP VARIANT GRAZ LEU-3. RX MEDLINE=93138927; PubMed=1487420; RA Liu J.S., Molchanova T.P., Gu L.H., Wilson J.B., Hopmeier P., RA Schnedl W., Balaun E., Krejs G.J., Huisman T.H.J.; RT "Hb Graz or alpha 2 beta 2(2)(NA2)His-->Leu; a new beta chain variant RT observed in four families from southern Austria."; RL Hemoglobin 16:493-501(1992). RN [58] RP VARIANT HELSINKI MET-83. RX MEDLINE=77062201; PubMed=826083; RA Ikkala E., Koskela J., Pikkarainen P., Rahiala E.-L., El-Hazmi M.A.F., RA Nagai K., Lang A., Lehmann H.; RT "Hb Helsinki: a variant with a high oxygen affinity and a substitution RT at a 2,3-DPG binding site (beta82[EF6] Lys replaced by Met)."; RL Acta Haematol. 56:257-275(1976). RN [59] RP VARIANT HIMEJI ASP-141. RX MEDLINE=86167527; PubMed=3754244; RA Ohba Y., Miyaji T., Murakami M., Kadowaki S., Fujita T., Oimomi M., RA Hatanaka H., Ishikawa K., Baba S., Hitaka K., Imai K.; RT "Hb Himeji or beta 140 (H18) Ala-->Asp. A slightly unstable hemoglobin RT with increased beta N-terminal glycation."; RL Hemoglobin 10:109-126(1986). RN [60] RP VARIANT HINSDALE LYS-140. RX MEDLINE=90093866; PubMed=2513289; RA Moo-Penn W.F., Johnson M.H., Jue D.L., Lonser R.; RT "Hb Hinsdale [beta 139 (H17)Asn-->Lys]: a variant in the central RT cavity showing reduced affinity for oxygen and 2,3- RT diphosphoglycerate."; RL Hemoglobin 13:455-464(1989). RN [61] RP VARIANT HINWIL ASN-39. RX MEDLINE=96351651; PubMed=8745430; RA Frischknecht H., Ventruto M., Hess D., Hunziker P., Rosatelli M.C., RA Cao A., Breitenstein U., Fehr J., Tuchschmid P.; RT "HB Hinwil or beta 38(C4)Thr-->Asn: a new beta chain variant detected RT in a Swiss family."; RL Hemoglobin 20:31-40(1996). RN [62] RP VARIANT HOWICK GLY-38. RX MEDLINE=94193408; PubMed=8144352; RA Owen M.C., Ockelford P.A., Wells R.M.G.; RT "Hb Howick [beta 37(C3)Trp-->Gly]: a new high oxygen affinity variant RT of the alpha 1 beta 2 contact."; RL Hemoglobin 17:513-521(1993). RN [63] RP VARIANT INDIANAPOLIS ARG-113. RX MEDLINE=79151109; PubMed=429365; RA Adams J.G. III, Steinberg M.H., Boxer L.A., Baehner R.L., Forget B.G., RA Tsistrakis G.A.; RT "The structure of hemoglobin Indianapolis [beta112(G14) arginine]. An RT unstable variant detectable only by isotopic labeling."; RL J. Biol. Chem. 254:3479-3482(1979). RN [64] RP VARIANT ISEHARA ASN-93. RX MEDLINE=92155974; PubMed=1787097; RA Harano T., Harano K., Kushida Y., Ueda S., Yoshii A., Nishinarita M.; RT "Hb Isehara (or Hb Redondo) [beta 92 (F8) His-->Asn]: an unstable RT variant with a proximal histidine substitution at the heme contact."; RL Hemoglobin 15:279-290(1991). RN [65] RP VARIANT ISTAMBUL GLN-93. RX MEDLINE=73054825; PubMed=4639022; RA Aksoy M., Erdem S., Efremov G.D., Wilson J.B., Huisman T.H.J., RA Schroeder W.A., Shelton J.R., Shelton J.B., Ulitin O.N., Muftuoglu A.; RT "Hemoglobin Istanbul: substitution of glutamine for histidine in a RT proximal histidine (F8(92))."; RL J. Clin. Invest. 51:2380-2387(1972). RN [66] RP VARIANT JACKSONVILLE ASP-55. RX MEDLINE=91331861; PubMed=2101840; RA Gaudry C.L. Jr., Pitel P.A., Jue D.L., Hine T.K., Johnson M.H., RA Moo-Penn W.F.; RT "Hb Jacksonville [alpha 2 beta 2(54)(D5)Val-->Asp]: a new unstable RT variant found in a patient with hemolytic anemia."; RL Hemoglobin 14:653-659(1990). RN [67] RP VARIANT JIANGHUA ILE-121. RX MEDLINE=84007581; PubMed=6618888; RA Lu Y.Q., Fan J.L., Liu J.F., Hu H.L., Peng X.H., Huang C.-H., RA Huang P.Y., Chen S.S., Jai P.C., Yang K.G.; RT "Hemoglobin Jianghua [beta 120(GH3) Lys leads to Ile]: a new fast- RT moving variant found in China."; RL Hemoglobin 7:321-326(1983). RN [68] RP VARIANT KARLSKOGA HIS-22. RX MEDLINE=93322190; PubMed=8330972; RA Landin B.; RT "Hb Karlskoga or alpha 2 beta (2)21(B3) Asp-->His: a new slow-moving RT variant found in Sweden."; RL Hemoglobin 17:201-208(1993). RN [69] RP VARIANT KNOSSOS SER-28. RX MEDLINE=83079719; PubMed=7173395; DOI=10.1016/0014-5793(82)81052-1; RA Arous N., Galacteros F., Fessas P., Loukopoulos D., Blouquit Y., RA Komis G., Sellaye M., Boussiou M., Rosa J.; RT "Structural study of hemoglobin Knossos, beta 27 (B9) Ala leads to RT Ser. A new abnormal hemoglobin present as a silent beta-thalassemia."; RL FEBS Lett. 147:247-250(1982). RN [70] RP VARIANT KODAIRA GLN-147. RX MEDLINE=92340295; PubMed=1634367; RA Harano T., Harano K., Kushida Y., Imai K., Nishinakamura R., RA Matsunaga T.; RT "Hb Kodaira [beta 146(HC3)His-->Gln]: a new beta chain variant with an RT amino acid substitution at the C-terminus."; RL Hemoglobin 16:85-91(1992). RN [71] RP VARIANT KOFU ILE-85. RX MEDLINE=86303641; PubMed=3744871; RA Harano T., Harano K., Ueda S., Imai N., Kitazumi T.; RT "A new electrophoretically-silent hemoglobin variant: hemoglobin Kofu RT or alpha 2 beta 2 84 (EF8) Thr-->Ile."; RL Hemoglobin 10:417-420(1986). RN [72] RP VARIANT HRADEC KRALOVE ASP-116. RX MEDLINE=94042221; PubMed=7693620; RA Divoky V., Svobodova M., Indrak K., Chrobak L., Molchanova T.P., RA Huisman T.H.J.; RT "Hb Hradec Kralove (Hb HK) or alpha 2 beta 2 115(G17)Ala-->Asp, a RT severely unstable hemoglobin variant resulting in a dominant beta- RT thalassemia trait in a Czech family."; RL Hemoglobin 17:319-328(1993). RN [73] RP VARIANT LA DESIRADE VAL-130. RX MEDLINE=87165149; PubMed=3557994; RA Merault G., Keclard L., Garin J., Poyart C., Blouquit Y., Arous N., RA Galacteros F., Feingold J., Rosa J.; RT "Hemoglobin La Desirade alpha A2 beta 2 129 (H7) Ala-->Val: a new RT unstable hemoglobin."; RL Hemoglobin 10:593-605(1986). RN [74] RP VARIANT LA ROCHE-SUR-YON HIS-82. RX MEDLINE=92172947; PubMed=1540659; DOI=10.1016/0925-4439(92)90052-O; RA Wajcman H., Kister J., Vasseur C., Blouquit Y., Trastour J.C., RA Cottenceau D., Galacteros F.; RT "Structure of the EF corner favors deamidation of asparaginyl residues RT in hemoglobin: the example of Hb La Roche-sur-Yon [beta 81 (EF5) RT Leu-->His]."; RL Biochim. Biophys. Acta 1138:127-132(1992). RN [75] RP VARIANT LAS PALMAS PHE-50. RX MEDLINE=88256753; PubMed=3384708; RA Malcorra-Azpiazu J.J., Balda-Aguirre M.I., Diaz-Chico J.C., Hu H., RA Wilson J.B., Webber B.B., Kutlar F., Kutlar A., Huisman T.H.J.; RT "Hb Las Palmas or alpha 2 beta 2(49)(CD8)Ser-->Phe, a mildly unstable RT hemoglobin variant."; RL Hemoglobin 12:163-170(1988). RN [76] RP VARIANT LINKOPING THR-37. RX MEDLINE=88083482; PubMed=3691763; RA Berlin G., Wranne B., Jeppsson J.-O.; RT "Hb Linkoping (beta 36 Pro-->Thr): a new high oxygen affinity RT hemoglobin variant found in two families of Finnish origin."; RL Eur. J. Haematol. 39:452-456(1987). RN [77] RP VARIANT MAPUTO TYR-48. RX MEDLINE=84031650; PubMed=6629824; RA Marinucci M., Boissel J.P., Massa A., Wajcman H., Tentori L., RA Labie D.; RT "Hemoglobin Maputo: a new beta-chain variant (alpha 2 beta 2 47 (CD6) RT Asp replaced by Tyr) in combination with hemoglobin S, identified by RT high performance liquid chromatography (HPLC)."; RL Hemoglobin 7:423-433(1983). RN [78] RP VARIANT MATERA LYS-56. RX MEDLINE=90346586; PubMed=2384314; RA Sciarratta G.V., Ivaldi G.; RT "Hb Matera [beta 55(D6)Met-->Lys]: a new unstable hemoglobin variant RT in an Italian family."; RL Hemoglobin 14:79-85(1990). RN [79] RP VARIANT MIYASHIRO GLY-24. RX MEDLINE=82166873; PubMed=7338468; RA Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Miyata H., RA Shinohara T., Hori T., Takayama J.; RT "Hemoglobin Miyashiro (beta 23[B5] val substituting for gly) an RT electrophoretically silent variant discovered by the isopropanol RT test."; RL Hemoglobin 5:653-666(1981). RN [80] RP VARIANT MIZUHO PRO-69. RX MEDLINE=77248961; PubMed=893142; RA Ohba Y., Miyaji T., Matsuoka M., Sugiyama K., Suzuki T., Sugiura T.; RT "Hemoglobin Mizuho or beta 68 (E 12) leucine leads to proline, a new RT unstable variant associated with severe hemolytic anemia."; RL Hemoglobin 1:467-477(1977). RN [81] RP VARIANT MUSCAT VAL-33. RX MEDLINE=92387956; PubMed=1517102; RA Ramachandran M., Gu L.H., Wilson J.B., Kitundu M.N., Adekile A.D., RA Liu J.C., McKie K.M., Huisman T.H.J.; RT "A new variant, HB Muscat [alpha 2 beta (2)32(B14)Leu-->Val] observed RT in association with HB S in an Arabian family."; RL Hemoglobin 16:259-266(1992). RN [82] RP VARIANT N-TIMONE GLU-9. RX MEDLINE=90236754; PubMed=2634671; RA Lena-Russo D., Orsini A., Vovan L., Bardakdjian-Michau J., Lacombe C., RA Blouquit Y., Craescu C.T., Galacteros F.; RT "Hb N-Timone [alpha 2 beta 2(8)(A5)Lys-->Glu]: a new fast-moving RT variant with normal stability and oxygen affinity."; RL Hemoglobin 13:743-747(1989). RN [83] RP VARIANT NAGOYA PRO-98. RX MEDLINE=85206960; PubMed=3838976; RA Ohba Y., Imanaka M., Matsuoka M., Hattori Y., Miyaji T., Funaki C., RA Shibata K., Shimokata H., Kuzuya F., Miwa S.; RT "A new unstable, high oxygen affinity hemoglobin: Hb Nagoya or beta 97 RT (FG4) His-->Pro."; RL Hemoglobin 9:11-24(1985). RN [84] RP VARIANT D-NEATH ALA-122. RX MEDLINE=93322197; PubMed=8330979; RA Welch S.G., Bateman C.; RT "Hb D-Neath or beta 121 (GH4) Glu-->Ala: a new member of the Hb D RT family."; RL Hemoglobin 17:255-259(1993). RN [85] RP VARIANT NORTH CHICAGO SER-37. RX MEDLINE=86139289; PubMed=3937824; RA Rahbar S., Louis J., Lee T., Asmerom Y.; RT "Hemoglobin North Chicago (beta 36 [C2] proline-->serine): a new high RT affinity hemoglobin."; RL Hemoglobin 9:559-576(1985). RN [86] RP VARIANT NORTH SHORE-CARACAS GLU-135. RX MEDLINE=77246803; PubMed=891976; DOI=10.1016/0014-5793(77)80453-5; RA Arends T., Lehmann H., Plowman D., Stathopoulou R.; RT "Haemoglobin North Shore-Caracas beta 134 (H12) valine replaced by RT glutamic acid."; RL FEBS Lett. 80:261-265(1977). RN [87] RP VARIANT OLOMOUC ASP-87. RX MEDLINE=87307470; PubMed=3623975; RA Indrak K., Wiedermann B.F., Batek F., Wilson J.B., Webber B.B., RA Kutlar A., Huisman T.H.J.; RT "Hb Olomouc or alpha 2 beta 2(86)(F2)Ala-->Asp, a new high oxygen RT affinity variant."; RL Hemoglobin 11:151-155(1987). RN [88] RP VARIANT PALMERSTON NORTH PHE-24. RX MEDLINE=83135041; PubMed=7161106; RA Brennan S.O., Williamson D., Whisson M.E., Carrell R.W.; RT "Hemoglobin Palmerston North beta 23 (B5) Val replaced by Phe. A new RT variant identified in a patient with polycythemia."; RL Hemoglobin 6:569-575(1982). RN [89] RP VARIANT PIERRE-BENITE ASP-91. RX MEDLINE=88256754; PubMed=3384709; RA Baklouti F., Giraud Y., Francina A., Richard G., Favre-Gilly J., RA Delaunay J.; RT "Hemoglobin Pierre-Benite [beta 90(F6)Glu-->Asp], a new high affinity RT variant found in a French family."; RL Hemoglobin 12:171-177(1988). RN [90] RP VARIANT PRESBYTERIAN LYS-109. RX MEDLINE=78215075; PubMed=668922; DOI=10.1016/0014-5793(78)80720-0; RA Moo-Penn W.F., Wolff J.A., Simon G., Vacek M., Jue D.L., Johnson M.H.; RT "Hemoglobin Presbyterian: beta108 (G10) asparagine leads to lysine, A RT hemoglobin variant with low oxygen affinity."; RL FEBS Lett. 92:53-56(1978). RN [91] RP VARIANT PUTTELANGE VAL-141. RX MEDLINE=96101899; PubMed=8522332; DOI=10.1007/BF00210304; RA Wajcman H., Girodon E., Prome D., North M.L., Plassa F., Duwig I., RA Kister J., Bergerat J.P., Oberling F., Lampert E., Lonsdorfer J., RA Goossens M., Galacteros F.; RT "Germline mosaicism for an alanine to valine substitution at residue RT beta 140 in hemoglobin Puttelange, a new variant with high oxygen RT affinity."; RL Hum. Genet. 96:711-716(1995). RN [92] RP VARIANT QUIN-HAI ARG-79. RX MEDLINE=84031648; PubMed=6629822; RA Jen P.C., Chen L.C., Chen P.F., Wong Y., Chen L.F., Guo Y.Y., RA Chang F.Q., Chow Y.C., Chiu Y.; RT "Hemoglobin Quin-Hai, beta 78 (EF2) Leu replaced by Arg, a new RT abnormal hemoglobin found in Guangdong, China."; RL Hemoglobin 7:407-412(1983). RN [93] RP VARIANT RAMBAM ASP-70. RX MEDLINE=98432396; PubMed=9761252; RA Bisse E., Zorn N., Eigel A., Lizama M., Huamam-Guillen P., Marz W., RA van Dorsselaer A., Wieland H.; RT "Hemoglobin Rambam (beta69[E13]Gly-->Asp), a pitfall in the assessment RT of diabetic control: characterization by electrospray mass RT spectrometry and HPLC."; RL Clin. Chem. 44:2172-2177(1998). RN [94] RP VARIANT RANDWICK GLY-16. RX MEDLINE=88256752; PubMed=3384707; RA Gilbert A.T., Fleming P.J., Sumner D.R., Hughes W.G., Ip F., RA Kwan Y.L., Holland R.A.B.; RT "Hemoglobin Randwick or beta 15 (A12)Trp-->Gly: a new unstable beta- RT chain hemoglobin variant."; RL Hemoglobin 12:149-161(1988). RN [95] RP VARIANT RIO GRANDE THR-9. RX MEDLINE=83185445; PubMed=6857757; RA Moo-Penn W.F., Johnson M.H., McGuffey J.E., Jue D.L., RA Therrell B.L. Jr.; RT "Hemoglobin Rio Grande [beta 8 (A5) Lys leads to Thr] a new variant RT found in a Mexican-American family."; RL Hemoglobin 7:91-95(1983). RN [96] RP VARIANT RUSH GLN-102. RX MEDLINE=74080282; PubMed=4129558; RA Adams J.G. III, Winter W.P., Tausk K., Heller P.; RT "Hemoglobin Rush (beta 101 (g3) glutamine): a new unstable hemoglobin RT causing mild hemolytic anemia."; RL Blood 43:261-269(1974). RN [97] RP VARIANT SAITAMA PRO-118. RX MEDLINE=83185440; PubMed=6687721; RA Ohba Y., Hasegawa Y., Amino H., Miwa S., Nakatsuji T., Hattori Y., RA Miyaji T.; RT "Hemoglobin Saitama or beta 117 (G19) His leads to Pro, a new variant RT causing hemolytic disease."; RL Hemoglobin 7:47-56(1983). RN [98] RP VARIANT M-SASKATOON TYR-64. RX PubMed=13897827; RA Gerald P.S., Efron M.L.; RT "Chemical studies of several varieties of Hb M."; RL Proc. Natl. Acad. Sci. U.S.A. 47:1758-1767(1961). RN [99] RP VARIANT SHELBY/LESLIE/DEACONESS LYS-132. RX MEDLINE=85130256; PubMed=6526653; RA Moo-Penn W.F., Johnson M.H., McGuffey J.E., Jue D.L.; RT "Hemoglobin Shelby [beta 131(H9) Gln-->Lys] a correction to the RT structure of hemoglobin Deaconess and hemoglobin Leslie."; RL Hemoglobin 8:583-593(1984). RN [100] RP VARIANT J-SICILIA ASN-66. RX MEDLINE=74302182; PubMed=4852224; DOI=10.1016/0014-5793(74)80050-5; RA Ricco G., Pich P.G., Mazza U., Rossi G., Ajmar P., Arese P., Gallo E.; RT "Hb J Sicilia: beta 65 (E9) Lys-Asn, a beta homologue of Hb Zambia."; RL FEBS Lett. 39:200-204(1974). RN [101] RP VARIANT STANMORE ALA-112. RX MEDLINE=92010936; PubMed=1917537; RA Como P.F., Wylie B.R., Trent R.J., Bruce D., Volpato F., Wilkinson T., RA Kronenberg H., Holland R.A.B., Tibben E.A.; RT "A new unstable and low oxygen affinity hemoglobin variant: Hb RT Stanmore [beta 111(G13)Val-->Ala]."; RL Hemoglobin 15:53-65(1991). RN [102] RP VARIANT ST MANDE TYR-103. RX MEDLINE=81212764; PubMed=7238856; DOI=10.1016/0014-5793(81)81046-0; RA Arous N., Braconnier F., Thillet J., Blouquit Y., Galacteros F., RA Chevrier M., Bordahandy C., Rosa J.; RT "Hemoglobin Saint Mande beta 102 (G4) asn replaced by tyr: a new low RT oxygen affinity variant."; RL FEBS Lett. 126:114-116(1981). RN [103] RP VARIANT WINDSOR ASP-12. RX MEDLINE=90093865; PubMed=2599880; RA Gilbert A.T., Fleming P.J., Sumner D.R., Hughes W.G., Holland R.A.B., RA Tibben E.A.; RT "Hemoglobin Windsor or beta 11 (A8)Val-->Asp: a new unstable beta- RT chain hemoglobin variant producing a hemolytic anemia."; RL Hemoglobin 13:437-453(1989). RN [104] RP VARIANT YAHATA TYR-113. RX MEDLINE=92010926; PubMed=1917530; RA Harano T., Harano K., Kushida Y., Ueda S.; RT "A new abnormal variant, Hb Yahata or beta 112(G14)Cys-->Tyr, found in RT a Japanese: structural confirmation by DNA sequencing of the beta- RT globin gene."; RL Hemoglobin 15:109-113(1991). RN [105] RP VARIANT YOKOHAMA PRO-32. RX MEDLINE=82166874; PubMed=7338469; RA Nakatsuji T., Miwa S., Ohba Y., Hattori Y., Miyaji T., Hino S., RA Matsumoto N.; RT "A new unstable hemoglobin, Hb Yokohama beta 31 (B13)Leu substituting RT for Pro, causing hemolytic anemia."; RL Hemoglobin 5:667-678(1981). RN [106] RP VARIANT ZENGCHENG MET-115. RX MEDLINE=91177717; PubMed=2079435; RA Plaseska D., Wilson J.B., Gu L.H., Kutlar F., Huisman T.H.J., RA Zeng Y.T., Shen M.; RT "Hb Zengcheng or alpha 2 beta(2)114(G16)Leu-->Met."; RL Hemoglobin 14:555-557(1990). RN [107] RP VARIANT IRAQ-HALABJA VAL-11. RX PubMed=10398311; RX DOI=10.1002/(SICI)1096-8652(199907)61:3<187::AID-AJH5>3.0.CO;2-7; RA Deutsch S., Darbellay R., Offord R., Frutiger A., Kister J., RA Wajcman H., Beris P.; RT "Hb Iraq-Halabja beta10 (A7) Ala-->Val (GCC-->GTC): a new beta-chain RT silent variant in a family with multiple Hb disorders."; RL Am. J. Hematol. 61:187-193(1999). RN [108] RP VARIANT VILLEJUIF ILE-124. RX PubMed=11300351; DOI=10.1081/HEM-100103071; RA Carbone V., Salzano A.M., Pagano L., Buffardi S., De Rosa C., RA Pucci P.; RT "Identification of Hb Villejuif [beta123(H1)Thr-->Ile] in Southern RT Italy."; RL Hemoglobin 25:67-78(2001). RN [109] RP VARIANT TSUKUMI TYR-118. RX PubMed=11300344; DOI=10.1081/HEM-100103076; RA North M.L., Duwig I., Riou J., Prome D., Yapo A.P., Kister J., RA Bardakdjian-Michau J., Cazenave J.-P., Wajcman H.; RT "Hb Tsukumi [beta117(G19)His-->Tyr] found in a Moroccan woman."; RL Hemoglobin 25:107-110(2001). RN [110] RP VARIANT CANTERBURY PHE-113. RX PubMed=11939514; DOI=10.1081/HEM-120002942; RA Brennan S.O., Potter H.C., Kubala L.M., Carnoutsos S.A., RA Ferguson M.M.; RT "Hb Canterbury [beta112(G14)Cys-->Phe]: a new, mildly unstable RT variant."; RL Hemoglobin 26:67-69(2002). RN [111] RP VARIANT PYRGOS ASP-84, AND VARIANT E LYS-27. RX PubMed=12144064; DOI=10.1081/HEM-120005459; RA Sawangareetrakul P., Svasti S., Yodsowon B., Winichagoon P., RA Srisomsap C., Svasti J., Fucharoen S.; RT "Double heterozygosity for Hb Pyrgos [beta83(EF7)Gly-->Asp] and Hb E RT [beta26(B8)Glu-->Lys] found in association with alpha-thalassemia."; RL Hemoglobin 26:191-196(2002). RN [112] RP VARIANT SANTANDER ASP-35. RX PubMed=12603091; DOI=10.1081/HEM-120016378; RA Villegas A., Ropero P., Nogales A., Gonzalez F.A., Mateo M., Mazo E., RA Rodrigo E., Arias M.; RT "Hb Santander [beta34(B16)Val-->Asp (GTC-->GAC)]: a new unstable RT variant found as a de novo mutation in a Spanish patient."; RL Hemoglobin 27:31-35(2003). RN [113] RP VARIANT NANTES LEU-35, AND VARIANT VEXIN LEU-117. RX PubMed=12908805; DOI=10.1081/HEM-120023384; RA Wajcman H., Bardakdjian-Michau J., Riou J., Prehu C., Kister J., RA Baudin-Creuza V., Prome D., Richelme-David S., Harousseau J.L., RA Galacteros F.; RT "Two new hemoglobin variants with increased oxygen affinity: Hb Nantes RT [beta34(B16)Val-->Leu] and Hb Vexin [beta116(G18)His-->Leu]."; RL Hemoglobin 27:191-199(2003). RN [114] RP VARIANT LYS-27. RX PubMed=15481886; DOI=10.1081/HEM-120040334; RA Flatz G., Sanguansermsri T., Sengchanh S., Horst D., Horst J.; RT "The 'hot-spot' of Hb E [beta26(B8)Glu-->Lys] in Southeast Asia: beta- RT globin anomalies in the Lao Theung population of southern Laos."; RL Hemoglobin 28:197-204(2004). CC -!- FUNCTION: Involved in oxygen transport from the lung to the CC various peripheral tissues. CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in CC adult hemoglobin A (HbA). CC -!- INTERACTION: CC P69905:HBA1; NbExp=1; IntAct=EBI-715554, EBI-714680; CC -!- TISSUE SPECIFICITY: Red blood cells. CC -!- PTM: Glucose reacts non-enzymatically with the N-terminus of the CC beta chain to form a stable ketoamine linkage. This takes place CC slowly and continuously throughout the 120-day life span of the CC red blood cell. The rate of glycation is increased in patients CC with diabetes mellitus. CC -!- PTM: S-nitrosylated; a nitric oxide group is first bound to Fe(2+) CC and then transferred to Cys-94 to allow capture of O(2). CC -!- PTM: Acetylated on Lys-60, Lys-83 and Lys-145 upon aspirin CC exposure. Ref.21 reports the identification of HBB acetylated on CC Lys-145 in the cytosolic fraction of HeLa cells. This may results CC from a contamination of the sample. CC -!- DISEASE: Defects in HBB are the cause of beta-thalassemia CC [MIM:141900]. The thalassemias are the most common monogenic CC diseases and occur mostly in Mediterranean and Southeast Asian CC populations. The hallmark of beta-thalassemia is an imbalance in CC globin-chain production in the adult HbA molecule. Absence of beta CC chain causes beta(0)-thalassemia, while reduced amounts of CC detectable beta globin causes beta(+)-thalassemia. In the severe CC forms of beta-thalassemia, the excess alpha globin chains CC accumulate in the developing erythroid precursors in the marrow. CC Their deposition leads to a vast increase in erythroid apoptosis CC that in turn causes ineffective erythropoiesis and severe CC microcytic hypochromic anemia. Clinically, beta-thalassemia is CC divided into thalassemia major (transfusion dependent), CC thalassemia intermedia (of intermediate severity), and thalassemia CC minor (asymptomatic). CC -!- DISEASE: Defects in HBB are the cause of sickle cell anemia CC [MIM:603903]; also known as sickle cell disease. Sickle cell CC anemia is characterized by abnormally shaped red cells resulting CC in chronic anemia and periodic episodes of pain, serious CC infections and damage to vital organs. Normal red blood cells are CC round and flexible and flow easily through blood vessels, but in CC sickle cell anemia, the abnormal hemoglobin (called Hb S) causes CC red blood cells to become stiff. They are C-shaped and resembles a CC sickle. These stiffer red blood cells can led to microvascular CC occlusion thus cutting off the blood supply to nearby tissues. CC -!- SIMILARITY: Belongs to the globin family. CC -!- WEB RESOURCE: NAME=HbVar; CC NOTE=Human hemoglobin variants and thalassemias; CC URL="http://globin.bx.psu.edu/cgi-bin/hbvar/query_vars3?mode=directlink&gene=HBB". CC -!- WEB RESOURCE: NAME=GeneReviews; CC URL="http://www.genetests.org/query?gene=HBB". CC -!- WEB RESOURCE: NAME=SHMPD; CC NOTE=The Singapore human mutation and polymorphism database; CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HBB". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U01317; AAA16334.1; -; Genomic_DNA. DR EMBL; V00497; CAA23756.1; -; mRNA. DR EMBL; V00499; CAA23758.1; -; Genomic_DNA. DR EMBL; V00500; CAA23759.1; ALT_SEQ; mRNA. DR EMBL; L26462; AAA21100.1; -; Genomic_DNA. DR EMBL; L26463; AAA21101.1; -; Genomic_DNA. DR EMBL; L26464; AAA21102.1; -; Genomic_DNA. DR EMBL; L26465; AAA21103.1; -; Genomic_DNA. DR EMBL; L26466; AAA21104.1; -; Genomic_DNA. DR EMBL; L26467; AAA21105.1; -; Genomic_DNA. DR EMBL; L26468; AAA21106.1; -; Genomic_DNA. DR EMBL; L26469; AAA21107.1; -; Genomic_DNA. DR EMBL; L26470; AAA21108.1; -; Genomic_DNA. DR EMBL; L26471; AAA21109.1; -; Genomic_DNA. DR EMBL; L26472; AAA21110.1; -; Genomic_DNA. DR EMBL; L26473; AAA21111.1; -; Genomic_DNA. DR EMBL; L26474; AAA21112.1; -; Genomic_DNA. DR EMBL; L26475; AAA21113.1; -; Genomic_DNA. DR EMBL; L26476; AAA21114.1; -; Genomic_DNA. DR EMBL; L26477; AAA21115.1; -; Genomic_DNA. DR EMBL; L26478; AAA21116.1; -; Genomic_DNA. DR EMBL; L48213; AAA88063.1; -; Genomic_DNA. DR EMBL; L48214; AAA88061.1; -; Genomic_DNA. DR EMBL; L48215; AAA88059.1; -; Genomic_DNA. DR EMBL; L48216; AAA88065.1; -; Genomic_DNA. DR EMBL; L48217; AAA88067.1; -; Genomic_DNA. DR EMBL; M36640; AAA52634.1; -; Genomic_DNA. DR EMBL; M11428; AAA52633.1; -; mRNA. DR EMBL; M25079; AAA35597.1; -; mRNA. DR EMBL; M25113; AAA35966.1; -; mRNA. DR EMBL; L48932; AAA88054.1; -; Genomic_DNA. DR EMBL; AF007546; AAB62944.1; -; Genomic_DNA. DR EMBL; AF117710; AAD19696.1; -; mRNA. DR EMBL; AF181989; AAF00489.1; -; mRNA. DR EMBL; AF349114; AAK29639.1; -; mRNA. DR EMBL; AY260740; AAP21062.1; -; Genomic_DNA. DR EMBL; AY136510; AAN11320.1; -; mRNA. DR EMBL; AY163866; AAN84548.1; -; Genomic_DNA. DR EMBL; AF527577; AAM92001.1; -; Genomic_DNA. DR EMBL; DQ126270; AAZ39745.1; -; Genomic_DNA. DR EMBL; DQ126271; AAZ39746.1; -; Genomic_DNA. DR EMBL; DQ126272; AAZ39747.1; -; Genomic_DNA. DR EMBL; DQ126273; AAZ39748.1; -; Genomic_DNA. DR EMBL; DQ126274; AAZ39749.1; -; Genomic_DNA. DR EMBL; DQ126275; AAZ39750.1; -; Genomic_DNA. DR EMBL; DQ126276; AAZ39751.1; -; Genomic_DNA. DR EMBL; DQ126277; AAZ39752.1; -; Genomic_DNA. DR EMBL; DQ126278; AAZ39753.1; -; Genomic_DNA. DR EMBL; DQ126279; AAZ39754.1; -; Genomic_DNA. DR EMBL; DQ126280; AAZ39755.1; -; Genomic_DNA. DR EMBL; DQ126281; AAZ39756.1; -; Genomic_DNA. DR EMBL; DQ126282; AAZ39757.1; -; Genomic_DNA. DR EMBL; DQ126283; AAZ39758.1; -; Genomic_DNA. DR EMBL; DQ126284; AAZ39759.1; -; Genomic_DNA. DR EMBL; DQ126285; AAZ39760.1; -; Genomic_DNA. DR EMBL; DQ126286; AAZ39761.1; -; Genomic_DNA. DR EMBL; DQ126287; AAZ39762.1; -; Genomic_DNA. DR EMBL; DQ126288; AAZ39763.1; -; Genomic_DNA. DR EMBL; DQ126289; AAZ39764.1; -; Genomic_DNA. DR EMBL; DQ126290; AAZ39765.1; -; Genomic_DNA. DR EMBL; DQ126291; AAZ39766.1; -; Genomic_DNA. DR EMBL; DQ126292; AAZ39767.1; -; Genomic_DNA. DR EMBL; DQ126293; AAZ39768.1; -; Genomic_DNA. DR EMBL; DQ126294; AAZ39769.1; -; Genomic_DNA. DR EMBL; DQ126295; AAZ39770.1; -; Genomic_DNA. DR EMBL; DQ126296; AAZ39771.1; -; Genomic_DNA. DR EMBL; DQ126297; AAZ39772.1; -; Genomic_DNA. DR EMBL; DQ126298; AAZ39773.1; -; Genomic_DNA. DR EMBL; DQ126299; AAZ39774.1; -; Genomic_DNA. DR EMBL; DQ126300; AAZ39775.1; -; Genomic_DNA. DR EMBL; DQ126301; AAZ39776.1; -; Genomic_DNA. DR EMBL; DQ126302; AAZ39777.1; -; Genomic_DNA. DR EMBL; DQ126303; AAZ39778.1; -; Genomic_DNA. DR EMBL; DQ126304; AAZ39779.1; -; Genomic_DNA. DR EMBL; DQ126305; AAZ39780.1; -; Genomic_DNA. DR EMBL; DQ126306; AAZ39781.1; -; Genomic_DNA. DR EMBL; DQ126307; AAZ39782.1; -; Genomic_DNA. DR EMBL; DQ126308; AAZ39783.1; -; Genomic_DNA. DR EMBL; DQ126309; AAZ39784.1; -; Genomic_DNA. DR EMBL; DQ126310; AAZ39785.1; -; Genomic_DNA. DR EMBL; DQ126311; AAZ39786.1; -; Genomic_DNA. DR EMBL; DQ126312; AAZ39787.1; -; Genomic_DNA. DR EMBL; DQ126313; AAZ39788.1; -; Genomic_DNA. DR EMBL; DQ126314; AAZ39789.1; -; Genomic_DNA. DR EMBL; DQ126315; AAZ39790.1; -; Genomic_DNA. DR EMBL; DQ126316; AAZ39791.1; -; Genomic_DNA. DR EMBL; DQ126317; AAZ39792.1; -; Genomic_DNA. DR EMBL; DQ126318; AAZ39793.1; -; Genomic_DNA. DR EMBL; DQ126319; AAZ39794.1; -; Genomic_DNA. DR EMBL; DQ126320; AAZ39795.1; -; Genomic_DNA. DR EMBL; DQ126321; AAZ39796.1; -; Genomic_DNA. DR EMBL; DQ126322; AAZ39797.1; -; Genomic_DNA. DR EMBL; DQ126323; AAZ39798.1; -; Genomic_DNA. DR EMBL; DQ126324; AAZ39799.1; -; Genomic_DNA. DR EMBL; DQ126325; AAZ39800.1; -; Genomic_DNA. DR EMBL; CR536530; CAG38767.1; -; mRNA. DR EMBL; CR541913; CAG46711.1; -; mRNA. DR EMBL; BC007075; AAH07075.1; -; mRNA. DR EMBL; A01592; CAA00182.1; -; Unassigned_DNA. DR PIR; A53136; HBHU. DR UniGene; Hs.523443; -. DR PDB; 1A00; X-ray; B/D=3-147. DR PDB; 1A01; X-ray; B/D=3-147. DR PDB; 1A0U; X-ray; B/D=3-147. DR PDB; 1A0Z; X-ray; B/D=3-147. DR PDB; 1A3N; X-ray; B/D=1-147. DR PDB; 1A3O; X-ray; B/D=1-147. DR PDB; 1ABW; X-ray; B/D=3-147. DR PDB; 1ABY; X-ray; B/D=3-147. DR PDB; 1AJ9; X-ray; B=1-147. DR PDB; 1B86; X-ray; B/D=1-147. DR PDB; 1BAB; X-ray; B/D=1-147. DR PDB; 1BBB; X-ray; B/D=1-147. DR PDB; 1BIJ; X-ray; B/D=1-147. DR PDB; 1BUW; X-ray; B/D=-. DR PDB; 1BZ0; X-ray; B/D=1-147. DR PDB; 1BZ1; X-ray; B/D=1-147. DR PDB; 1BZZ; X-ray; B/D=1-147. DR PDB; 1C7B; X-ray; B/D=3-147. DR PDB; 1C7C; X-ray; B/D=3-147. DR PDB; 1C7D; X-ray; B/D=3-147. DR PDB; 1CBL; X-ray; A/B/C/D=1-147. DR PDB; 1CBM; X-ray; A/B/C/D=1-147. DR PDB; 1CLS; X-ray; B/D=1-147. DR PDB; 1CMY; X-ray; B/D=1-147. DR PDB; 1COH; X-ray; B/D=1-147. DR PDB; 1DKE; X-ray; B/D=1-147. DR PDB; 1DXT; X-ray; B/D=1-147. DR PDB; 1DXU; X-ray; B/D=3-147. DR PDB; 1DXV; X-ray; B/D=3-147. DR PDB; 1FN3; X-ray; B/D=1-147. DR PDB; 1G9V; X-ray; B/D=1-147. DR PDB; 1GBU; X-ray; B/D=1-147. DR PDB; 1GBV; X-ray; B/D=1-147. DR PDB; 1GLI; X-ray; B/D=3-147. DR PDB; 1GZX; X-ray; B/D=1-147. DR PDB; 1HAB; X-ray; B/D=1-147. DR PDB; 1HAC; X-ray; B/D=1-147. DR PDB; 1HBA; X-ray; B/D=1-147. DR PDB; 1HBB; X-ray; B/D=1-147. DR PDB; 1HBS; X-ray; B/D/F/H=1-147. DR PDB; 1HCO; X-ray; B=1-147. DR PDB; 1HDB; X-ray; B/D=1-147. DR PDB; 1HGA; X-ray; B/D=1-147. DR PDB; 1HGB; X-ray; B/D=1-147. DR PDB; 1HGC; X-ray; B/D=1-147. DR PDB; 1HHO; X-ray; B=1-147. DR PDB; 1IRD; X-ray; B=1-147. DR PDB; 1J3Y; X-ray; B/D/F/H=1-147. DR PDB; 1J3Z; X-ray; B/D/F/H=1-147. DR PDB; 1J40; X-ray; B/D/F/H=1-147. DR PDB; 1J41; X-ray; B/D/F/H=1-147. DR PDB; 1J7S; X-ray; B/D=3-147. DR PDB; 1J7W; X-ray; B/D=3-147. DR PDB; 1J7Y; X-ray; B/D=3-147. DR PDB; 1JY7; X-ray; B/D/Q/S/V/X=1-147. DR PDB; 1K0Y; X-ray; B/D=1-147. DR PDB; 1K1K; X-ray; B=1-147. DR PDB; 1KD2; X-ray; B/D=1-147. DR PDB; 1LFL; X-ray; B/D/Q/S=1-147. DR PDB; 1LFQ; X-ray; B=1-147. DR PDB; 1LFT; X-ray; B=1-147. DR PDB; 1LFV; X-ray; B=1-147. DR PDB; 1LFY; X-ray; B=1-147. DR PDB; 1LFZ; X-ray; B=1-147. DR PDB; 1LJW; X-ray; B=1-147. DR PDB; 1M9P; X-ray; B/D=1-147. DR PDB; 1MKO; X-ray; B/D=1-147. DR PDB; 1NEJ; X-ray; B/D=1-147. DR PDB; 1NIH; X-ray; B/D=1-147. DR PDB; 1NQP; X-ray; B/D=1-147. DR PDB; 1O1I; X-ray; B=1-147. DR PDB; 1O1J; X-ray; B/D=1-147. DR PDB; 1O1K; X-ray; B/D=1-147. DR PDB; 1O1L; X-ray; B/D=1-147. DR PDB; 1O1M; X-ray; B/D=1-147. DR PDB; 1O1N; X-ray; B/D=1-147. DR PDB; 1O1O; X-ray; B/D=1-147. DR PDB; 1O1P; X-ray; B/D=1-147. DR PDB; 1QI8; X-ray; B/D=3-147. DR PDB; 1QSH; X-ray; B/D=1-147. DR PDB; 1QSI; X-ray; B/D=1-147. DR PDB; 1QXD; X-ray; B/D=1-147. DR PDB; 1QXE; X-ray; B/D=1-147. DR PDB; 1R1X; X-ray; B=1-147. DR PDB; 1R1Y; X-ray; B/D=1-147. DR PDB; 1RPS; X-ray; B/D=1-147. DR PDB; 1RQ3; X-ray; B/D=1-147. DR PDB; 1RQ4; X-ray; B/D=1-147. DR PDB; 1RQA; X-ray; B/D=3-147. DR PDB; 1RVW; X-ray; B=1-147. DR PDB; 1SDK; X-ray; B/D=1-147. DR PDB; 1SDL; X-ray; B/D=1-147. DR PDB; 1THB; X-ray; B/D=1-147. DR PDB; 1UIW; X-ray; B/D/F/H=1-147. DR PDB; 1VWT; X-ray; B/D=1-147. DR PDB; 1XXT; X-ray; B/D=1-147. DR PDB; 1XY0; X-ray; B/D=1-147. DR PDB; 1XYE; X-ray; B/D=1-147. DR PDB; 1XZ2; X-ray; B/D=1-147. DR PDB; 1XZ4; X-ray; B/D=1-147. DR PDB; 1XZ5; X-ray; B/D=1-147. DR PDB; 1XZ7; X-ray; B/D=1-147. DR PDB; 1XZU; X-ray; B/D=1-147. DR PDB; 1XZV; X-ray; B/D=1-147. DR PDB; 1Y09; X-ray; B/D=1-147. DR PDB; 1Y0A; X-ray; B/D=1-147. DR PDB; 1Y0C; X-ray; B/D=1-147. DR PDB; 1Y0D; X-ray; B/D=1-147. DR PDB; 1Y0T; X-ray; B/D=3-147. DR PDB; 1Y0W; X-ray; B/D=3-147. DR PDB; 1Y22; X-ray; B/D=3-147. DR PDB; 1Y2Z; X-ray; B/D=3-147. DR PDB; 1Y31; X-ray; B/D=3-147. DR PDB; 1Y35; X-ray; B/D=3-147. DR PDB; 1Y45; X-ray; B/D=3-147. DR PDB; 1Y46; X-ray; B/D=3-147. DR PDB; 1Y4B; X-ray; B/D=3-147. DR PDB; 1Y4F; X-ray; B/D=3-147. DR PDB; 1Y4G; X-ray; B/D=3-147. DR PDB; 1Y4P; X-ray; B/D=3-147. DR PDB; 1Y4Q; X-ray; B/D=3-147. DR PDB; 1Y4R; X-ray; B/D=3-147. DR PDB; 1Y4V; X-ray; B/D=3-147. DR PDB; 1Y5F; X-ray; B/D=3-147. DR PDB; 1Y5J; X-ray; B/D=3-147. DR PDB; 1Y5K; X-ray; B/D=3-147. DR PDB; 1Y7C; X-ray; B/D=3-147. DR PDB; 1Y7D; X-ray; B/D=3-147. DR PDB; 1Y7G; X-ray; B/D=3-147. DR PDB; 1Y7Z; X-ray; B/D=3-147. DR PDB; 1Y83; X-ray; B/D=3-147. DR PDB; 1Y85; X-ray; B/D=1-146. DR PDB; 1Y8W; X-ray; B/D=1-147. DR PDB; 1YDZ; X-ray; B/D=1-147. DR PDB; 1YE0; X-ray; B/D=3-147. DR PDB; 1YE1; X-ray; B/D=3-147. DR PDB; 1YE2; X-ray; B/D=3-147. DR PDB; 1YEN; X-ray; B/D=3-147. DR PDB; 1YEO; X-ray; B/D=3-147. DR PDB; 1YEQ; X-ray; B/D=3-147. DR PDB; 1YEU; X-ray; B/D=3-147. DR PDB; 1YEV; X-ray; B/D=3-147. DR PDB; 1YFF; X-ray; B/D/F/H=1-147. DR PDB; 1YG5; X-ray; B/D=3-147. DR PDB; 1YGD; X-ray; B/D=3-147. DR PDB; 1YGF; X-ray; B/D=3-147. DR PDB; 1YH9; X-ray; B/D=1-147. DR PDB; 1YHE; X-ray; B/D=1-147. DR PDB; 1YHR; X-ray; B/D=1-147. DR PDB; 1YIE; X-ray; B/D=3-147. DR PDB; 1YIH; X-ray; B/D=3-147. DR PDB; 1YVQ; X-ray; B/D=1-147. DR PDB; 1YVT; X-ray; B=1-147. DR PDB; 1YZI; X-ray; B=1-147. DR PDB; 2D5Z; X-ray; B/D=1-147. DR PDB; 2D60; X-ray; B/D=1-147. DR PDB; 2DN1; X-ray; B=1-147. DR PDB; 2DN2; X-ray; B/D=1-147. DR PDB; 2DN3; X-ray; B=-. DR PDB; 2H35; NMR; B/D=-. DR PDB; 2HBC; X-ray; B=1-147. DR PDB; 2HBD; X-ray; B=1-147. DR PDB; 2HBE; X-ray; B=1-147. DR PDB; 2HBF; X-ray; B=1-147. DR PDB; 2HBS; X-ray; B/D/F/H=1-147. DR PDB; 2HCO; X-ray; B=1-147. DR PDB; 2HHD; X-ray; B/D=1-147. DR PDB; 2HHE; X-ray; B/D=4-147. DR PDB; 4HHB; X-ray; B/D=1-147. DR PDB; 6HBW; X-ray; B/D=1-147. DR IntAct; P68871; -. DR SWISS-2DPAGE; P68871; HUMAN. DR DOSAC-COBS-2DPAGE; P02023; HUMAN. DR HSC-2DPAGE; P68871; HUMAN. DR PMMA-2DPAGE; P68871; -. DR REPRODUCTION-2DPAGE; P68871; HUMAN. DR Siena-2DPAGE; P68871; -. DR Ensembl; ENSG00000188170; Homo sapiens. DR H-InvDB; HIX0009387; -. DR HGNC; HGNC:4827; HBB. DR MIM; 141900; gene+phenotype. DR MIM; 603903; phenotype. DR DrugBank; APRD01053; Iron Dextran. DR LinkHub; P68871; -. DR ArrayExpress; P68871; -. DR GermOnline; ENSG00000188170; Homo sapiens. DR RZPD-ProtExp; I0513; -. DR RZPD-ProtExp; RZPDo834D0222; -. DR RZPD-ProtExp; RZPDo834E0633; -. DR RZPD-ProtExp; RZPDo839B0670; -. DR GO; GO:0005833; C:hemoglobin complex; TAS:UniProtKB. DR GO; GO:0030492; F:hemoglobin binding; IDA:UniProtKB. DR GO; GO:0019825; F:oxygen binding; IDA:UniProtKB. DR GO; GO:0005344; F:oxygen transporter activity; NAS:UniProtKB. DR GO; GO:0008430; F:selenium binding; IDA:UniProtKB. DR GO; GO:0030185; P:nitric oxide transport; NAS:UniProtKB. DR GO; GO:0015671; P:oxygen transport; TAS:UniProtKB. DR GO; GO:0045429; P:positive regulation of nitric oxide biosynt...; NAS:UniProtKB. DR InterPro; IPR002337; Beta_haem. DR InterPro; IPR000971; Globin. DR InterPro; IPR009050; Globin_like. DR InterPro; IPR012292; Globin_related. DR Gene3D; G3DSA:1.10.490.10; Globin_related; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00814; BETAHAEM. DR PROSITE; PS01033; GLOBIN; 1. KW 3D-structure; Acetylation; Direct protein sequencing; KW Disease mutation; Heme; Iron; Metal-binding; Oxygen transport; KW Polymorphism; S-nitrosylation; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 147 Hemoglobin subunit beta. FT /FTId=PRO_0000052976. FT METAL 64 64 Iron (heme distal ligand). FT METAL 93 93 Iron (heme proximal ligand). FT MOD_RES 2 2 N-acetylalanine (in variant Raleigh). FT MOD_RES 94 94 S-nitrosocysteine. FT MOD_RES 145 145 N6-acetyllysine. FT CARBOHYD 2 2 N-linked (Glc) (glycation); in Hb A1C. FT VARIANT 2 2 V -> A (in Raleigh; O(2) affinity down). FT /FTId=VAR_002856. FT VARIANT 3 3 H -> L (in Graz). FT /FTId=VAR_002857. FT VARIANT 3 3 H -> Q (in Okayama; O(2) affinity up). FT /FTId=VAR_002858. FT VARIANT 3 3 H -> R (in Deer Lodge; O(2) affinity up). FT /FTId=VAR_002859. FT VARIANT 3 3 H -> Y (in Fukuoka). FT /FTId=VAR_002860. FT VARIANT 6 6 P -> R (in Warwickshire). FT /FTId=VAR_002861. FT VARIANT 7 7 E -> A (in G-Makassar). FT /FTId=VAR_002862. FT VARIANT 7 7 E -> K (in C). FT /FTId=VAR_002864. FT VARIANT 7 7 E -> Q (in Machida). FT /FTId=VAR_002865. FT VARIANT 7 7 E -> V (in S; sickle cell anemia; FT dbSNP:rs334). FT /FTId=VAR_002863. FT VARIANT 8 8 E -> G (in G-San Jose; mildly unstable). FT /FTId=VAR_002866. FT VARIANT 8 8 E -> K (in G-Siriraj). FT /FTId=VAR_002867. FT VARIANT 9 9 K -> E (in N-Timone). FT /FTId=VAR_002868. FT VARIANT 9 9 K -> Q (in J-Luhe). FT /FTId=VAR_002869. FT VARIANT 9 9 K -> T (in Rio Grande). FT /FTId=VAR_002870. FT VARIANT 10 10 S -> C (in Porto Alegre; O(2) affinity FT up). FT /FTId=VAR_002871. FT VARIANT 11 11 A -> D (in Ankara). FT /FTId=VAR_002872. FT VARIANT 11 11 A -> V (in Iraq-Halabja). FT /FTId=VAR_025393. FT VARIANT 12 12 V -> D (in Windsor; O(2) affinity up; FT unstable). FT /FTId=VAR_002873. FT VARIANT 12 12 V -> I (in Hamilton). FT /FTId=VAR_002874. FT VARIANT 14 14 A -> D (in J-Lens). FT /FTId=VAR_002875. FT VARIANT 15 15 L -> P (in Saki; unstable). FT /FTId=VAR_002876. FT VARIANT 15 15 L -> R (in Soegn; unstable). FT /FTId=VAR_002877. FT VARIANT 16 16 W -> G (in Randwick; unstable). FT /FTId=VAR_002878. FT VARIANT 16 16 W -> R (in Belfast; O(2) affinity up; FT unstable). FT /FTId=VAR_002879. FT VARIANT 17 17 G -> D (in J-Baltimore/J-Trinidad/J- FT Ireland/J-Georgia/N-New Haven). FT /FTId=VAR_002880. FT VARIANT 17 17 G -> R (in D-Bushman). FT /FTId=VAR_002881. FT VARIANT 18 18 K -> E (in Nagasaki). FT /FTId=VAR_002882. FT VARIANT 18 18 K -> N (in J-Amiens). FT /FTId=VAR_002883. FT VARIANT 18 18 K -> Q (in Nikosia). FT /FTId=VAR_002884. FT VARIANT 19 19 V -> M (in Baden; slightly unstable). FT /FTId=VAR_002885. FT VARIANT 20 20 N -> D (in Alamo). FT /FTId=VAR_002886. FT VARIANT 20 20 N -> K (in D-Ouleh RABAH). FT /FTId=VAR_002887. FT VARIANT 20 20 N -> S (in Malay). FT /FTId=VAR_002888. FT VARIANT 21 21 V -> M (in Olympia; O(2) affinity up). FT /FTId=VAR_002889. FT VARIANT 22 22 D -> G (in Connecticut; O(2) affinity FT down). FT /FTId=VAR_002890. FT VARIANT 22 22 D -> H (in Karlskoga). FT /FTId=VAR_002892. FT VARIANT 22 22 D -> N (in Cocody). FT /FTId=VAR_002891. FT VARIANT 22 22 D -> Y (in Yusa). FT /FTId=VAR_002893. FT VARIANT 23 23 E -> A (in G-Coushatta/G-Saskatoon/G- FT Taegu/Hsin Chu). FT /FTId=VAR_002894. FT VARIANT 23 23 E -> G (in G-Taipei). FT /FTId=VAR_002895. FT VARIANT 23 23 E -> K (in E-Saskatoon; unstable). FT /FTId=VAR_002896. FT VARIANT 23 23 E -> Q (in D-Iran). FT /FTId=VAR_002897. FT VARIANT 23 23 E -> V (in D-Granada). FT /FTId=VAR_002898. FT VARIANT 24 24 V -> D (in Strasbourg; O(2) affinity up). FT /FTId=VAR_002899. FT VARIANT 24 24 V -> F (in Palmerston North; O(2) FT affinity up; unstable). FT /FTId=VAR_002900. FT VARIANT 24 24 V -> G (in Miyashiro; O(2) affinity up; FT unstable). FT /FTId=VAR_002901. FT VARIANT 25 25 G -> D (in Moscva; O(2) affinity down; FT unstable). FT /FTId=VAR_002902. FT VARIANT 25 25 G -> R (in Riverdale-Bronx; O(2) affinity FT up; unstable). FT /FTId=VAR_002903. FT VARIANT 25 25 G -> V (in Savannah; unstable). FT /FTId=VAR_002904. FT VARIANT 26 26 G -> D (in J-Auckland; unstable; O(2) FT affinity down). FT /FTId=VAR_002905. FT VARIANT 26 26 G -> R (in G-Taiwan Ami). FT /FTId=VAR_002906. FT VARIANT 27 27 E -> K (in E). FT /FTId=VAR_002907. FT VARIANT 27 27 E -> V (in Henri Mondor; slightly FT unstable). FT /FTId=VAR_002908. FT VARIANT 28 28 A -> D (in Volga/Drenthe; unstable). FT /FTId=VAR_002909. FT VARIANT 28 28 A -> S (in Knossos). FT /FTId=VAR_002910. FT VARIANT 28 28 A -> V (in Grange-blanche; O(2) affinity FT up). FT /FTId=VAR_002911. FT VARIANT 29 29 L -> P (in Genova/Hyogo; unstable). FT /FTId=VAR_002912. FT VARIANT 30 30 G -> D (in Lufkin; unstable). FT /FTId=VAR_002913. FT VARIANT 31 31 R -> S (in Tacoma; unstable). FT /FTId=VAR_002914. FT VARIANT 32 32 L -> P (in Yokohama; unstable). FT /FTId=VAR_002915. FT VARIANT 33 33 L -> R (in Castilla; unstable). FT /FTId=VAR_002916. FT VARIANT 33 33 L -> V (in Muscat; slightly unstable). FT /FTId=VAR_002917. FT VARIANT 35 35 V -> D (in Santander; unstable). FT /FTId=VAR_025394. FT VARIANT 35 35 V -> F (in Pitie-Salpetriere; O(2) FT affinity up). FT /FTId=VAR_002918. FT VARIANT 35 35 V -> L (in Nantes; increased oxygen FT affinity). FT /FTId=VAR_025395. FT VARIANT 36 36 Y -> F (in Philly; O(2) affinity up; FT unstable). FT /FTId=VAR_002919. FT VARIANT 37 37 P -> R (in Sunnybrook). FT /FTId=VAR_002920. FT VARIANT 37 37 P -> S (in North Chicago; O(2) affinity FT up). FT /FTId=VAR_002921. FT VARIANT 37 37 P -> T (in Linkoping/Finlandia; O(2) FT affinity up). FT /FTId=VAR_002922. FT VARIANT 38 38 W -> G (in Howick). FT /FTId=VAR_002923. FT VARIANT 38 38 W -> R (in Rothschild; O(2) affinity FT down). FT /FTId=VAR_002925. FT VARIANT 38 38 W -> S (in Hirose; O(2) affinity up). FT /FTId=VAR_002924. FT VARIANT 39 39 T -> N (in Hinwil; O(2) affinity up). FT /FTId=VAR_002926. FT VARIANT 40 40 Q -> E (in Vaasa; unstable). FT /FTId=VAR_002927. FT VARIANT 40 40 Q -> K (in Alabama). FT /FTId=VAR_002928. FT VARIANT 40 40 Q -> R (in Tianshui). FT /FTId=VAR_002929. FT VARIANT 42 42 F -> Y (in Mequon). FT /FTId=VAR_002930. FT VARIANT 43 43 F -> L (in Louisville; unstable). FT /FTId=VAR_002931. FT VARIANT 44 44 E -> Q (in Hoshida/Chaya). FT /FTId=VAR_002932. FT VARIANT 45 45 S -> C (in Mississippi). FT /FTId=VAR_002933. FT VARIANT 46 46 F -> S (in Cheverly; unstable). FT /FTId=VAR_002934. FT VARIANT 47 47 G -> E (in K-Ibadan). FT /FTId=VAR_002935. FT VARIANT 48 48 D -> A (in Avicenna). FT /FTId=VAR_002936. FT VARIANT 48 48 D -> G (in Gavello). FT /FTId=VAR_002937. FT VARIANT 48 48 D -> Y (in Maputo). FT /FTId=VAR_002938. FT VARIANT 49 49 L -> P (in Bab-Saadoum; slightly FT unstable). FT /FTId=VAR_002939. FT VARIANT 50 50 S -> F (in Las Palmas; slightly FT unstable). FT /FTId=VAR_002940. FT VARIANT 51 51 T -> K (in Edmonton). FT /FTId=VAR_002941. FT VARIANT 52 52 P -> R (in Willamette; O(2) affinity up; FT unstable). FT /FTId=VAR_002942. FT VARIANT 53 53 D -> A (in Ocho Rios). FT /FTId=VAR_002943. FT VARIANT 53 53 D -> H (in Summer Hill). FT /FTId=VAR_002944. FT VARIANT 55 55 V -> D (in Jacksonville; O(2) affinity FT up; unstable). FT /FTId=VAR_002945. FT VARIANT 56 56 M -> K (in Matera; unstable). FT /FTId=VAR_002946. FT VARIANT 57 57 G -> R (in Hamadan). FT /FTId=VAR_002947. FT VARIANT 58 58 N -> K (in G-ferrara; unstable). FT /FTId=VAR_002948. FT VARIANT 59 59 P -> R (in Dhofar/Yukuhashi). FT /FTId=VAR_002949. FT VARIANT 60 60 K -> E (in I-High Wycombe). FT /FTId=VAR_002950. FT VARIANT 61 61 V -> A (in Collingwood; unstable). FT /FTId=VAR_002951. FT VARIANT 62 62 K -> E (in N-Seatlle). FT /FTId=VAR_002952. FT VARIANT 62 62 K -> M (in Bologna; O(2) affinity down). FT /FTId=VAR_002953. FT VARIANT 62 62 K -> N (in Hikari). FT /FTId=VAR_002954. FT VARIANT 63 63 A -> D (in J-Europa). FT /FTId=VAR_002955. FT VARIANT 63 63 A -> P (in Duarte; unstable). FT /FTId=VAR_002956. FT VARIANT 64 64 H -> Y (in M-Saskatoon; O(2) affinity FT up). FT /FTId=VAR_002957. FT VARIANT 66 66 K -> M (in J-Antakya). FT /FTId=VAR_002958. FT VARIANT 66 66 K -> N (in J-Sicilia). FT /FTId=VAR_002959. FT VARIANT 66 66 K -> Q (in J-Cairo). FT /FTId=VAR_002960. FT VARIANT 67 67 K -> T (in Chico; O(2) affinity down). FT /FTId=VAR_002961. FT VARIANT 68 68 V -> A (in Sydney; unstable). FT /FTId=VAR_002962. FT VARIANT 68 68 V -> M (in Alesha; unstable). FT /FTId=VAR_002963. FT VARIANT 69 69 L -> H (in Brisbane; O(2) affinity up). FT /FTId=VAR_002964. FT VARIANT 69 69 L -> P (in Mizuho; unstable). FT /FTId=VAR_002965. FT VARIANT 70 70 G -> D (in Rambam). FT /FTId=VAR_002966. FT VARIANT 70 70 G -> R (in Kenitra). FT /FTId=VAR_002967. FT VARIANT 70 70 G -> S (in City of Hope). FT /FTId=VAR_002968. FT VARIANT 71 71 A -> D (in Seattle; O(2) affinity down; FT unstable). FT /FTId=VAR_002969. FT VARIANT 72 72 F -> S (in Christchurch; unstable). FT /FTId=VAR_002970. FT VARIANT 74 74 D -> G (in Tilburg; O(2) affinity down). FT /FTId=VAR_002971. FT VARIANT 74 74 D -> V (in Mobile; O(2) affinity down). FT /FTId=VAR_002972. FT VARIANT 74 74 D -> Y (in Vancouver; O(2) affinity FT down). FT /FTId=VAR_002973. FT VARIANT 75 75 G -> R (in Aalborg; unstable). FT /FTId=VAR_002974. FT VARIANT 75 75 G -> V (in Bushwick; unstable). FT /FTId=VAR_002975. FT VARIANT 76 76 L -> P (in Atlanta; unstable). FT /FTId=VAR_002976. FT VARIANT 76 76 L -> R (in Pasadena; O(2) affinity up; FT unstable). FT /FTId=VAR_002977. FT VARIANT 77 77 A -> D (in J-Chicago). FT /FTId=VAR_002978. FT VARIANT 78 78 H -> D (in J-Iran). FT /FTId=VAR_002979. FT VARIANT 78 78 H -> R (in Costa Rica). FT /FTId=VAR_002980. FT VARIANT 78 78 H -> Y (in Fukuyama). FT /FTId=VAR_002981. FT VARIANT 79 79 L -> R (in Quin-hai). FT /FTId=VAR_002982. FT VARIANT 80 80 D -> Y (in Tampa). FT /FTId=VAR_002983. FT VARIANT 81 81 N -> K (in G-Szuhu/Gifu). FT /FTId=VAR_002984. FT VARIANT 82 82 L -> H (in La Roche-sur-Yon; unstable and FT O(2) affinity up). FT /FTId=VAR_012663. FT VARIANT 82 82 L -> R (in Baylor; unstable). FT /FTId=VAR_002985. FT VARIANT 83 83 K -> M (in Helsinki; O(2) affinity up). FT /FTId=VAR_002986. FT VARIANT 83 83 K -> N (in Providence). FT /FTId=VAR_012664. FT VARIANT 84 84 G -> D (in Pyrgos). FT /FTId=VAR_025396. FT VARIANT 84 84 G -> R (in Muskegon). FT /FTId=VAR_002987. FT VARIANT 85 85 T -> I (in Kofu). FT /FTId=VAR_002988. FT VARIANT 87 87 A -> D (in Olomouc; O(2) affinity up). FT /FTId=VAR_002989. FT VARIANT 88 88 T -> I (in Quebec-Chori). FT /FTId=VAR_002990. FT VARIANT 88 88 T -> K (in D-Ibadan). FT /FTId=VAR_002991. FT VARIANT 88 88 T -> P (in Valletta). FT /FTId=VAR_002992. FT VARIANT 89 89 L -> P (in Santa Ana; unstable). FT /FTId=VAR_002993. FT VARIANT 89 89 L -> R (in Boras; unstable). FT /FTId=VAR_002994. FT VARIANT 90 90 S -> N (in Creteil; O(2) affinity up). FT /FTId=VAR_002995. FT VARIANT 90 90 S -> R (in Vanderbilt; O(2) affinity up). FT /FTId=VAR_002996. FT VARIANT 91 91 E -> D (in Pierre-Benite; O(2) affinity FT up). FT /FTId=VAR_002997. FT VARIANT 91 91 E -> K (in Agenogi; O(2) affinity down). FT /FTId=VAR_002998. FT VARIANT 92 92 L -> P (in Sabine; unstable). FT /FTId=VAR_002999. FT VARIANT 92 92 L -> R (in Caribbean; O(2) affinity down; FT unstable). FT /FTId=VAR_003000. FT VARIANT 93 93 H -> D (in J-Altgelds Gardens; unstable). FT /FTId=VAR_003001. FT VARIANT 93 93 H -> N (in Isehara; unstable). FT /FTId=VAR_003002. FT VARIANT 93 93 H -> P (in Newcastle and Duino; FT associated with S-104 in Duino; FT unstable). FT /FTId=VAR_003003. FT VARIANT 93 93 H -> Q (in Istambul; O(2) affinity up; FT unstable). FT /FTId=VAR_003004. FT VARIANT 94 94 C -> R (in Okazaki; O(2) affinity up; FT unstable). FT /FTId=VAR_003005. FT VARIANT 95 95 D -> G (in Chandigarh). FT /FTId=VAR_003006. FT VARIANT 95 95 D -> H (in Barcelona; O(2) affinity up). FT /FTId=VAR_003007. FT VARIANT 95 95 D -> N (in Bunbury; O(2) affinity up). FT /FTId=VAR_003008. FT VARIANT 96 96 K -> M (in J-Cordoba). FT /FTId=VAR_003009. FT VARIANT 96 96 K -> N (in Detroit). FT /FTId=VAR_003010. FT VARIANT 97 97 L -> P (in Debrousse; unstable; O(2) FT affinity up). FT /FTId=VAR_003011. FT VARIANT 97 97 L -> V (in Regina; O(2) affinity up). FT /FTId=VAR_003012. FT VARIANT 98 98 H -> L (in Wood; O(2) affinity up). FT /FTId=VAR_003013. FT VARIANT 98 98 H -> P (in Nagoya; O(2) affinity up; FT unstable). FT /FTId=VAR_003014. FT VARIANT 98 98 H -> Q (in Malmoe; O(2) affinity up). FT /FTId=VAR_003015. FT VARIANT 98 98 H -> Y (in Moriguchi). FT /FTId=VAR_003016. FT VARIANT 99 99 V -> G (in Nottingham; unstable). FT /FTId=VAR_003017. FT VARIANT 100 100 D -> E (in Coimbra; O(2) affinity up). FT /FTId=VAR_003018. FT VARIANT 101 101 P -> L (in Brigham; O(2) affinity up). FT /FTId=VAR_003019. FT VARIANT 101 101 P -> R (in New Mexico). FT /FTId=VAR_003020. FT VARIANT 102 102 E -> D (in Potomac; O(2) affinity up). FT /FTId=VAR_003021. FT VARIANT 102 102 E -> G (in Alberta; O(2) affinity up). FT /FTId=VAR_003022. FT VARIANT 102 102 E -> K (in British Columbia; O(2) FT affinity up). FT /FTId=VAR_003023. FT VARIANT 102 102 E -> Q (in Rush; unstable). FT /FTId=VAR_003024. FT VARIANT 103 103 N -> S (in Beth Israel; O(2) affinity FT down; unstable). FT /FTId=VAR_003025. FT VARIANT 103 103 N -> Y (in St Mande; O(2) affinity down). FT /FTId=VAR_003026. FT VARIANT 104 104 F -> L (in Heathrow; O(2) affinity up). FT /FTId=VAR_003027. FT VARIANT 105 105 R -> S (in Camperdown and Duino; FT associated with P-92 in Duino; unstable). FT /FTId=VAR_003028. FT VARIANT 105 105 R -> T (in Sherwood Forest). FT /FTId=VAR_003029. FT VARIANT 108 108 G -> R (in Burke; O(2) affinity down; FT unstable). FT /FTId=VAR_003030. FT VARIANT 109 109 N -> K (in Presbyterian; O(2) affinity FT down; unstable). FT /FTId=VAR_003031. FT VARIANT 110 110 V -> M (in San Diego; O(2) affinity up). FT /FTId=VAR_003032. FT VARIANT 111 111 L -> P (in Showa-Yakushiji). FT /FTId=VAR_003033. FT VARIANT 112 112 V -> A (in Stanmore; O(2) affinity down; FT unstable). FT /FTId=VAR_003034. FT VARIANT 113 113 C -> F (in Canterbury). FT /FTId=VAR_025397. FT VARIANT 113 113 C -> R (in Indianapolis). FT /FTId=VAR_003035. FT VARIANT 113 113 C -> Y (in Yahata). FT /FTId=VAR_003036. FT VARIANT 115 115 L -> M (in Zengcheng). FT /FTId=VAR_010144. FT VARIANT 115 115 L -> P (in Durham-N.C./Brescia; causes FT beta-thalassemia). FT /FTId=VAR_010145. FT VARIANT 116 116 A -> D (in Hradec Kralove; unstable; FT causes severe beta-thalassemia). FT /FTId=VAR_003037. FT VARIANT 116 116 A -> P (in Madrid; unstable). FT /FTId=VAR_003038. FT VARIANT 117 117 H -> L (in Vexin; increased oxygen FT affinity). FT /FTId=VAR_025398. FT VARIANT 117 117 H -> Q (in Hafnia). FT /FTId=VAR_003039. FT VARIANT 118 118 H -> P (in Saitama; unstable). FT /FTId=VAR_003040. FT VARIANT 118 118 H -> R (in P-Galveston). FT /FTId=VAR_003041. FT VARIANT 118 118 H -> Y (in Tsukumi). FT /FTId=VAR_025399. FT VARIANT 120 120 G -> A (in Iowa). FT /FTId=VAR_003042. FT VARIANT 121 121 K -> E (in Hijiyama). FT /FTId=VAR_003043. FT VARIANT 121 121 K -> I (in Jianghua). FT /FTId=VAR_003044. FT VARIANT 121 121 K -> Q (in Takamatsu). FT /FTId=VAR_003045. FT VARIANT 122 122 E -> A (in D-Neath). FT /FTId=VAR_003046. FT VARIANT 122 122 E -> G (in St Francis). FT /FTId=VAR_003047. FT VARIANT 122 122 E -> K (in O-Arab). FT /FTId=VAR_003049. FT VARIANT 122 122 E -> Q (in D-Los Angeles/D-Punjab/D- FT Portugal/D-Chicago/D-Oak Ridge). FT /FTId=VAR_003048. FT VARIANT 122 122 E -> V (in D-Camperdown/Beograd). FT /FTId=VAR_003050. FT VARIANT 124 124 T -> I (in Villejuif; asymptomatic FT variant). FT /FTId=VAR_003051. FT VARIANT 125 125 P -> Q (in Ty Gard; O(2) affinity up). FT /FTId=VAR_003053. FT VARIANT 125 125 P -> R (in Khartoum; unstable). FT /FTId=VAR_003052. FT VARIANT 125 125 P -> S (in Tunis). FT /FTId=VAR_003054. FT VARIANT 127 127 V -> A (in Beirut). FT /FTId=VAR_003055. FT VARIANT 127 127 V -> E (in Hofu; unstable). FT /FTId=VAR_003057. FT VARIANT 127 127 V -> G (in Dhonburi/Neapolis; unstable; FT beta-thalassemia). FT /FTId=VAR_003056. FT VARIANT 128 128 Q -> E (in Complutense). FT /FTId=VAR_003058. FT VARIANT 128 128 Q -> K (in Brest; unstable). FT /FTId=VAR_003059. FT VARIANT 129 129 A -> D (in J-Guantanamo; unstable). FT /FTId=VAR_003060. FT VARIANT 130 130 A -> P (in Crete; O(2) affinity up; FT unstable). FT /FTId=VAR_003061. FT VARIANT 130 130 A -> V (in La Desirade; O(2) affinity FT down; unstable). FT /FTId=VAR_003062. FT VARIANT 131 131 Y -> D (in Wien; unstable). FT /FTId=VAR_003063. FT VARIANT 131 131 Y -> S (in Nevers). FT /FTId=VAR_003064. FT VARIANT 132 132 Q -> E (in Camden/Tokuchi/Motown). FT /FTId=VAR_003065. FT VARIANT 132 132 Q -> K (in Shelby/Leslie/Deaconess; FT unstable). FT /FTId=VAR_003066. FT VARIANT 132 132 Q -> P (in Shangai; unstable). FT /FTId=VAR_003067. FT VARIANT 132 132 Q -> R (in Sarrebourg; unstable). FT /FTId=VAR_003068. FT VARIANT 133 133 K -> N (in Yamagata; O(2) affinity down). FT /FTId=VAR_003069. FT VARIANT 133 133 K -> Q (in K-Woolwich). FT /FTId=VAR_003070. FT VARIANT 134 134 V -> L (in Extredemura). FT /FTId=VAR_003071. FT VARIANT 135 135 V -> E (in North Shore-Caracas; FT unstable). FT /FTId=VAR_003072. FT VARIANT 136 136 A -> E (in Beckman; O(2) affinity down; FT unstable). FT /FTId=VAR_003073. FT VARIANT 136 136 A -> P (in Altdorf; O(2) affinity up; FT unstable). FT /FTId=VAR_003074. FT VARIANT 137 137 G -> D (in Hope; O(2) affinity down; FT unstable). FT /FTId=VAR_003075. FT VARIANT 139 139 A -> P (in Brockton; unstable). FT /FTId=VAR_003076. FT VARIANT 140 140 N -> D (in Geelong; unstable). FT /FTId=VAR_003077. FT VARIANT 140 140 N -> K (in Hinsdale; O(2) affinity down). FT /FTId=VAR_003078. FT VARIANT 140 140 N -> S (in S-Wake; associated with V-6). FT /FTId=VAR_025335. FT VARIANT 140 140 N -> Y (in Aurora; O(2) affinity up). FT /FTId=VAR_003079. FT VARIANT 141 141 A -> D (in Himeji; unstable; O(2) FT affinity down). FT /FTId=VAR_003080. FT VARIANT 141 141 A -> T (in St Jacques: O(2) affinity up). FT /FTId=VAR_003081. FT VARIANT 141 141 A -> V (in Puttelange; polycythemia; O(2) FT affinity up). FT /FTId=VAR_003082. FT VARIANT 142 142 L -> R (in Olmsted; unstable). FT /FTId=VAR_003083. FT VARIANT 143 143 A -> D (in Ohio; O(2) affinity up). FT /FTId=VAR_003084. FT VARIANT 144 144 H -> D (in Rancho Mirage). FT /FTId=VAR_003085. FT VARIANT 144 144 H -> P (in Syracuse; O(2) affinity up). FT /FTId=VAR_003087. FT VARIANT 144 144 H -> Q (in Little Rock; O(2) affinity FT up). FT /FTId=VAR_003086. FT VARIANT 144 144 H -> R (in Abruzzo; O(2) affinity up). FT /FTId=VAR_003088. FT VARIANT 145 145 K -> E (in Mito; O(2) affinity up). FT /FTId=VAR_003089. FT VARIANT 146 146 Y -> C (in Rainier; O(2) affinity up). FT /FTId=VAR_003090. FT VARIANT 146 146 Y -> H (in Bethesda; O(2) affinity up). FT /FTId=VAR_003091. FT VARIANT 147 147 H -> D (in Hiroshima; O(2) affinity up). FT /FTId=VAR_003092. FT VARIANT 147 147 H -> L (in Cowtown; O(2) affinity up). FT /FTId=VAR_003093. FT VARIANT 147 147 H -> P (in York; O(2) affinity up). FT /FTId=VAR_003094. FT VARIANT 147 147 H -> Q (in Kodaira; O(2) affinity up). FT /FTId=VAR_003095. FT HELIX 5 15 FT TURN 20 22 FT HELIX 23 34 FT HELIX 36 41 FT HELIX 43 45 FT HELIX 51 56 FT HELIX 58 76 FT TURN 77 79 FT HELIX 81 93 FT TURN 94 96 FT HELIX 101 118 FT HELIX 119 121 FT HELIX 124 141 FT HELIX 143 145 SQ SEQUENCE 147 AA; 15998 MW; A31F6D621C6556A1 CRC64; MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG KEFTPPVQAA YQKVVAGVAN ALAHKYH // ID HBB_PANPA Reviewed; 147 AA. AC P68872; P02023; Q13852; Q14481; Q14510; Q9BX96; Q9UCP8; Q9UCP9; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 20. DE Hemoglobin subunit beta (Hemoglobin beta chain) (Beta-globin). GN Name=HBB; OS Pan paniscus (Pygmy chimpanzee) (Bonobo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9597; RN [1] RP PROTEIN SEQUENCE OF 2-147. RX MEDLINE=83219265; PubMed=6406908; DOI=10.1038/303546a0; RA Goodman M., Braunitzer G., Stangl A., Schrank B.; RT "Evidence on human origins from haemoglobins of African apes."; RL Nature 303:546-548(1983). CC -!- FUNCTION: Involved in oxygen transport from the lung to the CC various peripheral tissues. CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in CC adult hemoglobin A (HbA). CC -!- TISSUE SPECIFICITY: Red blood cells. CC -!- SIMILARITY: Belongs to the globin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; D93303; HBCZP. DR SMR; P68872; 2-147. DR InterPro; IPR002337; Beta_haem. DR InterPro; IPR000971; Globin. DR InterPro; IPR009050; Globin_like. DR InterPro; IPR012292; Globin_related. DR Gene3D; G3DSA:1.10.490.10; Globin_related; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00814; BETAHAEM. DR PROSITE; PS01033; GLOBIN; 1. KW Direct protein sequencing; Heme; Iron; Metal-binding; KW Oxygen transport; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 147 Hemoglobin subunit beta. FT /FTId=PRO_0000053056. FT METAL 64 64 Iron (heme distal ligand). FT METAL 93 93 Iron (heme proximal ligand). SQ SEQUENCE 147 AA; 15998 MW; A31F6D621C6556A1 CRC64; MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG KEFTPPVQAA YQKVVAGVAN ALAHKYH // ID HBB_PANTR Reviewed; 147 AA. AC P68873; P02023; Q13852; Q14481; Q14510; Q28799; Q9BX96; Q9UCP8; AC Q9UCP9; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 20-MAR-2007, entry version 24. DE Hemoglobin subunit beta (Hemoglobin beta chain) (Beta-globin). GN Name=HBB; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-121. RX MEDLINE=85210896; PubMed=3999143; DOI=10.1016/0022-2836(85)90024-5; RA Savatier P., Trabuchet G., Faure C., Chebloune Y., Gouy M., RA Verdier G., Nigon V.M.; RT "Evolution of the primate beta-globin gene region. High rate of RT variation in CpG dinucleotides and in short repeated sequences between RT man and chimpanzee."; RL J. Mol. Biol. 182:21-29(1985). RN [2] RP PROTEIN SEQUENCE OF 2-147. RX MEDLINE=66071496; PubMed=5855051; RA Rifkin D.B., Konigsberg W.; RT "The characterization of the tryptic peptides from the hemoglobin of RT the chimpanzee (Pan troglodytes)."; RL Biochim. Biophys. Acta 104:457-461(1965). CC -!- FUNCTION: Involved in oxygen transport from the lung to the CC various peripheral tissues. CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains in CC adult hemoglobin A (HbA). CC -!- TISSUE SPECIFICITY: Red blood cells. CC -!- SIMILARITY: Belongs to the globin family. CC -!- CAUTION: Ref.1 sequence differs from that shown due to erroneous CC gene model prediction. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X02345; CAA26204.1; -; Genomic_DNA. DR PIR; B93303; HBCZ. DR SMR; P68873; 2-147. DR KEGG; hsa:3043; -. DR KEGG; ptr:450978; -. DR InterPro; IPR002337; Beta_haem. DR InterPro; IPR000971; Globin. DR InterPro; IPR009050; Globin_like. DR InterPro; IPR012292; Globin_related. DR Gene3D; G3DSA:1.10.490.10; Globin_related; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00814; BETAHAEM. DR PROSITE; PS01033; GLOBIN; 1. KW Direct protein sequencing; Heme; Iron; Metal-binding; KW Oxygen transport; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 147 Hemoglobin subunit beta. FT /FTId=PRO_0000053060. FT METAL 64 64 Iron (heme distal ligand). FT METAL 93 93 Iron (heme proximal ligand). SQ SEQUENCE 147 AA; 15998 MW; A31F6D621C6556A1 CRC64; MVHLTPEEKS AVTALWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS TPDAVMGNPK VKAHGKKVLG AFSDGLAHLD NLKGTFATLS ELHCDKLHVD PENFRLLGNV LVCVLAHHFG KEFTPPVQAA YQKVVAGVAN ALAHKYH // ID LACI_ECOLI Reviewed; 360 AA. AC P03023; O09196; P71309; Q2MC79; Q47338; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2003, sequence version 3. DT 20-MAR-2007, entry version 87. DE Lactose operon repressor. GN Name=lacI; OrderedLocusNames=b0345, JW0336; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=78246991; PubMed=355891; DOI=10.1038/274765a0; RA Farabaugh P.J.; RT "Sequence of the lacI gene."; RL Nature 274:765-769(1978). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Chen J., Matthews K.K.S.M.; RL Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Marsh S.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [7] RP PROTEIN SEQUENCE OF 1-147; 159-230 AND 233-360. RX MEDLINE=76091932; PubMed=1107032; RA Beyreuther K., Adler K., Fanning E., Murray C., Klemm A., Geisler N.; RT "Amino-acid sequence of lac repressor from Escherichia coli. RT Isolation, sequence analysis and sequence assembly of tryptic peptides RT and cyanogen-bromide fragments."; RL Eur. J. Biochem. 59:491-509(1975). RN [8] RP PROTEIN SEQUENCE OF 1-59; 96-101; 206-215 AND 328-347. RX MEDLINE=73143730; PubMed=4571224; RA Platt T., Files J.G., Weber K.; RT "Lac repressor. Specific proteolytic destruction of the NH 2 -terminal RT region and loss of the deoxyribonucleic acid-binding activity."; RL J. Biol. Chem. 248:110-121(1973). RN [9] RP PROTEIN SEQUENCE OF 60-70; 73-78 AND 83-86. RX MEDLINE=74126378; PubMed=4594037; RA Ganem D., Miller J.H., Files J.G., Platt T., Weber K.; RT "Reinitiation of a lac repressor fragment at a condon other than RT AUG."; RL Proc. Natl. Acad. Sci. U.S.A. 70:3165-3169(1973). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60. RX MEDLINE=88230449; PubMed=3286877; DOI=10.1016/0022-2836(88)90237-9; RA Gordon A.J.E., Burns P.A., Fix D.F., Yatagai F., Allen F.L., RA Horsfall M.J., Halliday J.A., Gray J., Bernelot-Moens C., RA Glickman B.W.; RT "Missense mutation in the lacI gene of Escherichia coli. Inferences on RT the structure of the repressor protein."; RL J. Mol. Biol. 200:239-251(1988). RN [11] RP PROTEIN SEQUENCE OF 1-35. RX MEDLINE=96087076; PubMed=7498473; DOI=10.1016/0014-5793(95)01153-6; RA Kamashev D.E., Esipova N.G., Ebralidse K.K., Mirzabekov A.D.; RT "Mechanism of Lac repressor switch-off: orientation of the Lac RT repressor DNA-binding domain is reversed upon inducer binding."; RL FEBS Lett. 375:27-30(1995). RN [12] RP MUTAGENESIS. RX MEDLINE=90183956; PubMed=2178920; RA Lehming N., Sartorius J., Kisters-Woike B., von Wilcken-Bergmann B., RA Mueller-Hill B.; RT "Mutant lac repressors with new specificities hint at rules for RT protein-DNA recognition."; RL EMBO J. 9:615-621(1990). RN [13] RP MUTAGENESIS. RX MEDLINE=94322386; PubMed=8046748; DOI=10.1006/jmbi.1994.1458; RA Markiewicz P., Kleina L.G., Cruz C., Ehret S., Miller J.H.; RT "Genetic studies of the lac repressor. XIV. Analysis of 4000 altered RT Escherichia coli lac repressors reveals essential and non-essential RT residues, as well as 'spacers' which do not require a specific RT sequence."; RL J. Mol. Biol. 240:421-433(1994). RN [14] RP 3D-STRUCTURE MODELING. RX MEDLINE=91249837; PubMed=2040302; RA Kisters-Woike B., Lehming N., Sartorius J., von Wilcken-Bergmann B., RA Mueller-Hill B.; RT "A model of the lac repressor-operator complex based on physical and RT genetic data."; RL Eur. J. Biochem. 198:411-419(1991). RN [15] RP 3D-STRUCTURE MODELING OF 1-56. RX MEDLINE=92020210; PubMed=1923807; DOI=10.1093/nar/19.19.5233; RA Shin J.A., Ebright R.H., Dervan P.B.; RT "Orientation of the Lac repressor DNA binding domain in complex with RT the left lac operator half site characterized by affinity cleaving."; RL Nucleic Acids Res. 19:5233-5236(1991). RN [16] RP STRUCTURE BY NMR. RX MEDLINE=89113344; PubMed=3064080; RA Boelens R., Lamerichs R.M.J.N., Rullmann J.A.C., van Boom J.H., RA Kaptein R.; RT "The interaction of lac repressor headpiece with its operator: an NMR RT view."; RL Protein Seq. Data Anal. 1:487-498(1988). RN [17] RP STRUCTURE BY NMR. RX MEDLINE=89302886; PubMed=2742823; DOI=10.1021/bi00433a037; RA Lamerichs R.M.J.N., Boelens R., van der Marel G.A., van Boom J.H., RA Kaptein R., Buck F., Fera B., Rueterjans H.; RT "H NMR study of a complex between the lac repressor headpiece and a 22 RT base pair symmetric lac operator."; RL Biochemistry 28:2985-2991(1989). RN [18] RP STRUCTURE BY NMR OF 1-56. RX MEDLINE=96275660; PubMed=8683581; DOI=10.1006/jmbi.1996.0356; RA Slijper M., Bonvin A.M., Boelens R., Kaptein R.; RT "Refined structure of lac repressor headpiece (1-56) determined by RT relaxation matrix calculations from 2D and 3D NOE data: change of RT tertiary structure upon binding to the lac operator."; RL J. Mol. Biol. 259:761-773(1996). RN [19] RP STRUCTURE BY NMR OF 1-62. RX MEDLINE=20113476; PubMed=10647179; DOI=10.1016/S0969-2126(00)88339-2; RA Spronk C.A., Bonvin A.M., Radha P.K., Melacini G., Boelens R., RA Kaptein R.; RT "The solution structure of Lac repressor headpiece 62 complexed to a RT symmetrical lac operator."; RL Structure 7:1483-1492(1999). RN [20] RP X-RAY CRYSTALLOGRAPHY (4.8 ANGSTROMS). RX MEDLINE=96239623; PubMed=8638105; RA Lewis M., Chang G., Horton N.C., Kercher M.A., Pace H.C., RA Schumacher M.A., Brennan R.G., Lu P.; RT "Crystal structure of the lactose operon repressor and its complexes RT with DNA and inducer."; RL Science 271:1247-1254(1996). CC -!- FUNCTION: Repressor of the lactose operon. Binds allolactose as an CC inducer. CC -!- SUBUNIT: Homotetramer. CC -!- INTERACTION: CC P00722:lacZ; NbExp=1; IntAct=EBI-909231, EBI-369998; CC -!- MISCELLANEOUS: Removing residues 1-59 results in loss of DNA- CC binding activity but retains tetrameric structure and inducer- CC binding activity. Deleting residues 340-360 results in loss of CC tetramer formation, but retains dimer formation, inducer-binding CC activity, and DNA-binding activity (if residues 1-59 are present). CC -!- SIMILARITY: Contains 1 HTH lacI-type DNA-binding domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; V00294; CAA23569.1; -; Genomic_DNA. DR EMBL; X58469; CAA41383.1; -; Genomic_DNA. DR EMBL; U86347; AAB47270.1; ALT_INIT; Genomic_DNA. DR EMBL; J01636; AAA24052.1; -; Genomic_DNA. DR EMBL; U72488; AAB36549.1; -; Genomic_DNA. DR EMBL; U78872; AAB37348.1; -; Genomic_DNA. DR EMBL; U78873; AAB37351.1; -; Genomic_DNA. DR EMBL; U78874; AAB37354.1; -; Genomic_DNA. DR EMBL; U73857; AAB18069.1; ALT_INIT; Genomic_DNA. DR EMBL; U00096; AAC73448.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76127.1; -; Genomic_DNA. DR PIR; A93198; RPECL. DR PDB; 1CJG; NMR; A/B=1-62. DR PDB; 1EFA; X-ray; A/B/C=1-333. DR PDB; 1JWL; X-ray; A/B/C=1-333. DR PDB; 1JYE; X-ray; A=1-349. DR PDB; 1JYF; X-ray; A=1-349. DR PDB; 1L1M; NMR; A/B=1-62. DR PDB; 1LBG; X-ray; A/B/C/D=1-360. DR PDB; 1LBH; X-ray; A/B/C/D=1-360. DR PDB; 1LBI; X-ray; A/B/C/D=1-360. DR PDB; 1LCC; NMR; A=1-51. DR PDB; 1LCD; NMR; A=1-51. DR PDB; 1LQC; NMR; @=1-56. DR PDB; 1LTP; Model; L=62-323. DR PDB; 1TLF; X-ray; A/B/C/D=60-360. DR PDB; 2BJC; NMR; A/B=1-62. DR DIP; DIP:10079N; -. DR IntAct; P03023; -. DR ECO2DBASE; H039.0; 6TH EDITION. DR GenomeReviews; U00096_GR; b0345. DR GenomeReviews; AP009048_GR; JW0336. DR KEGG; ecj:JW0336; -. DR KEGG; eco:b0345; -. DR EchoBASE; EB0520; -. DR EcoGene; EG10525; lacI. DR BioCyc; EcoCyc:PD00763; -. DR LinkHub; P03023; -. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR000843; HTH_LacI. DR InterPro; IPR010982; Lambda_DNA_bd. DR InterPro; IPR001761; Peripla_BP_Lac1. DR Pfam; PF00356; LacI; 1. DR Pfam; PF00532; Peripla_BP_1; 1. DR PRINTS; PR00036; HTHLACI. DR SMART; SM00354; HTH_LACI; 1. DR PROSITE; PS00356; HTH_LACI_1; 1. DR PROSITE; PS50932; HTH_LACI_2; 1. KW 3D-structure; Complete proteome; Direct protein sequencing; KW DNA-binding; Repressor; Transcription; Transcription regulation. FT CHAIN 1 360 Lactose operon repressor. FT /FTId=PRO_0000107963. FT DOMAIN 1 58 HTH lacI-type. FT DNA_BIND 6 25 H-T-H motif. FT VARIANT 282 282 Y -> D (in T41 mutant). FT MUTAGEN 17 17 Y->H: Broadening of specificity. FT MUTAGEN 22 22 R->N: Recognizes an operator variant. FT CONFLICT 286 286 L -> S (in Ref. 1, 4 and 7). FT STRAND 63 69 FT HELIX 74 89 FT STRAND 93 98 FT STRAND 101 103 FT HELIX 104 115 FT TURN 116 118 FT STRAND 122 126 FT HELIX 130 139 FT TURN 140 142 FT STRAND 145 150 FT STRAND 154 156 FT STRAND 158 161 FT HELIX 163 177 FT STRAND 181 186 FT HELIX 192 207 FT STRAND 213 217 FT HELIX 222 234 FT STRAND 240 246 FT HELIX 247 259 FT TURN 265 267 FT STRAND 268 271 FT HELIX 277 281 FT STRAND 282 284 FT STRAND 287 290 FT HELIX 293 308 FT STRAND 314 319 FT STRAND 322 324 FT HELIX 354 356 SQ SEQUENCE 360 AA; 38590 MW; 347A8DEE92D736CB CRC64; MKPVTLYDVA EYAGVSYQTV SRVVNQASHV SAKTREKVEA AMAELNYIPN RVAQQLAGKQ SLLIGVATSS LALHAPSQIV AAIKSRADQL GASVVVSMVE RSGVEACKAA VHNLLAQRVS GLIINYPLDD QDAIAVEAAC TNVPALFLDV SDQTPINSII FSHEDGTRLG VEHLVALGHQ QIALLAGPLS SVSARLRLAG WHKYLTRNQI QPIAEREGDW SAMSGFQQTM QMLNEGIVPT AMLVANDQMA LGAMRAITES GLRVGADISV VGYDDTEDSS CYIPPLTTIK QDFRLLGQTS VDRLLQLSQG QAVKGNQLLP VSLVKRKTTL APNTQTASPR ALADSLMQLA RQVSRLESGQ // ID LACY_ECOLI Reviewed; 417 AA. AC P02920; Q2MC81; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 20-MAR-2007, entry version 78. DE Lactose permease (Lactose-proton symport). GN Name=lacY; OrderedLocusNames=b0343, JW0334; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=80120651; PubMed=6444453; DOI=10.1038/283541a0; RA Buechel D.E., Gronenborn B., Mueller-Hill B.; RT "Sequence of the lactose permease gene."; RL Nature 283:541-545(1980). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RA Pastore J.C., Larigan J.D., Consler T.G., Kaback H.R.; RL Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP TOPOLOGY. RX PubMed=16453726; RA von Heijne G.; RT "The distribution of positively charged residues in bacterial inner RT membrane proteins correlates with the trans-membrane topology."; RL EMBO J. 5:3021-3027(1986). RN [7] RP TOPOLOGY. RX MEDLINE=90311318; PubMed=2164211; RA Calamia J., Manoil C.; RT "lac permease of Escherichia coli: topology and sequence elements RT promoting membrane insertion."; RL Proc. Natl. Acad. Sci. U.S.A. 87:4937-4941(1990). RN [8] RP TOPOLOGY. RX MEDLINE=96066665; PubMed=7578103; DOI=10.1021/bi00045a036; RA Ujwal M.L., Jung H., Bibi E., Manoil C., Altenbach C., Hubbell W.L., RA Kaback H.R.; RT "Membrane topology of helices VII and XI in the lactose permease of RT Escherichia coli studied by lacY-phoA fusion analysis and site- RT directed spectroscopy."; RL Biochemistry 34:14909-14917(1995). RN [9] RP MUTAGENESIS. RX MEDLINE=91167519; PubMed=1848449; DOI=10.1016/0005-2736(91)90390-T; RA King S.C., Hansen C.L., Wilson T.H.; RT "The interaction between aspartic acid 237 and lysine 358 in the RT lactose carrier of Escherichia coli."; RL Biochim. Biophys. Acta 1062:177-186(1991). RN [10] RP MUTAGENESIS. RX MEDLINE=92355521; PubMed=1644770; RA Huang A.-M., Lee J.-I., King S.C., Wilson T.H.; RT "Amino acid substitution in the lactose carrier protein with the use RT of amber suppressors."; RL J. Bacteriol. 174:5436-5441(1992). RN [11] RP REVIEW. RX MEDLINE=90366577; PubMed=2203471; DOI=10.1016/0005-2728(90)90239-Z; RA Kaback H.R.; RT "The lac permease of Escherichia coli: a prototypic energy-transducing RT membrane protein."; RL Biochim. Biophys. Acta 1018:160-162(1990). RN [12] RP MASS SPECTROMETRY OF FORMYLATED FORM. RX MEDLINE=99415921; PubMed=10485888; DOI=10.1073/pnas.96.19.10695; RA Whitelegge J.P., le Coutre J., Lee J.C., Engel C.K., Prive G.G., RA Faull K.F., Kaback H.R.; RT "Toward the bilayer proteome, electrospray ionization-mass RT spectrometry of large, intact transmembrane proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 96:10695-10698(1999). RN [13] RP TOPOLOGY. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=15919996; DOI=10.1126/science.1109730; RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.; RT "Global topology analysis of the Escherichia coli inner membrane RT proteome."; RL Science 308:1321-1323(2005). RN [14] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF MUTANT GLY-154. RX MEDLINE=22776143; PubMed=12893935; DOI=10.1126/science.1088196; RA Abramson J., Smirnova I., Kasho V., Verner G., Kaback H.R., Iwata S.; RT "Structure and mechanism of the lactose permease of Escherichia RT coli."; RL Science 301:610-615(2003). CC -!- FUNCTION: Responsible for transport of beta-galactosides into the CC cell, with the concomitant import of a proton (symport system). CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; multi-pass membrane CC protein. CC -!- MASS SPECTROMETRY: MW=47357; METHOD=Electrospray; RANGE=1-417; CC NOTE=Ref.12. CC -!- SIMILARITY: Belongs to the lacY/rafB permease family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J01636; AAA24054.1; -; Genomic_DNA. DR EMBL; V00295; CAA23571.1; -; Genomic_DNA. DR EMBL; X56095; CAA39575.1; -; Genomic_DNA. DR EMBL; U73857; AAB18067.1; -; Genomic_DNA. DR EMBL; U00096; AAC73446.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76125.1; -; Genomic_DNA. DR PIR; A03418; GREC. DR PDB; 1M2U; Model; A=1-417. DR PDB; 1PV6; X-ray; A/B=1-417. DR PDB; 1PV7; X-ray; A/B=1-417. DR PDB; 2CFP; X-ray; A=1-417. DR PDB; 2CFQ; X-ray; A=1-417. DR DIP; DIP:10080N; -. DR GenomeReviews; U00096_GR; b0343. DR GenomeReviews; AP009048_GR; JW0334. DR KEGG; ecj:JW0334; -. DR KEGG; eco:b0343; -. DR EchoBASE; EB0521; -. DR EcoGene; EG10526; lacY. DR BioCyc; EcoCyc:LACY-MONOMER; -. DR LinkHub; P02920; -. DR InterPro; IPR000576; LacY_symport. DR InterPro; IPR007114; MFS. DR Pfam; PF01306; LacY_symp; 1. DR PRINTS; PR00174; LACYSMPORT. DR TIGRFAMs; TIGR00882; 2A0105; 1. DR PROSITE; PS00896; LACY_1; 1. DR PROSITE; PS00897; LACY_2; 1. DR PROSITE; PS50850; MFS; 1. KW 3D-structure; Complete proteome; Formylation; Inner membrane; KW Membrane; Sugar transport; Symport; Transmembrane; Transport. FT CHAIN 1 417 Lactose permease. FT /FTId=PRO_0000196184. FT TOPO_DOM 1 7 Cytoplasmic. FT TRANSMEM 8 34 1. FT TOPO_DOM 35 41 Periplasmic. FT TRANSMEM 42 70 2. FT TOPO_DOM 71 74 Cytoplasmic. FT TRANSMEM 75 100 3. FT TOPO_DOM 101 104 Periplasmic. FT TRANSMEM 105 129 4. FT TOPO_DOM 130 140 Cytoplasmic. FT TRANSMEM 141 163 5. FT TOPO_DOM 164 166 Periplasmic. FT TRANSMEM 167 186 6. FT TOPO_DOM 187 220 Cytoplasmic. FT TRANSMEM 221 249 7. FT TOPO_DOM 250 253 Periplasmic. FT TRANSMEM 254 278 8. FT TOPO_DOM 279 288 Cytoplasmic. FT TRANSMEM 289 308 9. FT TOPO_DOM 309 311 Periplasmic. FT TRANSMEM 312 334 10. FT TOPO_DOM 335 346 Cytoplasmic. FT TRANSMEM 347 374 11. FT TOPO_DOM 375 377 Periplasmic. FT TRANSMEM 378 398 12. FT TOPO_DOM 399 417 Cytoplasmic. FT SITE 126 126 Substrate binding. FT SITE 144 144 Substrate binding. FT SITE 269 269 Substrate binding and proton FT translocation. FT SITE 302 302 Proton translocation. FT SITE 322 322 Proton translocation. FT SITE 325 325 Proton translocation. FT MOD_RES 1 1 N-formylmethionine; partial. FT MUTAGEN 237 237 D->N,G: Defect in melibiose transport. FT MUTAGEN 358 358 K->T: Defect in melibiose transport. FT TURN 2 4 FT HELIX 8 12 FT TURN 13 16 FT HELIX 17 23 FT TURN 24 28 FT HELIX 31 38 FT HELIX 42 54 FT TURN 55 57 FT HELIX 60 67 FT HELIX 68 70 FT HELIX 76 79 FT TURN 80 83 FT STRAND 84 87 FT HELIX 88 93 FT HELIX 96 99 FT TURN 100 102 FT HELIX 105 109 FT TURN 114 120 FT HELIX 121 135 FT HELIX 140 142 FT HELIX 144 164 FT HELIX 168 171 FT HELIX 173 177 FT HELIX 178 183 FT STRAND 201 203 FT HELIX 210 216 FT HELIX 220 231 FT TURN 232 235 FT HELIX 236 242 FT HELIX 245 249 FT STRAND 251 254 FT HELIX 257 267 FT HELIX 270 276 FT HELIX 279 286 FT HELIX 289 307 FT HELIX 312 320 FT HELIX 322 324 FT HELIX 326 340 FT TURN 343 345 FT HELIX 346 349 FT HELIX 351 356 FT HELIX 357 399 FT STRAND 408 411 FT TURN 414 416 SQ SEQUENCE 417 AA; 46503 MW; 24A8062F628CDA32 CRC64; MYYLKNTNFW MFGLFFFFYF FIMGAYFPFF PIWLHDINHI SKSDTGIIFA AISLFSLLFQ PLFGLLSDKL GLRKYLLWII TGMLVMFAPF FIFIFGPLLQ YNILVGSIVG GIYLGFCFNA GAPAVEAFIE KVSRRSNFEF GRARMFGCVG WALCASIVGI MFTINNQFVF WLGSGCALIL AVLLFFAKTD APSSATVANA VGANHSAFSL KLALELFRQP KLWFLSLYVI GVSCTYDVFD QQFANFFTSF FATGEQGTRV FGYVTTMGEL LNASIMFFAP LIINRIGGKN ALLLAGTIMS VRIIGSSFAT SALEVVILKT LHMFEVPFLL VGCFKYITSQ FEVRFSATIY LVCFCFFKQL AMIFMSVLAG NMYESIGFQG AYLVLGLVAL GFTLISVFTL SGPGPLSLLR RQVNEVA // ID BGAL_ECOLI Reviewed; 1024 AA. AC P00722; Q2MC80; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 20-MAR-2007, entry version 83. DE Beta-galactosidase (EC 3.2.1.23) (Lactase). GN Name=lacZ; OrderedLocusNames=b0344, JW0335; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=84028567; PubMed=6313347; RA Kalnins A., Otto K., Ruether U., Mueller-Hill B.; RT "Sequence of the lacZ gene of Escherichia coli."; RL EMBO J. 2:593-597(1983). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP PROTEIN SEQUENCE OF 2-1024. RX MEDLINE=78218239; PubMed=97298; RA Fowler A.V., Zabin I.; RT "Amino acid sequence of beta-galactosidase. XI. Peptide ordering RT procedures and the complete sequence."; RL J. Biol. Chem. 253:5521-5525(1978). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 356-476. RX MEDLINE=80188189; PubMed=6246435; DOI=10.1038/285038a0; RA Calos M.P., Miller J.H.; RT "Molecular consequences of deletion formation mediated by the RT transposon Tn9."; RL Nature 285:38-41(1980). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1008-1024. RX MEDLINE=80120651; PubMed=6444453; DOI=10.1038/283541a0; RA Buechel D.E., Gronenborn B., Mueller-Hill B.; RT "Sequence of the lactose permease gene."; RL Nature 283:541-545(1980). RN [8] RP ACTIVE SITE REGIONS. RX MEDLINE=83290932; PubMed=6411710; RA Fowler A.V., Smith P.J.; RT "The active site regions of lacZ and ebg beta-galactosidases are RT homologous."; RL J. Biol. Chem. 258:10204-10207(1983). RN [9] RP ACTIVE SITE GLU-462. RX MEDLINE=84108409; PubMed=6420154; RA Herrchen M., Legler G.; RT "Identification of an essential carboxylate group at the active site RT of lacZ beta-galactosidase from Escherichia coli."; RL Eur. J. Biochem. 138:527-531(1984). RN [10] RP ACTIVE SITE GLU-538. RX MEDLINE=92283812; PubMed=1350782; RA Gebler J.C., Aebersold R., Withers S.G.; RT "Glu-537, not Glu-461, is the nucleophile in the active site of (lac RT Z) beta-galactosidase from Escherichia coli."; RL J. Biol. Chem. 267:11126-11130(1992). RN [11] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS). RX MEDLINE=94277211; PubMed=8008071; DOI=10.1038/369761a0; RA Jacobson R.H., Zhang X.-J., Dubose R.F., Matthews B.W.; RT "Three-dimensional structure of beta-galactosidase from E. coli."; RL Nature 369:761-766(1994). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX MEDLINE=21590184; PubMed=11732897; DOI=10.1021/bi011727i; RA Juers D.H., Heightman T.D., Vasella A., McCarter J.D., Mackenzie L., RA Withers S.G., Matthews B.W.; RT "A structural view of the action of Escherichia coli (lacZ) beta- RT galactosidase."; RL Biochemistry 40:14781-14794(2001). CC -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D- CC galactose residues in beta-D-galactosides. CC -!- SUBUNIT: Homotetramer. CC -!- INTERACTION: CC P03023:lacI; NbExp=1; IntAct=EBI-369998, EBI-909231; CC P0ACA1:yibF; NbExp=1; IntAct=EBI-369998, EBI-1133142; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. CC -!- WEB RESOURCE: NAME=Worthington enzyme manual; CC URL="http://www.worthington-biochem.com/BG/". CC -!- WEB RESOURCE: NAME=ProZyme technical fact sheet; CC URL="http://www.prozyme.com/pdf/bg11.pdf". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J01636; AAA24053.1; -; Genomic_DNA. DR EMBL; V00296; CAA23573.1; -; Genomic_DNA. DR EMBL; U73857; AAB18068.1; -; Genomic_DNA. DR EMBL; U00096; AAC73447.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76126.1; -; Genomic_DNA. DR EMBL; V00295; CAA23570.1; -; Genomic_DNA. DR PIR; A90981; GBEC. DR PDB; 1BGL; X-ray; A/B/C/D/E/F/G/H=1-1024. DR PDB; 1BGM; X-ray; I/J/K/L/M/N/O/P=-. DR PDB; 1DP0; X-ray; A/B/C/D=10-1024. DR PDB; 1F49; X-ray; A/B/C/D/E/F/G/H=1-1024. DR PDB; 1F4A; X-ray; A/B/C/D=4-1024. DR PDB; 1F4H; X-ray; A/B/C/D=4-1024. DR PDB; 1GHO; X-ray; I/J/K/L/M/N/O/P=1-1024. DR PDB; 1HN1; X-ray; A/B/C/D=10-1024. DR PDB; 1JYN; X-ray; A/B/C/D=10-1024. DR PDB; 1JYV; X-ray; A/B/C/D=10-1024. DR PDB; 1JYW; X-ray; A/B/C/D=10-1024. DR PDB; 1JYX; X-ray; A/B/C/D=10-1024. DR PDB; 1JYY; X-ray; A/B/C/D/E/F/G/H=1-1024. DR PDB; 1JYZ; X-ray; I/J/K/L/M/N/O/P=1-1024. DR PDB; 1JZ0; X-ray; A/B/C/D/E/F/G/H=1-1024. DR PDB; 1JZ1; X-ray; I/J/K/L/M/N/O/P=1-1024. DR PDB; 1JZ2; X-ray; A/B/C/D=1-1024. DR PDB; 1JZ3; X-ray; A/B/C/D=10-1024. DR PDB; 1JZ4; X-ray; A/B/C/D=10-1024. DR PDB; 1JZ5; X-ray; A/B/C/D=10-1024. DR PDB; 1JZ6; X-ray; A/B/C/D=10-1024. DR PDB; 1JZ7; X-ray; A/B/C/D=10-1024. DR PDB; 1JZ8; X-ray; A/B/C/D=10-1024. DR PDB; 1PX3; X-ray; A/B/C/D=10-1024. DR PDB; 1PX4; X-ray; A/B/C/D=10-1024. DR IntAct; P00722; -. DR ECO2DBASE; E123.0; 6TH EDITION. DR GenomeReviews; U00096_GR; b0344. DR GenomeReviews; AP009048_GR; JW0335. DR KEGG; ecj:JW0335; -. DR KEGG; eco:b0344; -. DR EchoBASE; EB0522; -. DR EcoGene; EG10527; lacZ. DR BioCyc; EcoCyc:BETAGALACTOSID-MONOMER; -. DR LinkHub; P00722; -. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR InterPro; IPR008979; Gal_bd. DR InterPro; IPR011013; Gal_mut_like. DR InterPro; IPR006101; Glyco_hydro_2. DR InterPro; IPR013812; Glyco_hydro_2/20_Ig-like. DR InterPro; IPR006104; Glyco_hydro_2_carb-bd. DR InterPro; IPR006102; Glyco_hydro_2_Ig-like. DR InterPro; IPR006103; Glyco_hydro_2_TIM. DR InterPro; IPR004199; Glyco_hydro_42_D5. DR InterPro; IPR013781; Glyco_hydro_cat. DR Gene3D; G3DSA:2.70.98.10; Glyco_hydro_42_5; 1. DR Pfam; PF02929; Bgal_small_N; 1. DR Pfam; PF00703; Glyco_hydro_2; 1. DR Pfam; PF02836; Glyco_hydro_2_C; 1. DR Pfam; PF02837; Glyco_hydro_2_N; 1. DR PRINTS; PR00132; GLHYDRLASE2. DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1. DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1. KW 3D-structure; Complete proteome; Direct protein sequencing; KW Glycosidase; Hydrolase. FT INIT_MET 1 1 Removed. FT CHAIN 2 1024 Beta-galactosidase. FT /FTId=PRO_0000057650. FT ACT_SITE 462 462 Proton donor. FT ACT_SITE 538 538 Nucleophile. FT HELIX 15 17 FT STRAND 22 25 FT STRAND 36 38 FT HELIX 39 44 FT STRAND 51 53 FT STRAND 56 65 FT HELIX 66 68 FT HELIX 72 75 FT STRAND 82 87 FT HELIX 90 93 FT STRAND 99 104 FT STRAND 120 129 FT HELIX 131 135 FT STRAND 136 144 FT STRAND 146 154 FT STRAND 157 163 FT STRAND 169 172 FT TURN 174 176 FT STRAND 179 191 FT HELIX 193 197 FT STRAND 201 204 FT STRAND 212 217 FT STRAND 219 231 FT STRAND 235 248 FT STRAND 254 262 FT STRAND 265 274 FT STRAND 288 297 FT STRAND 303 306 FT STRAND 309 317 FT STRAND 322 330 FT STRAND 335 338 FT STRAND 341 344 FT STRAND 351 355 FT TURN 361 363 FT HELIX 369 381 FT STRAND 386 388 FT HELIX 397 405 FT STRAND 408 412 FT STRAND 420 422 FT TURN 423 428 FT HELIX 430 432 FT HELIX 433 447 FT STRAND 453 457 FT HELIX 466 478 FT TURN 488 490 FT STRAND 491 493 FT STRAND 497 499 FT STRAND 513 515 FT HELIX 520 524 FT STRAND 533 539 FT HELIX 549 558 FT STRAND 562 568 FT STRAND 575 578 FT STRAND 584 587 FT TURN 589 592 FT HELIX 599 602 FT HELIX 616 623 FT STRAND 626 632 FT STRAND 635 640 FT STRAND 651 658 FT STRAND 661 669 FT STRAND 677 681 FT STRAND 689 702 FT STRAND 707 709 FT STRAND 713 725 FT STRAND 739 742 FT STRAND 744 751 FT STRAND 754 759 FT TURN 760 762 FT STRAND 764 770 FT STRAND 776 783 FT HELIX 790 793 FT HELIX 806 813 FT TURN 814 817 FT STRAND 819 829 FT STRAND 831 844 FT STRAND 847 859 FT STRAND 864 872 FT STRAND 880 889 FT STRAND 893 903 FT STRAND 914 921 FT HELIX 922 925 FT STRAND 938 946 FT STRAND 949 962 FT HELIX 964 969 FT HELIX 973 975 FT STRAND 980 990 FT STRAND 998 1000 FT HELIX 1005 1007 FT STRAND 1012 1021 SQ SEQUENCE 1024 AA; 116483 MW; 9D295EF4CEF90B08 CRC64; MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ QLRSLNGEWR FAWFPAPEAV PESWLECDLP EADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPTENP TGCYSLTFNV DESWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLPS EFDLSAFLRA GENRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPT TQISDFHVAT RFNDDFSRAV LEAEVQMCGE LRDYLRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPK LWSAEIPNLY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL LIRGVNRHEH HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY TLCDRYGLYV VDEANIETHG MVPMNRLTDD PRWLPAMSER VTRMVQRDRN HPSVIIWSLG NESGHGANHD ALYRWIKSVD PSRPVQYEGG GADTTATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE TRPLILCEYA HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGQTIEVT SEYLFRHSDN ELLHWMVALD GKPLASGEVP LDVAPQGKQL IELPELPQPE SAGQLWLTVR VVQPNATAWS EAGHISAWQQ WRLAENLSVT LPAASHAIPH LTTSEMDFCI ELGNKRWQFN RQSGFLSQMW IGDKKQLLTP LRDQFTRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTA HAWQHQGKTL FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLNCQLA QVAERVNWLG LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH QWRGDFQFNI SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW SPSVSAEFQL SAGRYHYQLV WCQK // ID THGA_ECOLI Reviewed; 203 AA. AC P07464; P77862; Q2MC82; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1988, sequence version 1. DT 20-MAR-2007, entry version 71. DE Galactoside O-acetyltransferase (EC 2.3.1.18) (GAT) (Thiogalactoside DE acetyltransferase). GN Name=lacA; OrderedLocusNames=b0342, JW0333; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=85200082; PubMed=3922433; DOI=10.1016/S0300-9084(85)80235-2; RA Fowler A.V., Hediger M.A., Musso R.E., Zabin I.; RT "The amino acid sequence of thiogalactoside transacetylase of RT Escherichia coli."; RL Biochimie 67:101-108(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=86016712; PubMed=3901000; RA Hediger M.A., Johnson D.F., Nierlich D.P., Zabin I.; RT "DNA sequence of the lactose operon: the lacA gene and the RT transcriptional termination region."; RL Proc. Natl. Acad. Sci. U.S.A. 82:6414-6418(1985). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26. RX MEDLINE=80120651; PubMed=6444453; DOI=10.1038/283541a0; RA Buechel D.E., Gronenborn B., Mueller-Hill B.; RT "Sequence of the lactose permease gene."; RL Nature 283:541-545(1980). RN [7] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS). RX MEDLINE=21936195; PubMed=11937062; DOI=10.1016/S0969-2126(02)00741-4; RA Wang X.G., Olsen L.R., Roderick S.L.; RT "Structure of the lac operon galactoside acetyltransferase."; RL Structure 10:581-588(2002). CC -!- FUNCTION: May assist cellular detoxification by acetylating non- CC metabolizable pyranosides, thereby preventing their reentry into CC the cell. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + a beta-D-galactoside = CoA + a 6- CC acetyl-beta-D-galactoside. CC -!- PATHWAY: Lactose biosynthesis. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- PTM: The N-terminus of this protein is heterogeneous because the CC initiator methionine is only partially cleaved. CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J01636; AAA24055.1; -; Genomic_DNA. DR EMBL; X51872; CAA36162.1; -; Genomic_DNA. DR EMBL; U73857; AAB18066.1; -; Genomic_DNA. DR EMBL; U00096; AAC73445.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76124.1; -; Genomic_DNA. DR EMBL; V00295; CAA23572.1; -; Genomic_DNA. DR PIR; A94061; XXECTG. DR PDB; 1KQA; X-ray; A/B/C=1-203. DR PDB; 1KRR; X-ray; A/B/C=1-203. DR PDB; 1KRU; X-ray; A/B/C=1-203. DR PDB; 1KRV; X-ray; A/B/C=1-203. DR DIP; DIP:10078N; -. DR IntAct; P07464; -. DR GenomeReviews; U00096_GR; b0342. DR GenomeReviews; AP009048_GR; JW0333. DR KEGG; ecj:JW0333; -. DR KEGG; eco:b0342; -. DR EchoBASE; EB0519; -. DR EcoGene; EG10524; lacA. DR BioCyc; EcoCyc:GALACTOACETYLTRAN-MONOMER; -. DR GO; GO:0008870; F:galactoside O-acetyltransferase activity; IEA:EC. DR InterPro; IPR001451; Hexapep_transf. DR InterPro; IPR011004; Trimer_LpxA_like. DR Pfam; PF00132; Hexapep; 3. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. KW 3D-structure; Acyltransferase; Complete proteome; KW Direct protein sequencing; Lactose biosynthesis; Repeat; Transferase. FT CHAIN 1 203 Galactoside O-acetyltransferase. FT /FTId=PRO_0000068696. FT HELIX 5 11 FT HELIX 22 37 FT HELIX 44 54 FT STRAND 55 57 FT STRAND 68 71 FT STRAND 76 78 FT STRAND 88 91 FT STRAND 96 98 FT STRAND 109 114 FT TURN 119 121 FT STRAND 127 129 FT STRAND 132 134 FT STRAND 172 175 FT TURN 176 179 FT STRAND 180 184 FT HELIX 187 189 SQ SEQUENCE 203 AA; 22799 MW; 31C7FEA0B0150D70 CRC64; MNMPMTERIR AGKLFTDMCE GLPEKRLRGK TLMYEFNHSH PSEVEKRESL IKEMFATVGE NAWVEPPVYF SYGSNIHIGR NFYANFNLTI VDDYTVTIGD NVLIAPNVTL SVTGHPVHHE LRKNGEMYSF PITIGNNVWI GSHVVINPGV TIGDNSVIGA GSIVTKDIPP NVVAAGVPCR VIREINDRDK HYYFKDYKVE SSV // ID 12S1_ARATH Reviewed; 472 AA. AC P15455; Q9FFH7; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2002, sequence version 2. DT 31-OCT-2006, entry version 58. DE 12S seed storage protein CRA1 precursor [Contains: 12S seed storage DE protein CRA1 alpha chain (12S seed storage protein CRA1 acidic chain); DE 12S seed storage protein CRA1 beta chain (12S seed storage protein DE CRA1 basic chain)]. GN Name=CRA1; OrderedLocusNames=At5g44120; ORFNames=MLN1.4; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Landsberg erecta; RA Pang P.P., Pruitt R.E., Meyerowitz E.M.; RT "Molecular cloning, genome organization, expression and evolution of RT 12S seed storage protein genes of Arabidopsis thaliana."; RL Plant Mol. Biol. 11:805-820(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=97471969; PubMed=9330910; DOI=10.1093/dnares/4.3.215; RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., RA Miyajima N., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence RT features of the 1.6 Mb regions covered by twenty physically assigned RT P1 clones."; RL DNA Res. 4:215-230(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 420-472. RC STRAIN=cv. Columbia; TISSUE=Green siliques; RX MEDLINE=94108489; PubMed=8281187; RX DOI=10.1046/j.1365-313X.1993.04061051.x; RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., RA Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., RA Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y., RA de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., RA Bardet C., Tremousaygue D., Lescure B.; RT "An inventory of 1152 expressed sequence tags obtained by partial RT sequencing of cDNAs from Arabidopsis thaliana."; RL Plant J. 4:1051-1061(1993). CC -!- FUNCTION: This is a seed storage protein. CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a CC basic chain derived from a single precursor and linked by a CC disulfide bond. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced. According to EST CC sequences; CC Name=1; CC IsoId=P15455-1; Sequence=Displayed; CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M37247; AAA32777.1; -; Genomic_DNA. DR EMBL; X14312; CAA32493.1; -; Genomic_DNA. DR EMBL; AB005239; BAB10979.1; -; Genomic_DNA. DR EMBL; AY070730; AAL50071.1; -; mRNA. DR EMBL; Z17590; CAA79005.1; -; mRNA. DR PIR; S08509; S08509. DR UniGene; At.20540; -. DR HSSP; P04776; 1FXZ. DR GenomeReviews; BA000015_GR; AT5G44120. DR KEGG; ath:At5g44120; -. DR TAIR; At5g44120; -. DR ArrayExpress; P15455; -. DR InterPro; IPR006045; Cupin_1. DR InterPro; IPR011051; Cupin_RmlC_type. DR InterPro; IPR006044; Seedstore11s_pln. DR Pfam; PF00190; Cupin_1; 2. DR PRINTS; PR00439; 11SGLOBULIN. DR PROSITE; PS00305; 11S_SEED_STORAGE; 1. KW Alternative splicing; Seed storage protein; Signal; Storage protein. FT SIGNAL 1 24 Potential. FT CHAIN 25 282 12S seed storage protein CRA1 alpha chain FT (By similarity). FT /FTId=PRO_0000031999. FT CHAIN 283 472 12S seed storage protein CRA1 beta chain FT (By similarity). FT /FTId=PRO_0000032000. FT DISULFID 112 289 Interchain (between alpha and beta FT chains) (Potential). FT CONFLICT 167 167 E -> Q (in Ref. 1). FT CONFLICT 356 356 V -> E (in Ref. 1). SQ SEQUENCE 472 AA; 52595 MW; 700B468E4D251994 CRC64; MARVSSLLSF CLTLLILFHG YAAQQGQQGQ QFPNECQLDQ LNALEPSHVL KSEAGRIEVW DHHAPQLRCS GVSFARYIIE SKGLYLPSFF NTAKLSFVAK GRGLMGKVIP GCAETFQDSS EFQPRFEGQG QSQRFRDMHQ KVEHIRSGDT IATTPGVAQW FYNDGQEPLV IVSVFDLASH QNQLDRNPRP FYLAGNNPQG QVWLQGREQQ PQKNIFNGFG PEVIAQALKI DLQTAQQLQN QDDNRGNIVR VQGPFGVIRP PLRGQRPQEE EEEEGRHGRH GNGLEETICS ARCTDNLDDP SRADVYKPQL GYISTLNSYD LPILRFIRLS ALRGSIRQNA MVLPQWNANA NAILYVTDGE AQIQIVNDNG NRVFDGQVSQ GQLIAVPQGF SVVKRATSNR FQWVEFKTNA NAQINTLAGR TSVLRGLPLE VITNGFQISP EEARRVKFNT LETTLTHSSG PASYGRPRVA AA // ID OPSD_HUMAN Reviewed; 348 AA. AC P08100; Q16414; Q2M249; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 20-MAR-2007, entry version 91. DE Rhodopsin (Opsin-2). GN Name=RHO; Synonyms=OPN2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=84272729; PubMed=6589631; RA Nathans J., Hogness D.S.; RT "Isolation and nucleotide sequence of the gene encoding human RT rhodopsin."; RL Proc. Natl. Acad. Sci. U.S.A. 81:4851-4855(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.; RT "Genome-wide discovery and analysis of human seven transmembrane helix RT receptor genes."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Retina; RG The German cDNA consortium; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-120. RX PubMed=8566799; DOI=10.1016/0378-1119(95)00688-5; RA Bennett J., Beller B., Sun D., Kariko K.; RT "Sequence analysis of the 5.34-kb 5' flanking region of the human RT rhodopsin-encoding gene."; RL Gene 167:317-320(1995). RN [6] RP REVIEW ON RP4 VARIANTS. RX MEDLINE=94004905; PubMed=8401533; RA Al-Maghtheh M., Gregory C., Inglehearn C., Hardcastle A., RA Bhattacharya S.; RT "Rhodopsin mutations in autosomal dominant retinitis pigmentosa."; RL Hum. Mutat. 2:249-255(1993). RN [7] RP VARIANT RP4 HIS-23. RX MEDLINE=90136922; PubMed=2137202; DOI=10.1038/343364a0; RA Dryja T.P., McGee T.L., Reichei E., Hahn L.B., Cowley G.S., RA Yandell D.W., Sandberg M.A., Berson E.L.; RT "A point mutation of the rhodopsin gene in one form of retinitis RT pigmentosa."; RL Nature 343:364-366(1990). RN [8] RP VARIANTS RP4. RX MEDLINE=91051574; PubMed=2239971; RA Farrar G.J., Kenna P., Redmond R., McWilliam P., Bradley D.G., RA Humphries M.M., Sharp E.M., Inglehearn C.F., Bashir R., Jay M., RA Watty A., Ludwig M., Schinzel A., Samanns C., Gal A., RA Bhattacharya S.S., Humphries P.; RT "Autosomal dominant retinitis pigmentosa: absence of the rhodopsin RT proline-->histidine substitution (codon 23) in pedigrees from RT Europe."; RL Am. J. Hum. Genet. 47:941-945(1990). RN [9] RP VARIANTS RP4 HIS-23; ARG-58; LEU-347 AND SER-347. RX MEDLINE=91015273; PubMed=2215617; RA Dryja T.P., McGee T.L., Hahn L.B., Cowley G.S., Olsson J.E., RA Reichel E., Sandberg M.A., Berson E.L.; RT "Mutations within the rhodopsin gene in patients with autosomal RT dominant retinitis pigmentosa."; RL N. Engl. J. Med. 323:1302-1307(1990). RN [10] RP VARIANT RP4 ILE-255 DEL. RX MEDLINE=91090106; PubMed=1985460; RA Inglehearn C.F., Bashir R., Lester D.H., Jay M., Bird A.C., RA Bhattacharya S.S.; RT "A 3-bp deletion in the rhodopsin gene in a family with autosomal RT dominant retinitis pigmentosa."; RL Am. J. Hum. Genet. 48:26-30(1991). RN [11] RP VARIANT RP4 ARG-347. RX MEDLINE=92120672; PubMed=1840561; RA Gal A., Artlich A., Ludwig M., Niemeyer G., Olek K., Schwinger E., RA Schinzel A.; RT "Pro-347-Arg mutation of the rhodopsin gene in autosomal dominant RT retinitis pigmentosa."; RL Genomics 11:468-470(1991). RN [12] RP VARIANTS RP4. RX MEDLINE=91319709; PubMed=1862076; RA Sung C.H., Davenport C.M., Hennessey J.C., Maumenee I.H., RA Jacobson S.G., Heckenlively J.R., Nowakowski R., Fishman G., RA Gouras P., Nathans J.; RT "Rhodopsin mutations in autosomal dominant retinitis pigmentosa."; RL Proc. Natl. Acad. Sci. U.S.A. 88:6481-6485(1991). RN [13] RP VARIANTS RP4. RX MEDLINE=92021049; PubMed=1833777; RA Dryja T.P., Hahn L.B., Cowley G.S., McGee T.L., Berson E.L.; RT "Mutation spectrum of the rhodopsin gene among patients with autosomal RT dominant retinitis pigmentosa."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9370-9374(1991). RN [14] RP VARIANTS RP4 MET-17; HIS-23; ARG-58; SER-182 AND LEU-267. RX MEDLINE=91377732; PubMed=1897520; RA Sheffield V.C., Fishman G.A., Beck J.S., Kimura A.E., Stone E.M.; RT "Identification of novel rhodopsin mutations associated with retinitis RT pigmentosa by GC-clamped denaturing gradient gel electrophoresis."; RL Am. J. Hum. Genet. 49:699-706(1991). RN [15] RP VARIANT RP4 ARG-207. RX MEDLINE=93258325; PubMed=1302614; DOI=10.1093/hmg/1.9.769; RA Farrar G.J., Findlay J.B.C., Kumar-Singh R., Kenna P., Humphries M.M., RA Sharpe E., Humphries P.; RT "Autosomal dominant retinitis pigmentosa: a novel mutation in the RT rhodopsin gene in the original 3q linked family."; RL Hum. Mol. Genet. 1:769-771(1992). RN [16] RP VARIANTS RP4 MET-17 AND LEU-347. RX MEDLINE=93004784; PubMed=1391967; RA Fujiki K., Hotta Y., Hayakawa M., Sakuma H., Shiono T., Noro M., RA Sakuma T., Tamai M., Hikiji K., Kawaguchi R., Hoshi A., Nakajima A., RA Kanai A.; RT "Point mutations of rhodopsin gene found in Japanese families with RT autosomal dominant retinitis pigmentosa (ADRP)."; RL Jpn. J. Hum. Genet. 37:125-132(1992). RN [17] RP VARIANTS RP4 ARG-106; GLY-135; SER-140; GLU-188 AND ARG-211, AND RP VARIANTS ALA-51; ILE-104 AND MET-209. RX MEDLINE=93304432; PubMed=8317502; RA Macke J.P., Davenport C.M., Jacobson S.G., Hennessey J.C., RA Gonzalez-Fernandez F., Conway B.P., Heckenlively J., Palmer R., RA Maumenee I.H., Sieving P., Gouras P., Good W., Nathans J.; RT "Identification of novel rhodopsin mutations responsible for retinitis RT pigmentosa: implications for the structure and function of RT rhodopsin."; RL Am. J. Hum. Genet. 53:80-89(1993). RN [18] RP VARIANT RP4 SER-15. RX MEDLINE=93357759; PubMed=8353500; DOI=10.1093/hmg/2.6.813; RA Kranich H., Bartkowski S., Denton M.J., Krey S., Dickinson P., RA Duvigneau C., Gal A.; RT "Autosomal dominant 'sector' retinitis pigmentosa due to a point RT mutation predicting an Asn-15-Ser substitution of rhodopsin."; RL Hum. Mol. Genet. 2:813-814(1993). RN [19] RP VARIANT CSNBAD1 GLU-292. RX MEDLINE=93364423; PubMed=8358437; DOI=10.1038/ng0793-280; RA Dryja T.P., Berson E.L., Rao V.R., Oprian D.D.; RT "Heterozygous missense mutation in the rhodopsin gene as a cause of RT congenital stationary night blindness."; RL Nat. Genet. 4:280-283(1993). RN [20] RP VARIANTS RP4. RX MEDLINE=94375083; PubMed=8088850; DOI=10.1006/geno.1994.1301; RA Vaithinathan R., Berson E.L., Dryja T.P.; RT "Further screening of the rhodopsin gene in patients with autosomal RT dominant retinitis pigmentosa."; RL Genomics 21:461-463(1994). RN [21] RP VARIANT RP4 THR-44. RX MEDLINE=94357587; PubMed=8076945; DOI=10.1007/BF00208284; RA Reig C., Antich J., Gean E., Garcia-Sandoval B., Ramos C., Ayuso C., RA Carballo M.; RT "Identification of a novel rhodopsin mutation (Met-44-Thr) in a RT simplex case of retinitis pigmentosa."; RL Hum. Genet. 94:283-286(1994). RN [22] RP VARIANTS RP4 PHE-110; PRO-131 AND VAL-164. RX MEDLINE=95072600; PubMed=7981701; DOI=10.1093/hmg/3.7.1203; RA Fuchs S., Kranich H., Denton M.J., Zrenner E., Bhattacharya S.S., RA Humphries P., Gal A.; RT "Three novel rhodopsin mutations (C110F, L131P, A164V) in patients RT with autosomal dominant retinitis pigmentosa."; RL Hum. Mol. Genet. 3:1203-1203(1994). RN [23] RP VARIANT RP4 GLN-171. RX MEDLINE=95078852; PubMed=7987326; DOI=10.1093/hmg/3.8.1421; RA Antinolo G., Sanchez B., Borrego S., Rueda T., Chaparro P., RA Cabeza J.C.; RT "Identification of a new mutation at codon 171 of rhodopsin gene RT causing autosomal dominant retinitis pigmentosa."; RL Hum. Mol. Genet. 3:1421-1421(1994). RN [24] RP VARIANTS RP4 PHE-127; PRO-131; ASN-178; ARG-267 AND ARG-297. RX MEDLINE=95078858; PubMed=7987331; DOI=10.1093/hmg/3.8.1433; RA Souied E., Gerber S., Rozet J.M., Bonneau D., Dufier J.-L., Ghazi I., RA Philip N., Soubrane G., Coscas G., Munnich A.; RT "Five novel missense mutations of the rhodopsin gene in autosomal RT dominant retinitis pigmentosa."; RL Hum. Mol. Genet. 3:1433-1434(1994). RN [25] RP VARIANTS RP4 ARG-40 AND LYS-216. RX MEDLINE=94362717; PubMed=8081400; RA Al-Maghtheh M., Inglehearn C., Lunt P., Jay M., Bird A., RA Bhattacharya S.; RT "Two new rhodopsin transversion mutations (L40R; M216K) in families RT with autosomal dominant retinitis pigmentosa."; RL Hum. Mutat. 3:409-410(1994). RN [26] RP VARIANT RP4 LEU-345. RX MEDLINE=94321123; PubMed=8045708; RA Rosas D.J., Roman A.J., Weissbrod P., Macke J.P., Nathans J.; RT "Autosomal dominant retinitis pigmentosa in a large family: a clinical RT and molecular genetic study."; RL Invest. Ophthalmol. Vis. Sci. 35:3134-3144(1994). RN [27] RP VARIANT ARRP LYS-150. RX MEDLINE=95078913; PubMed=7987385; DOI=10.1038/ng0994-10; RA Kumaramanickavel G., Maw M., Denton M.J., John S., Srikumari C.R., RA Orth U., Oehlmann R., Gal A.; RT "Missense rhodopsin mutation in a family with recessive RP."; RL Nat. Genet. 8:10-11(1994). RN [28] RP VARIANT RP4 ALA-347. RX MEDLINE=95359993; PubMed=7633434; DOI=10.1093/hmg/4.4.775; RA Macke J.P., Hennessey J.C., Nathans J.; RT "Rhodopsin mutation proline347-to-alanine in a family with autosomal RT dominant retinitis pigmentosa indicates an important role for proline RT at position 347."; RL Hum. Mol. Genet. 4:775-776(1995). RN [29] RP VARIANT CSNBAD1 ASP-90. RX MEDLINE=95148641; PubMed=7846071; RA Sieving P.A., Richards J.E., Naarendorp F., Bingham E.L., Scott K., RA Alpern M.; RT "Dark-light: model for nightblindness from the human rhodopsin Gly- RT 90-->Asp mutation."; RL Proc. Natl. Acad. Sci. U.S.A. 92:880-884(1995). RN [30] RP VARIANT RP4 TRP-135. RX MEDLINE=96142043; PubMed=8554077; RA Souied E., Soubrane G., Benlian P., Coscas G.J., Gerber S., RA Munnich A., Kaplan J.; RT "Retinitis punctata albescens associated with the Arg135Trp mutation RT in the rhodopsin gene."; RL Am. J. Ophthalmol. 121:19-25(1996). RN [31] RP VARIANT RP4 ARG-109. RX MEDLINE=98112414; PubMed=9452035; RA Goliath R., Bardien S., September A., Martin R., Ramesar R., RA Greenberg J.; RT "Rhodopsin mutation G109R in a family with autosomal dominant RT retinitis pigmentosa."; RL Hum. Mutat. Suppl. 1:S40-S41(1998). RN [32] RP VARIANT CSNBAD1 ILE-94. RX MEDLINE=99103467; PubMed=9888392; RX DOI=10.1002/(SICI)1098-1004(1999)13:1<75::AID-HUMU9>3.0.CO;2-4; RA Al-Jandal N., Farrar G.J., Kiang A.-S., Humphries M.M., Bannon N., RA Findlay J.B.C., Humphries P., Kenna P.F.; RT "A novel mutation within the rhodopsin gene (Thr-94-Ile) causing RT autosomal dominant congenital stationary night blindness."; RL Hum. Mutat. 13:75-81(1999). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=495 nm; CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Rod shaped photoreceptor cells which mediates CC vision in dim light. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region. CC -!- DISEASE: Defects in RHO are the cause of retinitis pigmentosa 4 CC (RP4) [MIM:180380]; a form of autosomal dominant retinitis CC pigmentosa. Retinitis pigmentosa (RP) [MIM:268000] leads to CC degeneration of retinal photoreceptor cells. Patients typically CC have night vision blindness and loss of midperipheral visual CC field. As their condition progresses, they lose their far CC peripheral visual field and eventually central vision as well. CC -!- DISEASE: Defects in RHO are a cause of autosomal recessive CC retinitis pigmentosa (ARRP) [MIM:268000]. CC -!- DISEASE: Defects in RHO are a cause of autosomal dominant CC congenital stationary night blindness 1 (CSNBAD1) [MIM:610445]; CC also known as rhodopsin-related congenital stationary night CC blindness. Congenital stationary night blindness is a CC nonprogressive retinal disorder characterized by impaired night CC vision and ocular symptoms such as myopia, hyperopia, nystagmus CC and reduced visual acuity. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC -!- WEB RESOURCE: NAME=RHO; NOTE=Rhodopsin mutations page; CC URL="http://mol.ophth.uiowa.edu/MOL_WWW/Rhotab.html". CC -!- WEB RESOURCE: NAME=Mutations of the RHO gene; CC NOTE=Retina International's Scientific Newsletter; CC URL="http://www.retina-international.com/sci-news/rhomut.htm". CC -!- WEB RESOURCE: NAME=GeneReviews; CC URL="http://www.genetests.org/query?gene=RHO". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U49742; AAC31763.1; -; Genomic_DNA. DR EMBL; AB065668; BAC05894.1; -; Genomic_DNA. DR EMBL; BX537381; CAD97623.1; -; mRNA. DR EMBL; BC112104; AAI12105.1; -; mRNA. DR EMBL; BC112106; AAI12107.1; -; mRNA. DR EMBL; U16824; AAA97436.1; -; Genomic_DNA. DR EMBL; S81166; AAB35906.1; -; Genomic_DNA. DR PIR; A41200; OOHU. DR UniGene; Hs.247565; -. DR HSSP; P02699; 1EDS. DR SMR; P08100; 1-348. DR GlycoSuiteDB; P08100; -. DR Ensembl; ENSG00000163914; Homo sapiens. DR KEGG; hsa:6010; -. DR HGNC; HGNC:10012; RHO. DR MIM; 180380; gene+phenotype. DR MIM; 268000; phenotype. DR MIM; 610445; phenotype. DR ArrayExpress; P08100; -. DR GermOnline; ENSG00000163914; Homo sapiens. DR RZPD-ProtExp; RZPDo834D0247; -. DR RZPD-ProtExp; T1321; -. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; TAS:ProtInc. DR GO; GO:0007603; P:phototransduction, visible light; TAS:ProtInc. DR GO; GO:0016056; P:rhodopsin mediated signaling; TAS:ProtInc. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR000732; Rhodopsin. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00579; RHODOPSIN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Acetylation; Chromophore; Disease mutation; KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane; KW Palmitate; Phosphorylation; Photoreceptor protein; Polymorphism; KW Receptor; Retinal protein; Retinitis pigmentosa; Sensory transduction; KW Transducer; Transmembrane; Vision. FT CHAIN 1 348 Rhodopsin. FT /FTId=PRO_0000197677. FT TOPO_DOM 1 36 Extracellular. FT TRANSMEM 37 61 1 (Potential). FT TOPO_DOM 62 73 Cytoplasmic. FT TRANSMEM 74 98 2 (Potential). FT TOPO_DOM 99 113 Extracellular. FT TRANSMEM 114 133 3 (Potential). FT TOPO_DOM 134 152 Cytoplasmic. FT TRANSMEM 153 176 4 (Potential). FT TOPO_DOM 177 202 Extracellular. FT TRANSMEM 203 230 5 (Potential). FT TOPO_DOM 231 252 Cytoplasmic. FT TRANSMEM 253 276 6 (Potential). FT TOPO_DOM 277 284 Extracellular. FT TRANSMEM 285 309 7 (Potential). FT TOPO_DOM 310 348 Cytoplasmic. FT BINDING 296 296 Retinal chromophore (covalent). FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 334 334 Phosphoserine (By similarity). FT MOD_RES 338 338 Phosphoserine (By similarity). FT MOD_RES 343 343 Phosphoserine (By similarity). FT LIPID 322 322 S-palmitoyl cysteine (By similarity). FT LIPID 323 323 S-palmitoyl cysteine (By similarity). FT CARBOHYD 2 2 N-linked (GlcNAc...) (By similarity). FT CARBOHYD 15 15 N-linked (GlcNAc...) (By similarity). FT DISULFID 110 187 By similarity. FT VARIANT 4 4 T -> K (in RP4). FT /FTId=VAR_004765. FT VARIANT 15 15 N -> S (in RP4). FT /FTId=VAR_004766. FT VARIANT 17 17 T -> M (in RP4). FT /FTId=VAR_004767. FT VARIANT 23 23 P -> H (in RP4; most common variant). FT /FTId=VAR_004768. FT VARIANT 23 23 P -> L (in RP4). FT /FTId=VAR_004769. FT VARIANT 28 28 Q -> H (in RP4). FT /FTId=VAR_004770. FT VARIANT 40 40 L -> R (in RP4). FT /FTId=VAR_004771. FT VARIANT 44 44 M -> T (in RP4). FT /FTId=VAR_004772. FT VARIANT 45 45 F -> L (in RP4). FT /FTId=VAR_004773. FT VARIANT 46 46 L -> R (in RP4). FT /FTId=VAR_004774. FT VARIANT 51 51 G -> A (effect not known). FT /FTId=VAR_004775. FT VARIANT 51 51 G -> R (in RP4). FT /FTId=VAR_004776. FT VARIANT 51 51 G -> V (in RP4). FT /FTId=VAR_004777. FT VARIANT 53 53 P -> R (in RP4). FT /FTId=VAR_004778. FT VARIANT 58 58 T -> R (in RP4). FT /FTId=VAR_004779. FT VARIANT 68 71 Missing (in RP4). FT /FTId=VAR_004780. FT VARIANT 87 87 V -> D (in RP4). FT /FTId=VAR_004781. FT VARIANT 89 89 G -> D (in RP4). FT /FTId=VAR_004782. FT VARIANT 90 90 G -> D (in CSNBAD1). FT /FTId=VAR_004783. FT VARIANT 94 94 T -> I (in CSNBAD1). FT /FTId=VAR_004784. FT VARIANT 104 104 V -> I. FT /FTId=VAR_004785. FT VARIANT 106 106 G -> R (in RP4). FT /FTId=VAR_004786. FT VARIANT 106 106 G -> W (in RP4). FT /FTId=VAR_004787. FT VARIANT 109 109 G -> R (in RP4). FT /FTId=VAR_004788. FT VARIANT 110 110 C -> F (in RP4). FT /FTId=VAR_004789. FT VARIANT 110 110 C -> Y (in RP4). FT /FTId=VAR_004790. FT VARIANT 114 114 G -> D (in RP4). FT /FTId=VAR_004791. FT VARIANT 125 125 L -> R (in RP4). FT /FTId=VAR_004792. FT VARIANT 127 127 S -> F (in RP4). FT /FTId=VAR_004793. FT VARIANT 131 131 L -> P (in RP4). FT /FTId=VAR_004794. FT VARIANT 135 135 R -> G (in RP4). FT /FTId=VAR_004795. FT VARIANT 135 135 R -> L (in RP4). FT /FTId=VAR_004796. FT VARIANT 135 135 R -> W (in RP4). FT /FTId=VAR_004797. FT VARIANT 140 140 C -> S (in RP4). FT /FTId=VAR_004798. FT VARIANT 150 150 E -> K (in ARRP). FT /FTId=VAR_004799. FT VARIANT 164 164 A -> E (in RP4). FT /FTId=VAR_004800. FT VARIANT 164 164 A -> V (in RP4). FT /FTId=VAR_004801. FT VARIANT 167 167 C -> R (in RP4). FT /FTId=VAR_004802. FT VARIANT 171 171 P -> L (in RP4). FT /FTId=VAR_004803. FT VARIANT 171 171 P -> Q (in RP4). FT /FTId=VAR_004804. FT VARIANT 171 171 P -> S (in RP4). FT /FTId=VAR_004805. FT VARIANT 178 178 Y -> C (in RP4). FT /FTId=VAR_004806. FT VARIANT 178 178 Y -> N (in RP4). FT /FTId=VAR_004807. FT VARIANT 181 181 E -> K (in RP4). FT /FTId=VAR_004808. FT VARIANT 182 182 G -> S (in RP4). FT /FTId=VAR_004809. FT VARIANT 186 186 S -> P (in RP4). FT /FTId=VAR_004810. FT VARIANT 188 188 G -> E (in RP4). FT /FTId=VAR_004811. FT VARIANT 188 188 G -> R (in RP4). FT /FTId=VAR_004812. FT VARIANT 190 190 D -> G (in RP4). FT /FTId=VAR_004814. FT VARIANT 190 190 D -> N (in RP4). FT /FTId=VAR_004813. FT VARIANT 190 190 D -> Y (in RP4). FT /FTId=VAR_004815. FT VARIANT 207 207 M -> R (in RP4). FT /FTId=VAR_004816. FT VARIANT 209 209 V -> M (effect not known). FT /FTId=VAR_004817. FT VARIANT 211 211 H -> P (in RP4). FT /FTId=VAR_004818. FT VARIANT 211 211 H -> R (in RP4). FT /FTId=VAR_004819. FT VARIANT 216 216 M -> K (in RP4). FT /FTId=VAR_004820. FT VARIANT 220 220 F -> C (in RP4). FT /FTId=VAR_004821. FT VARIANT 222 222 C -> R (in RP4). FT /FTId=VAR_004822. FT VARIANT 255 255 Missing (in RP4). FT /FTId=VAR_004823. FT VARIANT 264 264 Missing (in RP4). FT /FTId=VAR_004824. FT VARIANT 267 267 P -> L (in RP4). FT /FTId=VAR_004825. FT VARIANT 267 267 P -> R (in RP4). FT /FTId=VAR_004826. FT VARIANT 292 292 A -> E (in CSNBAD1). FT /FTId=VAR_004827. FT VARIANT 296 296 K -> E (in RP4). FT /FTId=VAR_004828. FT VARIANT 297 297 S -> R (in RP4). FT /FTId=VAR_004829. FT VARIANT 342 342 T -> M (in RP4). FT /FTId=VAR_004830. FT VARIANT 345 345 V -> L (in RP4). FT /FTId=VAR_004831. FT VARIANT 345 345 V -> M (in RP4). FT /FTId=VAR_004832. FT VARIANT 347 347 P -> A (in RP4). FT /FTId=VAR_004833. FT VARIANT 347 347 P -> L (in RP4; common variant). FT /FTId=VAR_004834. FT VARIANT 347 347 P -> Q (in RP4). FT /FTId=VAR_004835. FT VARIANT 347 347 P -> R (in RP4). FT /FTId=VAR_004836. FT VARIANT 347 347 P -> S (in RP4). FT /FTId=VAR_004837. SQ SEQUENCE 348 AA; 38893 MW; 6F4F6FCBA34265B2 CRC64; MNGTEGPNFY VPFSNATGVV RSPFEYPQYY LAEPWQFSML AAYMFLLIVL GFPINFLTLY VTVQHKKLRT PLNYILLNLA VADLFMVLGG FTSTLYTSLH GYFVFGPTGC NLEGFFATLG GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVAFT WVMALACAAP PLAGWSRYIP EGLQCSCGID YYTLKPEVNN ESFVIYMFVV HFTIPMIIIF FCYGQLVFTV KEAAAQQQES ATTQKAEKEV TRMVIIMVIA FLICWVPYAS VAFYIFTHQG SNFGPIFMTI PAFFAKSAAI YNPVIYIMMN KQFRNCMLTT ICCGKNPLGD DEASATVSKT ETSQVAPA // ID AMIC_PSEAE Reviewed; 385 AA. AC P27017; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 5. DT 20-MAR-2007, entry version 50. DE Aliphatic amidase expression-regulating protein. GN Name=amiC; OrderedLocusNames=PA3364; OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-19. RC STRAIN=PAC; RX MEDLINE=91317707; PubMed=1907262; RA Wilson S.A., Drew R.E.; RT "Cloning and DNA sequence of amiC, a new gene regulating expression of RT the Pseudomonas aeruginosa aliphatic amidase, and purification of the RT amiC product."; RL J. Bacteriol. 173:4914-4921(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; RX MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). RN [3] RP CRYSTALLIZATION. RX MEDLINE=92106343; PubMed=1762155; DOI=10.1016/0022-2836(91)90579-U; RA Wilson S.A., Chayen N.E., Hemmings A.M., Drew R.E., Pearl L.H.; RT "Crystallization of and preliminary X-ray data for the negative RT regulator (AmiC) of the amidase operon of Pseudomonas aeruginosa."; RL J. Mol. Biol. 222:869-871(1991). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SEQUENCE REVISION TO 27-28. RX MEDLINE=95112789; PubMed=7813419; RA Pearl L.H., O'Hara B.P., Drew R.E., Wilson S.A.; RT "Crystal structure of AmiC: the controller of transcription RT antitermination in the amidase operon of Pseudomonas aeruginosa."; RL EMBO J. 13:5810-5817(1994). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF COMPLEX WITH AMIR. RC STRAIN=PAC1; RX MEDLINE=99437995; PubMed=10508151; DOI=10.1093/emboj/18.19.5175; RA O'Hara B.P., Norman R.A., Wan P.T., Roe S.M., Barrett T.E., Drew R.E., RA Pearl L.H.; RT "Crystal structure and induction mechanism of AmiC-AmiR: a ligand- RT regulated transcription antitermination complex."; RL EMBO J. 18:5175-5186(1999). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). RC STRAIN=PAC1; RX MEDLINE=20175740; PubMed=10708652; DOI=10.1093/protein/13.2.129; RA O'Hara B.P., Wilson S.A., Lee A.W., Roe S.M., Siligardi G., Drew R.E., RA Pearl L.H.; RT "Structural adaptation to selective pressure for altered ligand RT specificity in the Pseudomonas aeruginosa amide receptor, AmiC."; RL Protein Eng. 13:129-132(2000). CC -!- FUNCTION: Negatively regulates the expression of the aliphatic CC amidase operon. AmiC functions by inhibiting the action of amiR at CC the protein level. It exhibits protein kinase activity. CC -!- SUBUNIT: Homodimer. Forms a complex with amiR. CC -!- DOMAIN: Consists of two beta-alpha-beta domains with a central CC cleft in which the amide binds. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X13776; CAA32024.1; -; Genomic_DNA. DR EMBL; AE004091; AAG06752.1; -; Genomic_DNA. DR PIR; C83226; C83226. DR PDB; 1PEA; X-ray; @=1-385. DR PDB; 1QNL; X-ray; A=1-385. DR PDB; 1QO0; X-ray; A/B=1-385. DR IntAct; P27017; -. DR GenomeReviews; AE004091_GR; PA3364. DR KEGG; pae:PA3364; -. DR BioCyc; PAER287:PA3364-MONOMER; -. DR LinkHub; P27017; -. DR InterPro; IPR000709; Leu_Ile_Val_bd. DR PRINTS; PR00337; LEUILEVALBP. KW 3D-structure; Complete proteome; Direct protein sequencing; Kinase; KW Repressor; Transferase. FT INIT_MET 1 1 Removed. FT CHAIN 2 385 Aliphatic amidase expression-regulating FT protein. FT /FTId=PRO_0000064581. FT VARIANT 106 106 T -> N (in strain: PAC181; butyramide FT inducible phenotype). FT CONFLICT 27 28 QR -> HA (in Ref. 1). FT CONFLICT 186 186 V -> L (in Ref. 1). FT CONFLICT 263 263 A -> P (in Ref. 1). FT CONFLICT 305 305 S -> N (in Ref. 1). FT CONFLICT 319 319 C -> D (in Ref. 1). FT CONFLICT 383 383 A -> P (in Ref. 1). FT STRAND 8 12 FT STRAND 15 17 FT HELIX 20 38 FT TURN 39 42 FT STRAND 49 53 FT HELIX 59 71 FT STRAND 77 80 FT HELIX 84 96 FT STRAND 100 103 FT STRAND 116 118 FT HELIX 123 125 FT HELIX 127 135 FT TURN 136 138 FT STRAND 140 149 FT HELIX 150 165 FT STRAND 169 176 FT HELIX 182 195 FT STRAND 198 203 FT HELIX 208 220 FT STRAND 228 232 FT HELIX 235 238 FT HELIX 243 246 FT STRAND 250 254 FT HELIX 262 272 FT HELIX 283 302 FT HELIX 307 314 FT STRAND 319 321 FT STRAND 324 328 FT TURN 330 332 FT STRAND 335 337 FT STRAND 340 344 FT STRAND 350 355 FT HELIX 368 370 SQ SEQUENCE 385 AA; 42807 MW; 33924B6C36017B79 CRC64; MGSHQERPLI GLLFSETGVT ADIERSQRYG ALLAVEQLNR EGGVGGRPIE TLSQDPGGDP DRYRLCAEDF IRNRGVRFLV GCYMSHTRKA VMPVVERADA LLCYPTPYEG FEYSPNIVYG GPAPNQNSAP LAAYLIRHYG ERVVFIGSDY IYPRESNHVM RHLYRQHGGT VLEEIYIPLY PSDDDVQRAV ERIYQARADV VFSTVVGTGT AELYRAIARR YGDGRRPPIA SLTTSEAEVA KMESDVAEGQ VVVAPYFSSI DTAASRAFVQ ACHGFFPENA TITAWAEAAY WQTLLLGRAA QAAGSWRVED VQRHLYDICI DAPQGPVRVE RQNNHSRLSS RIAEIDARGV FQVRWQSPEP IRPDPYVVVH NLDDWSASMG GGALP // ID AMIR_PSEAE Reviewed; 196 AA. AC P10932; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 08-DEC-2000, sequence version 2. DT 20-MAR-2007, entry version 55. DE Aliphatic amidase regulator. GN Name=amiR; OrderedLocusNames=PA3363; OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=PAC433; RX MEDLINE=89211409; PubMed=2495988; DOI=10.1016/0014-5793(89)80249-2; RA Lowe N., Rice P.M., Drew R.E.; RT "Nucleotide sequence of the aliphatic amidase regulator gene (amiR) of RT Pseudomonas aeruginosa."; RL FEBS Lett. 246:39-43(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228; RX MEDLINE=20437337; PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., RA Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an RT opportunistic pathogen."; RL Nature 406:959-964(2000). RN [3] RP CHARACTERIZATION. RX MEDLINE=95286483; PubMed=7539417; RA Wilson S.A., Drew R.E.; RT "Transcriptional analysis of the amidase operon from Pseudomonas RT aeruginosa."; RL J. Bacteriol. 177:3052-3057(1995). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF COMPLEX WITH AMIC. RC STRAIN=PAC1; RX MEDLINE=99437995; PubMed=10508151; DOI=10.1093/emboj/18.19.5175; RA O'Hara B.P., Norman R.A., Wan P.T., Roe S.M., Barrett T.E., Drew R.E., RA Pearl L.H.; RT "Crystal structure and induction mechanism of AmiC-AmiR: a ligand- RT regulated transcription antitermination complex."; RL EMBO J. 18:5175-5186(1999). CC -!- FUNCTION: Positive controlling element of amiE, the gene for CC aliphatic amidase. Acts as a transcriptional antitermination CC factor. It is thought to allow RNA polymerase read through a rho- CC independent transcription terminator between the amiE promoter and CC gene. CC -!- SUBUNIT: Forms a complex with amiC. CC -!- SIMILARITY: Contains 1 ANTAR domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X13776; CAA32023.1; -; Genomic_DNA. DR EMBL; AE004091; AAG06751.1; -; Genomic_DNA. DR PIR; B83226; B83226. DR PIR; S03884; S03884. DR PDB; 1QO0; X-ray; D/E=1-196. DR IntAct; P10932; -. DR GenomeReviews; AE004091_GR; PA3363. DR KEGG; pae:PA3363; -. DR BioCyc; PAER287:PA3363-MONOMER; -. DR InterPro; IPR005561; AmiR_NasR_reg. DR InterPro; IPR011006; CheY_like. DR InterPro; IPR008327; Res_reg_antiterm. DR Pfam; PF03861; ANTAR; 1. DR PIRSF; PIRSF036382; RR_antiterm; 1. DR PROSITE; PS50921; ANTAR; 1. KW 3D-structure; Complete proteome; Transcription; KW Transcription antitermination; Transcription regulation. FT CHAIN 1 196 Aliphatic amidase regulator. FT /FTId=PRO_0000064582. FT DOMAIN 129 190 ANTAR. FT CONFLICT 48 48 S -> A (in Ref. 1). FT CONFLICT 64 64 R -> G (in Ref. 1). FT CONFLICT 141 141 E -> D (in Ref. 1). FT CONFLICT 154 154 A -> V (in Ref. 1). FT CONFLICT 170 170 Y -> H (in Ref. 1). FT HELIX 3 8 FT HELIX 9 12 FT STRAND 14 19 FT HELIX 23 35 FT STRAND 38 42 FT STRAND 54 59 FT HELIX 65 75 FT STRAND 81 86 FT HELIX 91 100 FT STRAND 103 109 FT HELIX 112 114 FT HELIX 115 160 FT HELIX 164 175 FT TURN 176 179 FT HELIX 182 189 SQ SEQUENCE 196 AA; 21903 MW; 306A4F30E8E4C6C0 CRC64; MSANSLLGSL RELQVLVLNP PGEVSDALVL QLIRIGCSVR QCWPPPESFD VPVDVVFTSI FQNRHHDEIA ALLAAGTPRT TLVALVEYES PAVLSQIIEL ECHGVITQPL DAHRVLPVLV SARRISEEMA KLKQKTEQLQ ERIAGQARIN QAKALLMQRH GWDEREAHQY LSREAMKRRE PILKIAQELL GNEPSA // ID GCN4_YEAST Reviewed; 281 AA. AC P03069; P03068; Q70D88; Q70D91; Q70D96; Q70D99; Q70DA0; Q96UT3; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 20-MAR-2007, entry version 82. DE General control protein GCN4 (Amino acid biosynthesis regulatory DE protein). GN Name=GCN4; Synonyms=AAS3, ARG9; OrderedLocusNames=YEL009C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=85038531; PubMed=6387704; RA Hinnebusch A.G.; RT "Evidence for translational regulation of the activator of general RT amino acid control in yeast."; RL Proc. Natl. Acad. Sci. U.S.A. 81:6442-6446(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=84298088; PubMed=6433345; RA Thireos G., Penn M.D., Greer H.; RT "5' untranslated sequences are required for the translational control RT of a yeast regulatory gene."; RL Proc. Natl. Acad. Sci. U.S.A. 81:5096-5100(1984). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-24; SER-62; RP ALA-82; ALA-91; ALA-125 AND GLU-196. RC STRAIN=CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556, RC CLIB 630, CLIB 95, K1, R12, R13, Sigma 1278B, YIIc12, and YIIc17; RX PubMed=15087486; DOI=10.1093/nar/gkh529; RA Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S., RA Souciet J.-L.; RT "Differential evolution of the Saccharomyces cerevisiae DUP240 RT paralogs and implication of recombination in phylogeny."; RL Nucleic Acids Res. 32:2069-2078(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=97313264; PubMed=9169868; RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., RA Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., RA Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., RA Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., RA Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; RL Nature 387:78-81(1997). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 249-281. RX PubMed=11896344; DOI=10.1046/j.1537-2995.2002.00018.x; RA Czerwinski M., Krop-Watorek A., Lisowska E., Spitalnik S.L.; RT "Construction of dimeric F(ab) useful in blood group serology."; RL Transfusion 42:257-264(2002). RN [6] RP DOMAINS. RX MEDLINE=87002456; PubMed=3530496; DOI=10.1016/0092-8674(86)90070-X; RA Hope I.A., Struhl K.; RT "Functional dissection of a eukaryotic transcriptional activator RT protein, GCN4 of yeast."; RL Cell 46:885-894(1986). RN [7] RP DOMAINS, AND MUTAGENESIS OF 97-PHE-PHE-98; MET-107; TYR-110; LEU-113 RP AND 120-TRP--PHE-124. RX PubMed=7862116; RA Drysdale C.M., Duenas E., Jackson B.M., Reusser U., Braus G.H., RA Hinnebusch A.G.; RT "The transcriptional activator GCN4 contains multiple activation RT domains that are critically dependent on hydrophobic amino acids."; RL Mol. Cell. Biol. 15:1220-1233(1995). RN [8] RP PHOSPHORYLATION AT THR-165. RX PubMed=12101234; DOI=10.1128/MCB.22.15.5395-5404.2002; RA Shemer R., Meimoun A., Holtzman T., Kornitzer D.; RT "Regulation of the transcription factor Gcn4 by Pho85 cyclin PCL5."; RL Mol. Cell. Biol. 22:5395-5404(2002). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 250-281. RX MEDLINE=92054531; PubMed=1948029; RA O'Shea E.K., Klemm J.D., Kim P.S., Alber T.; RT "X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel RT coiled coil."; RL Science 254:539-544(1991). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 226-281. RX MEDLINE=93113690; PubMed=1473154; DOI=10.1016/S0092-8674(05)80070-4; RA Ellenberger T.E., Brandl C.J., Struhl K., Harrison S.C.; RT "The GCN4 basic region leucine zipper binds DNA as a dimer of RT uninterrupted alpha helices: crystal structure of the protein-DNA RT complex."; RL Cell 71:1223-1237(1992). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 249-281. RX MEDLINE=99057965; PubMed=9837709; DOI=10.1006/jmbi.1998.2214; RA Eckert D.M., Malashkevich V.N., Kim P.S.; RT "Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried RT polar residues."; RL J. Mol. Biol. 284:859-865(1998). RN [12] RP STRUCTURE BY NMR OF 237-281. RX MEDLINE=91367802; PubMed=1891459; DOI=10.1093/protein/4.5.519; RA Saudek V., Pastore A., Morelli M.A., Frank R., Gausepohl H., RA Gibson T.; RT "The solution structure of a leucine-zipper motif peptide."; RL Protein Eng. 4:519-529(1991). CC -!- FUNCTION: Is a transcription factor that is responsible for the CC activation of more than 30 genes required for amino acid or for CC purine biosynthesis in response to amino acid or purine CC starvation. Binds and recognize the DNA sequence: 5'-TGA[CG]TCA- CC 3'. CC -!- SUBUNIT: Binds DNA as a dimer. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- DOMAIN: Residues 89 to 100 and 106 to 125 define the N-terminal CC activation domain (NTAD) and the central acidic activation domain CC (CAAD) respectively, which can function independently to promote CC high-level transcription of the target genes. CC -!- PTM: Phosphorylated by the cyclin-CDK PCL5-PHO85. Phosphorylation CC of Thr-165 induces degradation of GCN4 by the E3 ubiquitin ligase CC complex SCF(Cdc4). CC -!- SIMILARITY: Belongs to the bZIP family. GCN4 subfamily. CC -!- SIMILARITY: Contains 1 bZIP domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; K02205; AAA34640.1; -; Genomic_DNA. DR EMBL; K02649; AAA65521.1; -; Genomic_DNA. DR EMBL; AJ585686; CAE52206.1; -; Genomic_DNA. DR EMBL; AJ585687; CAE52207.1; -; Genomic_DNA. DR EMBL; AJ585688; CAE52208.1; -; Genomic_DNA. DR EMBL; AJ585689; CAE52209.1; -; Genomic_DNA. DR EMBL; AJ585690; CAE52210.1; -; Genomic_DNA. DR EMBL; AJ585691; CAE52211.1; -; Genomic_DNA. DR EMBL; AJ585692; CAE52212.1; -; Genomic_DNA. DR EMBL; AJ585693; CAE52213.1; -; Genomic_DNA. DR EMBL; AJ585694; CAE52214.1; -; Genomic_DNA. DR EMBL; AJ585695; CAE52215.1; -; Genomic_DNA. DR EMBL; AJ585696; CAE52216.1; -; Genomic_DNA. DR EMBL; AJ585697; CAE52217.1; -; Genomic_DNA. DR EMBL; AJ585698; CAE52218.1; -; Genomic_DNA. DR EMBL; AJ585699; CAE52219.1; -; Genomic_DNA. DR EMBL; AJ585700; CAE52220.1; -; Genomic_DNA. DR EMBL; AJ585701; CAE52221.1; -; Genomic_DNA. DR EMBL; AJ585702; CAE52222.1; -; Genomic_DNA. DR EMBL; AJ585703; CAE52223.1; -; Genomic_DNA. DR EMBL; AJ585704; CAE52224.1; -; Genomic_DNA. DR EMBL; AF416613; AAL09032.1; -; mRNA. DR EMBL; U18530; AAB64486.1; -; Genomic_DNA. DR PIR; A03605; RGBYA2. DR PDB; 1CE9; X-ray; A/B/C/D=251-281. DR PDB; 1DGC; X-ray; A=220-281. DR PDB; 1FAV; X-ray; A=-. DR PDB; 1GCL; X-ray; A/B/C/D=249-281. DR PDB; 1GCM; X-ray; A/B/C=249-281. DR PDB; 1GK6; X-ray; A/B=-. DR PDB; 1GZL; X-ray; A/B=-. DR PDB; 1IHQ; NMR; A/B=-. DR PDB; 1IJ0; X-ray; A/B/C=249-281. DR PDB; 1IJ1; X-ray; A/B/C=249-281. DR PDB; 1IJ2; X-ray; A/B/C=249-281. DR PDB; 1IJ3; X-ray; A/B/C=249-281. DR PDB; 1KQL; X-ray; A/B=255-281. DR PDB; 1LD4; EM; E/F/G/H/I/J/K/L=225-281. DR PDB; 1LLM; X-ray; C/D=-. DR PDB; 1NKN; X-ray; A/B/C/D=-. DR PDB; 1PIQ; X-ray; A=249-279. DR PDB; 1RB1; X-ray; A/B/C=249-281. DR PDB; 1RB4; X-ray; A/B/C=249-281. DR PDB; 1RB5; X-ray; A/B/C=249-281. DR PDB; 1RB6; X-ray; A/B/C=249-281. DR PDB; 1SWI; X-ray; A/B/C=249-281. DR PDB; 1TMZ; NMR; A/B=-. DR PDB; 1UNT; X-ray; A/B=249-281. DR PDB; 1UNU; X-ray; A/B=249-281. DR PDB; 1UNV; X-ray; A/B=249-281. DR PDB; 1UNW; X-ray; A/B=249-281. DR PDB; 1UNX; X-ray; A/B=249-281. DR PDB; 1UNY; X-ray; A/B=249-281. DR PDB; 1UNZ; X-ray; A/B=249-281. DR PDB; 1UO0; X-ray; A/B=249-281. DR PDB; 1UO1; X-ray; A/B=249-281. DR PDB; 1UO2; X-ray; A/B=249-281. DR PDB; 1UO3; X-ray; A/B=249-281. DR PDB; 1UO4; X-ray; A/B=249-281. DR PDB; 1UO5; X-ray; A/B=249-281. DR PDB; 1W5G; X-ray; A/B=249-281. DR PDB; 1W5H; X-ray; A/B=249-281. DR PDB; 1W5I; X-ray; A/B=249-281. DR PDB; 1W5J; X-ray; A/B/C/D=249-281. DR PDB; 1W5K; X-ray; A/B/C/D=249-281. DR PDB; 1W5L; X-ray; A/B=249-281. DR PDB; 1YSA; X-ray; C/D=226-281. DR PDB; 1ZII; X-ray; A/B=249-281. DR PDB; 1ZIJ; X-ray; A/B/C=249-281. DR PDB; 1ZIK; X-ray; A/B=249-281. DR PDB; 1ZIL; X-ray; A/B=249-281. DR PDB; 1ZIM; X-ray; A/B/C=249-281. DR PDB; 1ZTA; NMR; @=247-281. DR PDB; 2B1F; X-ray; A/B/C/D=251-281. DR PDB; 2B22; X-ray; A=251-281. DR PDB; 2BNI; X-ray; A/B/C/D=249-281. DR PDB; 2DGC; X-ray; A=220-281. DR PDB; 2ZTA; X-ray; A/B=249-281. DR DIP; DIP:591N; -. DR TRANSFAC; T00321; -. DR Ensembl; YEL009C; Saccharomyces cerevisiae. DR GenomeReviews; U00092_GR; YEL009C. DR KEGG; sce:YEL009C; -. DR CYGD; YEL009c; -. DR SGD; S000000735; GCN4. DR BioCyc; SCER-S28-01:SCER-S28-01-001585-MONOMER; -. DR LinkHub; P03069; -. DR GermOnline; YEL009C; Saccharomyces cerevisiae. DR GO; GO:0005634; C:nucleus; IPI:SGD. DR GO; GO:0003700; F:transcription factor activity; IDA:SGD. DR GO; GO:0008652; P:amino acid biosynthetic process; TAS:SGD. DR GO; GO:0006990; P:unfolded protein response, positive regulat...; IMP:SGD. DR InterPro; IPR011616; bZIP_1. DR InterPro; IPR004827; TF_bZIP. DR Pfam; PF00170; bZIP_1; 1. DR SMART; SM00338; BRLZ; 1. DR PROSITE; PS50217; BZIP; 1. DR PROSITE; PS00036; BZIP_BASIC; 1. KW 3D-structure; Activator; Amino-acid biosynthesis; Complete proteome; KW DNA-binding; Nuclear protein; Phosphorylation; Transcription; KW Transcription regulation. FT CHAIN 1 281 General control protein GCN4. FT /FTId=PRO_0000076490. FT DOMAIN 253 274 Leucine-zipper. FT DNA_BIND 231 249 Basic motif. FT REGION 89 100 Required for transcriptional activation. FT REGION 106 125 Required for transcriptional activation. FT MOD_RES 165 165 Phosphothreonine (by PHO85). FT VARIANT 24 24 S -> P (in strain: CLIB 219). FT VARIANT 62 62 P -> S (in strain: CLIB 630 haplotype FT Ha2). FT VARIANT 82 82 T -> A (in strain: CLIB 556 haplotype FT Ha1). FT VARIANT 91 91 D -> A (in strain: CLIB 95, CLIB 219, FT CLIB 382, CLIB 388, CLIB 410, CLIB 413, FT CLIB 556, CLIB 630, K1, R12, R13 FT haplotype Ha2, Sigma 1278B haplotype Ha1, FT YIIc12 and YIIc17). FT VARIANT 125 125 D -> A (in strain: CLIB 556 haplotype FT Ha1). FT VARIANT 196 196 D -> E (in strain: CLIB 388, CLIB 410, FT CLIB 413, CLIB 630 haplotype Ha1, K1, FT YIIc12 haplotype Ha2 and YIIc17 haplotype FT Ha1). FT MUTAGEN 97 98 FF->AA: Reduces transcriptional FT activation activity; when associated with FT A-107; A-110; A-113; A-120; A-123 and A- FT 124. FT MUTAGEN 107 107 M->A: Reduces transcriptional activation FT activity; when associated with A-97; A- FT 98; A-110; A-113; A-120; A-123 and A-124. FT MUTAGEN 110 110 Y->A: Reduces transcriptional activation FT activity; when associated with A-97; A- FT 98; A-107; A-113; A-120; A-123 and A-124. FT MUTAGEN 113 113 L->A: Reduces transcriptional activation FT activity; when associated with A-97; A- FT 98; A-107; A-110; A-120; A-123 and A-124. FT MUTAGEN 120 124 WTSLF->ATSAA: Reduces transcriptional FT activation activity; when associated with FT A-97; A-98; A-107; A-110 and A-113. FT CONFLICT 239 281 ARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVG FT ER -> PGVLVRESCKE (in Ref. 2). FT HELIX 230 276 FT HELIX 250 276 FT HELIX 251 278 SQ SEQUENCE 281 AA; 31310 MW; 2ED1B8E35D509578 CRC64; MSEYQPSLFA LNPMGFSPLD GSKSTNENVS ASTSTAKPMV GQLIFDKFIK TEEDPIIKQD TPSNLDFDFA LPQTATAPDA KTVLPIPELD DAVVESFFSS STDSTPMFEY ENLEDNSKEW TSLFDNDIPV TTDDVSLADK AIESTEEVSL VPSNLEVSTT SFLPTPVLED AKLTQTRKVK KPNSVVKKSH HVGKDDESRL DHLGVVAYNR KQRSIPLSPI VPESSDPAAL KRARNTEAAR RSRARKLQRM KQLEDKVEEL LSKNYHLENE VARLKKLVGE R // ID FLAV_ANASO Reviewed; 170 AA. AC P0A3E0; P11241; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 20-MAR-2007, entry version 17. DE Flavodoxin. GN Name=isiB; OS Anabaena sp. (strain PCC 7119). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=1168; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92074973; PubMed=1720613; RA Fillat M.F., Borrias W.E., Weisbeek P.J.; RT "Isolation and overexpression in Escherichia coli of the flavodoxin RT gene from Anabaena PCC 7119."; RL Biochem. J. 280:187-191(1991). RN [2] RP PROTEIN SEQUENCE OF 2-37. RX MEDLINE=90381288; PubMed=2119231; DOI=10.1016/0167-4838(90)90091-S; RA Fillat M.F., Edmondson D.E., Gomez-Moreno C.; RT "Structural and chemical properties of a flavodoxin from Anabaena PCC RT 7119."; RL Biochim. Biophys. Acta 1040:301-307(1990). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=99318886; PubMed=10388575; DOI=10.1006/jmbi.1999.2863; RA Fernandez-Recio J., Romero A., Sancho J.; RT "Energetics of a hydrogen bond (charged and neutral) and of a cation- RT pi interaction in apoflavodoxin."; RL J. Mol. Biol. 290:319-330(1999). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. CC -!- COFACTOR: FMN. CC -!- INTERACTION: CC P08165:FDXR (xeno); NbExp=3; IntAct=EBI-593907, EBI-593948; CC P10933:PETH (xeno); NbExp=1; IntAct=EBI-593907, EBI-931306; CC P21890:petH; NbExp=5; IntAct=EBI-593907, EBI-593915; CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S68006; AAB20462.1; -; Genomic_DNA. DR PDB; 1DX9; X-ray; A/B/C/D=1-170. DR PDB; 1FTG; X-ray; @=3-170. DR PDB; 1OBO; X-ray; A/B=3-170. DR PDB; 1OBV; X-ray; A=3-170. DR PDB; 1QHE; X-ray; A=3-170. DR IntAct; P0A3E0; -. DR LinkHub; P0A3E0; -. DR GO; GO:0009055; F:electron carrier activity; IDA:UniProtKB. DR GO; GO:0010181; F:FMN binding; TAS:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0010106; P:cellular response to iron ion starvation; TAS:UniProtKB. DR GO; GO:0006118; P:electron transport; IDA:UniProtKB. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW 3D-structure; Direct protein sequencing; Electron transport; KW Flavoprotein; FMN; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 170 Flavodoxin. FT /FTId=PRO_0000171600. FT DOMAIN 5 165 Flavodoxin-like. FT STRAND 3 8 FT STRAND 11 13 FT HELIX 14 26 FT TURN 28 30 FT STRAND 31 35 FT TURN 36 38 FT HELIX 41 46 FT STRAND 48 57 FT TURN 58 60 FT HELIX 64 70 FT HELIX 71 75 FT STRAND 82 88 FT TURN 91 96 FT HELIX 100 111 FT STRAND 137 143 FT TURN 145 147 FT HELIX 149 151 FT HELIX 152 167 SQ SEQUENCE 170 AA; 18964 MW; 069E8DEBA9E33302 CRC64; MSKKIGLFYG TQTGKTESVA EIIRDEFGND VVTLHDVSQA EVTDLNDYQY LIIGCPTWNI GELQSDWEGL YSELDDVDFN GKLVAYFGTG DQIGYADNFQ DAIGILEEKI SQRGGKTVGY WSTDGYDFND SKALRNGKFV GLALDEDNQS DLTDDRIKSW VAQLKSEFGL // ID FLAV_ANASP Reviewed; 170 AA. AC P0A3D9; P11241; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 20-MAR-2007, entry version 21. DE Flavodoxin. GN Name=isiB; OrderedLocusNames=alr2405; OS Anabaena sp. (strain PCC 7120). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=103690; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89296496; PubMed=2500643; DOI=10.1093/nar/17.11.4384; RA Leonhardt K.G., Straus N.A.; RT "Sequence of the flavodoxin gene from Anabaena variabilis 7120."; RL Nucleic Acids Res. 17:4384-4384(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21595285; PubMed=11759840; DOI=10.1093/dnares/8.5.205; RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., RA Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., RA Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., RA Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M., RA Yasuda M., Tabata S.; RT "Complete genomic sequence of the filamentous nitrogen-fixing RT cyanobacterium Anabaena sp. strain PCC 7120."; RL DNA Res. 8:205-213(2001). RN [3] RP STRUCTURE BY NMR. RX MEDLINE=91104858; PubMed=2125478; DOI=10.1021/bi00493a014; RA Stockman B.J., Krezel A.M., Markley J.L., Leonhardt K.G., Straus N.A.; RT "Hydrogen-1, carbon-13, and nitrogen-15 NMR spectroscopy of Anabaena RT 7120 flavodoxin: assignment of beta-sheet and flavin binding site RT resonances and analysis of protein-flavin interactions."; RL Biochemistry 29:9600-9609(1990). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=93271891; PubMed=1303762; RA Rao S.T., Shaffie F., Yu C., Satyshur K.A., Stockman B.J., RA Markley J.L., Sundaralingam M.; RT "Structure of the oxidized long-chain flavodoxin from Anabaena 7120 at RT 2-A resolution."; RL Protein Sci. 1:1413-1427(1992). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS). RX PubMed=15299298; DOI=10.1107/S0907444994011716; RA Burkhart B.M., Ramakrishnan B., Yan H., Reedstrom R.J., Markley J.L., RA Straus N.A., Sundaralingam M.; RT "Structure of the trigonal form of recombinant oxidized flavodoxin RT from Anabaena 7120 at 1.40-A resolution."; RL Acta Crystallogr. D 51:318-330(1995). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. CC -!- COFACTOR: FMN. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X14577; CAA32720.1; -; Genomic_DNA. DR EMBL; BA000019; BAB74104.1; -; Genomic_DNA. DR PIR; AF2106; AF2106. DR PDB; 1FLV; X-ray; @=1-170. DR PDB; 1RCF; X-ray; @=1-170. DR GenomeReviews; BA000019_GR; alr2405. DR KEGG; ana:alr2405; -. DR LinkHub; P0A3D9; -. DR GO; GO:0009767; P:photosynthetic electron transport; NAS:UniProtKB. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW 3D-structure; Complete proteome; Electron transport; Flavoprotein; KW FMN; Transport. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 170 Flavodoxin. FT /FTId=PRO_0000171601. FT DOMAIN 5 165 Flavodoxin-like. FT STRAND 4 8 FT STRAND 11 13 FT HELIX 14 25 FT TURN 26 28 FT STRAND 31 35 FT HELIX 41 46 FT STRAND 48 53 FT TURN 58 60 FT HELIX 64 70 FT HELIX 71 75 FT STRAND 82 88 FT TURN 91 96 FT HELIX 100 111 FT STRAND 137 143 FT TURN 145 147 FT HELIX 149 151 FT HELIX 152 166 SQ SEQUENCE 170 AA; 18964 MW; 069E8DEBA9E33302 CRC64; MSKKIGLFYG TQTGKTESVA EIIRDEFGND VVTLHDVSQA EVTDLNDYQY LIIGCPTWNI GELQSDWEGL YSELDDVDFN GKLVAYFGTG DQIGYADNFQ DAIGILEEKI SQRGGKTVGY WSTDGYDFND SKALRNGKFV GLALDEDNQS DLTDDRIKSW VAQLKSEFGL // ID FLAV_AQUAE Reviewed; 185 AA. AC O67866; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 20-MAR-2007, entry version 42. DE Flavodoxin. GN Name=fldA; Synonyms=floX; OrderedLocusNames=aq_2096; OS Aquifex aeolicus. OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex. OX NCBI_TaxID=63363; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VF5; RX MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831; RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.; RT "The complete genome of the hyperthermophilic bacterium Aquifex RT aeolicus."; RL Nature 392:353-358(1998). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes (By similarity). CC -!- COFACTOR: FMN (By similarity). CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000657; AAC07825.1; -; Genomic_DNA. DR PIR; F70479; F70479. DR PDB; 2ARK; X-ray; A/B/C/D/E/F=1-185. DR GenomeReviews; AE000657_GR; aq_2096. DR KEGG; aae:aq_2096; -. DR BioCyc; AAEO63363:AQ_2096-MONOMER; -. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW 3D-structure; Complete proteome; Electron transport; Flavoprotein; KW FMN; Transport. FT CHAIN 1 185 Flavodoxin. FT /FTId=PRO_0000171602. FT DOMAIN 4 159 Flavodoxin-like. FT STRAND 2 8 FT STRAND 11 13 FT HELIX 14 27 FT STRAND 32 38 FT TURN 39 41 FT HELIX 44 49 FT STRAND 51 58 FT HELIX 66 74 FT HELIX 76 78 FT TURN 79 81 FT STRAND 87 97 FT HELIX 101 114 FT STRAND 122 127 FT STRAND 130 141 FT HELIX 145 165 FT HELIX 172 178 FT HELIX 180 182 SQ SEQUENCE 185 AA; 20444 MW; 7C138666D5B89281 CRC64; MGKVLVIYDT RTGNTKKMAE LVAEGARSLE GTEVRLKHVD EATKEDVLWA DGLAVGSPTN MGLVSWKMKR FFDDVLGDLW GEIDGKIACA FSSSGGWGGG NEVACMSILT MLMNFGFLVF GVTDYVGKKF TLHYGAVVAG EPRSEEEKEA CRRLGRRLAE WVAIFVDGRK ELLEKIRKDP ARFVD // ID FLS1_ARATH Reviewed; 336 AA. AC Q96330; O04730; O04731; O04732; O04830; O04831; O04832; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 23-JAN-2007, entry version 50. DE Flavonol synthase/flavanone 3-hydroxylase (EC 1.14.11.23) DE (EC 1.14.11.9) (FLS 1). GN Name=FLS1; OrderedLocusNames=At5g08640; ORFNames=MAH20.20; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Landsberg erecta; RX MEDLINE=97267154; PubMed=9112784; DOI=10.1104/pp.113.4.1437; RA Pelletier M.K., Murrell J.R., Shirley B.W.; RT "Characterization of flavonol synthase and leucoanthocyanidin RT dioxygenase genes in Arabidopsis. Further evidence for differential RT regulation of 'early' and 'late' genes."; RL Plant Physiol. 113:1437-1445(1997). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=cv. Columbia, and cv. Landsberg erecta; RA Hartmann U., Weisshaar B.; RT "Isolation of an Arabidopsis clone encoding flavonol synthase."; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX MEDLINE=98069011; PubMed=9405937; DOI=10.1093/dnares/4.4.291; RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. RT Sequence features of the regions of 1,044,062 bp covered by thirteen RT physically assigned P1 clones."; RL DNA Res. 4:291-300(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the formation of flavonols from CC dihydroflavonols. It can act on dihydrokaempferol to produce CC kaempferol, on dihydroquercetin to produce quercitin and on CC dihydromyricetin to produce myricetin. CC -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a CC flavonol + succinate + CO(2) + H(2)O. CC -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a CC dihydroflavonol + succinate + CO(2). CC -!- COFACTOR: Binds 1 ascorbate molecule per subunit. CC -!- COFACTOR: Binds 1 iron ion per subunit. CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U72631; AAB17393.1; -; Genomic_DNA. DR EMBL; U84258; AAC69362.1; -; Genomic_DNA. DR EMBL; U84259; AAC69363.1; -; mRNA. DR EMBL; U84260; AAB41504.1; -; mRNA. DR EMBL; AB006697; BAB10013.1; -; Genomic_DNA. DR EMBL; AY058068; AAL24176.1; -; mRNA. DR EMBL; BT000494; AAN18063.1; -; mRNA. DR EMBL; AY086328; AAM64397.1; -; mRNA. DR UniGene; At.8771; -. DR HSSP; Q96323; 1GP6. DR GenomeReviews; BA000015_GR; AT5G08640. DR KEGG; ath:At5g08640; -. DR TAIR; At5g08640; -. DR ArrayExpress; Q96330; -. DR GermOnline; AT5G08640; Arabidopsis thaliana. DR GO; GO:0045431; F:flavonol synthase activity; IEA:EC. DR GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC. DR InterPro; IPR005123; 2OG-FeII_Oase. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. KW Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; KW Oxidoreductase; Vitamin C. FT CHAIN 1 336 Flavonol synthase/flavanone 3- FT hydroxylase. FT /FTId=PRO_0000067291. FT METAL 221 221 Iron (By similarity). FT METAL 223 223 Iron (By similarity). FT METAL 277 277 Iron (By similarity). SQ SEQUENCE 336 AA; 38282 MW; 3283E3AFE603D2A9 CRC64; MEVERVQDIS SSSLLTEAIP LEFIRSEKEQ PAITTFRGPT PAIPVVDLSD PDEESVRRAV VKASEEWGLF QVVNHGIPTE LIRRLQDVGR KFFELPSSEK ESVAKPEDSK DIEGYGTKLQ KDPEGKKAWV DHLFHRIWPP SCVNYRFWPK NPPEYREVNE EYAVHVKKLS ETLLGILSDG LGLKRDALKE GLGGEMAEYM MKINYYPPCP RPDLALGVPA HTDLSGITLL VPNEVPGLQV FKDDHWFDAE YIPSAVIVHI GDQILRLSNG RYKNVLHRTT VDKEKTRMSW PVFLEPPREK IVGPLPELTG DDNPPKFKPF AFKDYSYRKL NKLPLD // ID FLAV_AZOCH Reviewed; 180 AA. AC P23001; P35708; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 23-JAN-2007, entry version 48. DE Flavodoxin-B (FldB). GN Name=nifF; OS Azotobacter chroococcum mcd 1. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=355; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8765738; RA Peelen S., Wijmenga S., Erbel P.J., Robson R.L., Eady R.R., RA Vervoort J.; RT "Possible role of a short extra loop of the long-chain flavodoxin from RT Azotobacter chroococcum in electron transfer to nitrogenase: complete RT 1H, 15N and 13C backbone assignments and secondary solution structure RT of the flavodoxin."; RL J. Biomol. NMR 7:315-330(1996). RN [2] RP PROTEIN SEQUENCE OF 2-21. RC STRAIN=MCD 1155; RX MEDLINE=91315397; PubMed=1859358; RA Bagby S., Barker P.D., Hill H.A.O., Sanghera G.S., Dunbar B., RA Ashby G.A., Eady R.R., Thorneley R.N.F.; RT "Direct electrochemistry of two genetically distinct flavodoxins RT isolated from Azotobacter chroococcum grown under nitrogen-fixing RT conditions."; RL Biochem. J. 277:313-319(1991). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. NifF is the electron donor to nitrogenase. CC -!- COFACTOR: FMN. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M73019; AAB36613.1; -; Genomic_DNA. DR HSSP; P11241; 1OBO. DR SMR; P23001; 2-180. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Direct protein sequencing; Electron transport; Flavoprotein; FMN; KW Nitrogen fixation; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 180 Flavodoxin-B. FT /FTId=PRO_0000171603. FT DOMAIN 4 173 Flavodoxin-like. SQ SEQUENCE 180 AA; 19524 MW; A19BE720B93F551D CRC64; MAKIGLFFGS NTGKTRKVAK SIKKRFDDET MSDAVNVNRV SAEDFAQYQF LILGTPTLGE GELPGLSSDC ENESWEEFLP KIEGLDFSGK TVALFGLGDQ VGYPENFLDA MGELHSFFTE RGAKVVGAWS TDGYEFEGST AVVDGKFVGL ALDLDNQSGK TDERVAAWLA QIAPEFGLSL // ID FLAV_AZOVI Reviewed; 180 AA. AC P00324; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 20-MAR-2007, entry version 61. DE Flavodoxin-2. GN Name=nifF; OS Azotobacter vinelandii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=354; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89123097; PubMed=2644218; RA Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., RA Wilson M.S., Cash V.L., Beynon J., Newton W.E., Dean D.R.; RT "Physical and genetic map of the major nif gene cluster from RT Azotobacter vinelandii."; RL J. Bacteriol. 171:1017-1027(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88087273; PubMed=3121629; RA Bennett L., Jacobson M., Dean D.R.; RT "Isolation, sequencing, and mutagenesis of the nifF gene encoding RT flavodoxin from Azotobacter vinelandii."; RL J. Biol. Chem. 263:1364-1369(1988). RN [3] RP PROTEIN SEQUENCE OF 2-180. RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW; RX MEDLINE=77242321; PubMed=889809; DOI=10.1021/bi00635a005; RA Tanaka M., Haniu M., Yasunobu K.T., Yoch D.C.; RT "Complete amino acid sequence of azotoflavin, a flavodoxin from RT Azotobacter vinelandii."; RL Biochemistry 16:3525-3537(1977). RN [4] RP PROTEIN SEQUENCE OF 2-21, AND MASS SPECTROMETRY. RC STRAIN=OP / UW136; RX MEDLINE=96276406; PubMed=8694750; RA Gangeswaran R., Eady R.R.; RT "Flavodoxin 1 of Azotobacter vinelandii: characterization and role in RT electron donation to purified assimilatory nitrate reductase."; RL Biochem. J. 317:103-108(1996). RN [5] RP STRUCTURE BY NMR. RC STRAIN=ATCC 478 / NRS 16 / DSM 2289 / VKM B-1617; RX MEDLINE=98180401; PubMed=9521106; RA Steensma E., Nijman M.J.M., Bollen Y.J.M., de Jager P.A., RA van den Berg W.A.M., van Dongen W.M.A.M., van Mierlo C.P.M.; RT "Apparent local stability of the secondary structure of Azotobacter RT vinelandii holoflavodoxin II as probed by hydrogen exchange: RT implications for redox potential regulation and flavodoxin folding."; RL Protein Sci. 7:306-317(1998). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. NifF is the electron donor to nitrogenase. CC -!- COFACTOR: FMN. CC -!- SUBUNIT: Monomer. CC -!- MASS SPECTROMETRY: MW=19533; MW_ERR=5; METHOD=Electrospray; CC RANGE=2-180; NOTE=Ref.4. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M20568; AAA64735.1; -; Genomic_DNA. DR EMBL; J03519; AAA22154.1; -; Genomic_DNA. DR PIR; A29935; FXAVEP. DR PDB; 1YOB; X-ray; A/B=1-180. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW 3D-structure; Direct protein sequencing; Electron transport; KW Flavoprotein; FMN; Nitrogen fixation; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 180 Flavodoxin-2. FT /FTId=PRO_0000171605. FT DOMAIN 4 173 Flavodoxin-like. FT STRAND 3 7 FT STRAND 10 12 FT HELIX 13 22 FT TURN 27 29 FT HELIX 36 38 FT HELIX 41 45 FT STRAND 48 55 FT TURN 58 60 FT HELIX 65 67 FT HELIX 74 81 FT STRAND 90 96 FT TURN 99 101 FT TURN 103 107 FT HELIX 108 118 FT TURN 119 121 FT STRAND 123 125 FT STRAND 141 151 FT TURN 153 155 FT HELIX 157 159 FT HELIX 160 171 FT HELIX 172 175 SQ SEQUENCE 180 AA; 19663 MW; 8B1B43F23AB5E8B4 CRC64; MAKIGLFFGS NTGKTRKVAK SIKKRFDDET MSDALNVNRV SAEDFAQYQF LILGTPTLGE GELPGLSSDC ENESWEEFLP KIEGLDFSGK TVALFGLGDQ VGYPENYLDA LGELYSFFKD RGAKIVGSWS TDGYEFESSE AVVDGKFVGL ALDLDNQSGK TDERVAAWLA QIAPEFGLSL // ID FLAV_BACSU Reviewed; 158 AA. AC O34737; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 31-OCT-2006, entry version 48. DE Probable flavodoxin-1. GN Name=ykuN; OrderedLocusNames=BSU14150; OS Bacillus subtilis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1423; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=168; RA Scanlan E., Devine K.M.; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=168; RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786; RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M., RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., RA Yoshikawa H., Danchin A.; RT "The complete genome sequence of the Gram-positive bacterium Bacillus RT subtilis."; RL Nature 390:249-256(1997). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes (Potential). CC -!- COFACTOR: FMN (By similarity). CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ222587; CAA10877.1; -; Genomic_DNA. DR EMBL; Z99111; CAB13288.1; -; Genomic_DNA. DR PIR; C69866; C69866. DR HSSP; P00323; 1J9E. DR GenomeReviews; AL009126_GR; BSU14150. DR KEGG; bsu:BG13298; -. DR SubtiList; BG13298; ykuN. DR BioCyc; BSUB1423:BSU1417-MONOMER; -. DR InterPro; IPR010087; Flav_short. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR TIGRFAMs; TIGR01753; flav_short; 1. DR PROSITE; PS00201; FLAVODOXIN; FALSE_NEG. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Complete proteome; Electron transport; Flavoprotein; FMN; Transport. FT CHAIN 1 158 Probable flavodoxin-1. FT /FTId=PRO_0000171607. FT DOMAIN 4 144 Flavodoxin-like. SQ SEQUENCE 158 AA; 17793 MW; FECE71BF6E552D3F CRC64; MAKALITYAS MSGNTEDIAF IIKDTLQEYE LDIDCVEIND MDASCLTSYD YVLIGTYTWG DGDLPYEAED FFEEVKQIQL NGLKTACFGS GDYSYPKFCE AVNLFNVMLQ EAGAAVYQET LKIELAPETD EDVESCRAFA RGFLAWADYM NKEKIHVS // ID FLAV_CHOCR Reviewed; 173 AA. AC P14070; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 20-MAR-2007, entry version 53. DE Flavodoxin. OS Chondrus crispus (Carragheen). OC Eukaryota; Rhodophyta; Florideophyceae; Gigartinales; Gigartinaceae; OC Chondrus. OX NCBI_TaxID=2769; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=90088453; PubMed=2597140; RA Wakabayashi S., Kimura K., Matsubara H., Rogers L.J.; RT "The amino acid sequence of a flavodoxin from the eukaryotic red alga RT Chondrus crispus."; RL Biochem. J. 263:981-984(1989). RN [2] RP PROTEIN SEQUENCE OF 1-34. RA Takruri I.A.H., Boulter D., Fitzgerald M.P., Hutber G.N., Rogers L.J.; RT "N-terminal amino acid sequences of flavodoxins from Chondrus crispus RT and Nostoc strain MAC."; RL Phytochemistry 25:2113-2115(1986). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS). RX MEDLINE=90368796; PubMed=2394748; RA Fukuyama K., Wakabayashi S., Matsubara H., Rogers L.J.; RT "Tertiary structure of oxidized flavodoxin from an eukaryotic red alga RT Chondrus crispus at 2.35-A resolution. Localization of charged RT residues and implication for interaction with electron transfer RT partners."; RL J. Biol. Chem. 265:15804-15812(1990). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX MEDLINE=92292160; PubMed=1602481; DOI=10.1016/0022-2836(92)90400-E; RA Fukuyama K., Matsubara H., Rogers L.J.; RT "Crystal structure of oxidized flavodoxin from a red alga Chondrus RT crispus refined at 1.8-A resolution. Description of the flavin RT mononucleotide binding site."; RL J. Mol. Biol. 225:775-789(1992). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. CC -!- COFACTOR: FMN. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; S06648; S06648. DR PDB; 2FCR; X-ray; @=1-173. DR LinkHub; P14070; -. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW 3D-structure; Direct protein sequencing; Electron transport; KW Flavoprotein; FMN; Transport. FT CHAIN 1 173 Flavodoxin. FT /FTId=PRO_0000171612. FT DOMAIN 2 168 Flavodoxin-like. FT CONFLICT 29 29 D -> S (in Ref. 2). FT CONFLICT 33 33 D -> S (in Ref. 2). FT STRAND 2 6 FT STRAND 9 11 FT HELIX 12 24 FT HELIX 25 27 FT HELIX 34 36 FT HELIX 40 45 FT STRAND 47 54 FT HELIX 69 75 FT HELIX 77 79 FT STRAND 86 93 FT TURN 95 97 FT TURN 102 104 FT HELIX 105 115 FT STRAND 119 121 FT HELIX 126 128 FT STRAND 141 148 FT TURN 149 151 FT HELIX 156 171 SQ SEQUENCE 173 AA; 18871 MW; EF1F3A3554CA4166 CRC64; KIGIFFSTST GNTTEVADFI GKTLGAKADA PIDVDDVTDP QALKDYDLLF LGAPTWNTGA DTERSGTSWD EFLYDKLPEV DMKDLPVAIF GLGDAEGYPD NFCDAIEEIH DCFAKQGAKP VGFSNPDDYD YEESKSVRDG KFLGLPLDMV NDQIPMEKRV AGWVEAVVSE TGV // ID FLAV_CLOSA Reviewed; 160 AA. AC P18855; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 31-OCT-2006, entry version 39. DE Flavodoxin. GN Name=floX; OS Clostridium saccharobutylicum. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=169679; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91123180; PubMed=1991710; RA Santangelo J.D., Jones D.T., Woods D.R.; RT "Metronidazole activation and isolation of Clostridium acetobutylicum RT electron transport genes."; RL J. Bacteriol. 173:1088-1095(1991). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. CC -!- COFACTOR: FMN. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC -!- CAUTION: Was originally thought to originate from CC C.acetobutylicum. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M36770; AAA23238.1; -; Genomic_DNA. DR HSSP; P00322; 2FVX. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Electron transport; Flavoprotein; FMN; Transport. FT CHAIN 1 160 Flavodoxin. FT /FTId=PRO_0000171614. FT DOMAIN 3 153 Flavodoxin-like. SQ SEQUENCE 160 AA; 17763 MW; 6153F8A1F0BCDC8D CRC64; MKISILYSSK TGKTERVAKL IEEGVKRSGN IEVKTMNLDA VDKKFLQESE GIIFGTPTYY ANISWEMKKW IDESSEFNLE GKLGAAFSTA NSIAGGSDIA LLTILNHLMV KGMLVYSGGV AFGKPKTHLG YVHINEIQEN EDENARIFGE RIANKVKQIF // ID FLAV_CLOBE Reviewed; 138 AA. AC P00322; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 20-MAR-2007, entry version 58. DE Flavodoxin. OS Clostridium beijerinckii (Clostridium MP). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1520; RN [1] RP PROTEIN SEQUENCE. RX MEDLINE=74277392; PubMed=4843142; RA Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G.; RT "The amino acid sequence of the Clostridium MP flavodoxin."; RL J. Biol. Chem. 249:4393-4396(1974). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF OXIDIZED FORM. RX MEDLINE=74277391; PubMed=4843141; RA Burnett R.M., Darling G.D., Kendall D.S., Lequesne M.E., Mayhew S.G., RA Smith W.W., Ludwig M.L.; RT "The structure of the oxidized form of clostridial flavodoxin at 1.9-A RT resolution."; RL J. Biol. Chem. 249:4383-4392(1974). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX MEDLINE=97178811; PubMed=9063874; DOI=10.1021/bi962180o; RA Ludwig M.L., Pattridge K.A., Metzger A.L., Dixon M.M., Eren M., RA Feng Y., Swenson R.P.; RT "Control of oxidation-reduction potentials in flavodoxin from RT Clostridium beijerinckii: the role of conformation changes."; RL Biochemistry 36:1259-1280(1997). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. CC -!- COFACTOR: FMN. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PDB; 1FLA; X-ray; @=1-138. DR PDB; 1FLD; X-ray; @=1-138. DR PDB; 1FLN; X-ray; @=1-138. DR PDB; 1FVX; X-ray; @=1-138. DR PDB; 2FAX; X-ray; @=1-138. DR PDB; 2FDX; X-ray; @=1-138. DR PDB; 2FLV; X-ray; @=1-138. DR PDB; 2FOX; X-ray; @=1-138. DR PDB; 2FVX; X-ray; @=1-138. DR PDB; 3NLL; X-ray; @=1-138. DR PDB; 4NLL; X-ray; @=1-138. DR PDB; 4NUL; X-ray; @=1-138. DR PDB; 5NLL; X-ray; @=1-138. DR PDB; 5NUL; X-ray; @=1-138. DR PDB; 5ULL; X-ray; @=1-138. DR PDB; 6NUL; X-ray; @=1-138. DR LinkHub; P00322; -. DR InterPro; IPR010087; Flav_short. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR TIGRFAMs; TIGR01753; flav_short; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW 3D-structure; Direct protein sequencing; Electron transport; KW Flavoprotein; FMN; Transport. FT CHAIN 1 138 Flavodoxin. FT /FTId=PRO_0000171613. FT DOMAIN 1 136 Flavodoxin-like. FT STRAND 2 6 FT STRAND 8 10 FT HELIX 11 25 FT STRAND 31 34 FT HELIX 35 37 FT HELIX 40 43 FT STRAND 47 53 FT TURN 57 59 FT TURN 63 65 FT HELIX 66 73 FT HELIX 74 76 FT STRAND 81 93 FT HELIX 94 105 FT STRAND 115 120 FT HELIX 122 124 FT HELIX 125 136 SQ SEQUENCE 138 AA; 15332 MW; 98BE3746EC000FF1 CRC64; MKIVYWSGTG NTEKMAELIA KGIIESGKDV NTINVSDVNI DELLNEDILI LGCSAMGDEV LEESEFEPFI EEISTKISGK KVALFGSYGW GDGKWMRDFE ERMNGYGCVV VETPLIVQNE PDEAEQDCIE FGKKIANI // ID FLAV_DESDE Reviewed; 148 AA. AC P26492; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 31-OCT-2006, entry version 37. DE Flavodoxin. OS Desulfovibrio desulfuricans. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=876; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ATCC 29577 / CIP 107039 / LMG 7529 / NCIB 8307 / VKM B-1799; RX MEDLINE=91316149; PubMed=1859847; DOI=10.1016/0167-4781(91)90190-W; RA Helms L.R., Swenson R.P.; RT "Cloning and characterization of the flavodoxin gene from RT Desulfovibrio desulfuricans."; RL Biochim. Biophys. Acta 1089:417-419(1991). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. CC -!- COFACTOR: FMN. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X59438; CAA42064.1; -; mRNA. DR PIR; S17000; FXDVD. DR HSSP; P00323; 1BU5. DR InterPro; IPR010087; Flav_short. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR TIGRFAMs; TIGR01753; flav_short; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Electron transport; Flavoprotein; FMN; Transport. FT CHAIN 1 148 Flavodoxin. FT /FTId=PRO_0000171615. FT DOMAIN 4 145 Flavodoxin-like. SQ SEQUENCE 148 AA; 15694 MW; 1CE35B4B79817459 CRC64; MSKVLIVFGS STGNTESIAQ KLEELIAAGG HEVTLLNAAD ASAENLADGY DAVLFGCSAW GMEDLEMQDD FLSLFEEFNR IGLAGRKVAA FASGDQEYEH FCGAVPAIEE RAKELGATII AEGLKMEGDA SNDPEAVASF AEDVLKQL // ID FLAV_DESGI Reviewed; 146 AA. AC Q01095; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 31-OCT-2006, entry version 38. DE Flavodoxin. OS Desulfovibrio gigas. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=879; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759; RX MEDLINE=92329549; PubMed=1627649; DOI=10.1016/0167-4781(92)90034-W; RA Helms L.R., Swenson R.P.; RT "The primary structures of the flavodoxins from two strains of RT Desulfovibrio gigas. Cloning and nucleotide sequence of the structural RT genes."; RL Biochim. Biophys. Acta 1131:325-328(1992). CC -!- FUNCTION: Electron-transfer proteins that function in various CC electron transport systems in micro-organisms. Functionally CC interchangeable with ferredoxin. CC -!- COFACTOR: FMN. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X64766; CAA46013.1; -; Genomic_DNA. DR PIR; S24311; S24311. DR HSSP; P00323; 1BU5. DR InterPro; IPR010087; Flav_short. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR TIGRFAMs; TIGR01753; flav_short; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Electron transport; Flavoprotein; FMN; Transport. FT CHAIN 1 146 Flavodoxin. FT /FTId=PRO_0000171617. FT DOMAIN 4 143 Flavodoxin-like. SQ SEQUENCE 146 AA; 15470 MW; 95D9E73B1FCF1403 CRC64; MPKALIVYGS TTGNTEGVAE AIAKTLNSEG METTVVNVAD VTAPGLAEGY DVVLLGCSTW GDDEIELQED FVPLYEDLDR AGLKDKKVGV FGCGDSSYTY FCGAVDVIEK KAEELGATLV ASSLKIDGEP DSAEVLDWAR EVLARV // ID FLAV_DESSA Reviewed; 146 AA. AC P18086; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 20-MAR-2007, entry version 39. DE Flavodoxin. OS Desulfovibrio salexigens. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=880; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 14822 / DSM 2638 / NCIB 8403 / VKM B-1763; RX MEDLINE=90241257; PubMed=2334437; DOI=10.1016/0006-291X(90)92393-E; RA Helms L.R., Krey G.D., Swenson R.P.; RT "Identification, sequence determination, and expression of the RT flavodoxin gene from Desulfovibrio salexigens."; RL Biochem. Biophys. Res. Commun. 168:809-817(1990). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. CC -!- COFACTOR: FMN. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M35475; AAA23368.1; -; Genomic_DNA. DR PIR; A34640; A34640. DR HSSP; P00323; 1FX1. DR InterPro; IPR010087; Flav_short. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR TIGRFAMs; TIGR01753; flav_short; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Electron transport; Flavoprotein; FMN; Transport. FT CHAIN 1 146 Flavodoxin. FT /FTId=PRO_0000171619. FT DOMAIN 4 143 Flavodoxin-like. SQ SEQUENCE 146 AA; 15812 MW; BDE3651310E1F780 CRC64; MSKSLIVYGS TTGNTETAAE YVAEAFENKE IDVELKNVTD VSVADLGNGY DIVLFGCSTW GEEEIELQDD FIPLYDSLEN ADLKGKKVSV FGCGDSDYTY FCGAVDAIEE KLEKMGAVVI GDSLKIDGDP ERDEIVSWGS GIADKI // ID FLAV_DESVH Reviewed; 148 AA. AC P00323; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 2. DT 20-MAR-2007, entry version 66. DE Flavodoxin. GN OrderedLocusNames=DVU_2680; OS Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB OS 8303). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=882; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89008444; PubMed=3170590; RA Krey G.D., Vanin E.F., Swenson R.P.; RT "Cloning, nucleotide sequence, and expression of the flavodoxin gene RT from Desulfovibrio vulgaris (Hildenborough)."; RL J. Biol. Chem. 263:15436-15443(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Curley G.P., Voordouw G.; RT "Cloning and sequencing of the gene encoding flavodoxin from RT Desulfovibrio vulgaris Hildenborough."; RL FEMS Microbiol. Lett. 49:295-299(1988). RN [3] RP PROTEIN SEQUENCE. RX MEDLINE=77118626; PubMed=402366; RA Dubourdieu M., Fox J.L.; RT "Amino acid sequence of Desulfovibrio vulgaris flavodoxin."; RL J. Biol. Chem. 252:1453-1463(1977). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15077118; DOI=10.1038/nbt959; RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J., RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., RA Dimitrov G., Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., RA Feldblyum T.V., Wall J.D., Voordouw G., Fraser C.M.; RT "The genome sequence of the anaerobic, sulfate-reducing bacterium RT Desulfovibrio vulgaris Hildenborough."; RL Nat. Biotechnol. 22:554-559(2004). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=91162643; PubMed=2002503; DOI=10.1016/0022-2836(91)90884-9; RA Warr W., Tulinsky A., Swenson R.P., Watenpaugh K.D.; RT "Comparison of the crystal structures of a flavodoxin in its three RT oxidation states at cryogenic temperatures."; RL J. Mol. Biol. 218:195-208(1991). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE=74087652; PubMed=4521211; RA Watenpaugh K.D., Sieker L.C., Jensen L.H.; RT "The binding of riboflavin-5'-phosphate in a flavoprotein: flavodoxin RT at 2.0-A resolution."; RL Proc. Natl. Acad. Sci. U.S.A. 70:3857-3860(1973). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX MEDLINE=73044810; PubMed=4508313; RA Watenpaugh K.D., Sieker L.C., Jensen L.H., Legall J., Dubourdieu M.; RT "Structure of the oxidized form of a flavodoxin at 2.5-A resolution: RT resolution of the phase ambiguity by anomalous scattering."; RL Proc. Natl. Acad. Sci. U.S.A. 69:3185-3188(1972). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX MEDLINE=99089597; PubMed=9874201; RA Walsh M.A., McCarthy A., O'Farrell P.A., McArdle P., Cunningham P.D., RA Mayhew S.G., Higgins T.M.; RT "X-ray crystal structure of the Desulfovibrio vulgaris (Hildenborough) RT apoflavodoxin-riboflavin complex."; RL Eur. J. Biochem. 258:362-371(1998). RN [9] RP STRUCTURE BY NMR. RX MEDLINE=93238683; PubMed=8477691; RA Knauf M.A., Loehr F., Curley G.P., O'Farrell P., Mayhew S.G., RA Mueller F., Rueterjans H.; RT "Homonuclear and heteronuclear NMR studies of oxidized Desulfovibrio RT vulgaris flavodoxin. Sequential assignments and identification of RT secondary structure elements."; RL Eur. J. Biochem. 213:167-184(1993). RN [10] RP STRUCTURE BY NMR. RX MEDLINE=96283837; PubMed=8681954; RA Knauf M.A., Loehr F., Bluemel M., Mayhew S.G., Rueterjans H.; RT "NMR investigation of the solution conformation of oxidized flavodoxin RT from Desulfovibrio vulgaris. Determination of the tertiary structure RT and detection of protein-bound water molecules."; RL Eur. J. Biochem. 238:423-434(1996). RN [11] RP STRUCTURE BY NMR. RX MEDLINE=93237739; PubMed=8477184; RA Stockman B.J., Euvrard A., Kloosterman D.A., Scahill T.A., RA Swenson R.P.; RT "1H and 15N resonance assignments and solution secondary structure of RT oxidized Desulfovibrio vulgaris flavodoxin determined by heteronuclear RT three-dimensional NMR spectroscopy."; RL J. Biomol. NMR 3:133-149(1993). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. CC -!- COFACTOR: FMN. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J04033; AAA23367.1; -; Genomic_DNA. DR EMBL; AE017285; AAS97152.1; -; Genomic_DNA. DR PIR; A31991; FXDV. DR PDB; 1AKQ; X-ray; @=2-148. DR PDB; 1AKR; X-ray; @=2-148. DR PDB; 1AKT; X-ray; @=2-148. DR PDB; 1AKU; X-ray; @=2-148. DR PDB; 1AKV; X-ray; @=2-148. DR PDB; 1AKW; X-ray; @=2-148. DR PDB; 1AZL; X-ray; @=2-148. DR PDB; 1BU5; X-ray; A=2-148. DR PDB; 1C7E; X-ray; A/B=2-148. DR PDB; 1C7F; X-ray; A/B=2-148. DR PDB; 1F4P; X-ray; A=2-148. DR PDB; 1FX1; X-ray; @=1-148. DR PDB; 1I1O; X-ray; A=3-148. DR PDB; 1J8Q; X-ray; A=3-148. DR PDB; 1J9E; X-ray; A=3-148. DR PDB; 1J9G; X-ray; A=3-148. DR PDB; 1WSB; X-ray; A=1-148. DR PDB; 1WSW; X-ray; A=1-148. DR PDB; 1XT6; X-ray; A=3-148. DR PDB; 1XYV; X-ray; A=1-148. DR PDB; 1XYY; X-ray; A=1-148. DR PDB; 2FX2; X-ray; @=3-148. DR PDB; 3FX2; X-ray; @=3-148. DR PDB; 4FX2; X-ray; @=3-148. DR PDB; 5FX2; X-ray; @=3-148. DR GenomeReviews; AE017285_GR; DVU_2680. DR KEGG; dvu:DVU2680; -. DR TIGR; DVU_2680; -. DR BioCyc; DVUL882:DVU2680-MONOMER; -. DR LinkHub; P00323; -. DR InterPro; IPR010087; Flav_short. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR TIGRFAMs; TIGR01753; flav_short; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW 3D-structure; Complete proteome; Direct protein sequencing; KW Electron transport; Flavoprotein; FMN; Transport. FT CHAIN 1 148 Flavodoxin. FT /FTId=PRO_0000171620. FT DOMAIN 4 145 Flavodoxin-like. FT CONFLICT 28 28 D -> N (in Ref. 2). FT STRAND 3 9 FT STRAND 11 13 FT HELIX 14 29 FT STRAND 32 37 FT HELIX 38 40 FT TURN 44 49 FT STRAND 51 57 FT STRAND 62 64 FT TURN 69 71 FT HELIX 72 76 FT HELIX 78 80 FT STRAND 87 94 FT STRAND 98 100 FT HELIX 103 114 FT STRAND 124 128 FT HELIX 130 133 FT HELIX 134 145 SQ SEQUENCE 148 AA; 15823 MW; E07630E7047ABD3F CRC64; MPKALIVYGS TTGNTEYTAE TIARELADAG YEVDSRDAAS VEAGGLFEGF DLVLLGCSTW GDDSIELQDD FIPLFDSLEE TGAQGRKVAC FGCGDSSYEY FCGAVDAIEE KLKNLGAEIV QDGLRIDGDP RAARDDIVGW AHDVRGAI // ID FLAV_DESVM Reviewed; 148 AA. AC P71165; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 31-OCT-2006, entry version 35. DE Flavodoxin. OS Desulfovibrio vulgaris (strain Miyazaki). OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=883; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RC STRAIN=Isolate F; RX MEDLINE=98230696; PubMed=9562622; RA Kitamura M., Sagara T., Taniguchi M., Ashida M., Ezoe K., Kohno K., RA Kojima S., Ozawa K., Akutsu H., Kumagai I., Nakaya T.; RT "Cloning and expression of the gene encoding flavodoxin from RT Desulfovibrio vulgaris (Miyazaki F)."; RL J. Biochem. 123:891-898(1998). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. CC -!- COFACTOR: FMN. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D88493; BAA13628.1; -; Genomic_DNA. DR HSSP; P00323; 1J9E. DR InterPro; IPR010087; Flav_short. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR TIGRFAMs; TIGR01753; flav_short; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Electron transport; Flavoprotein; FMN; Transport. FT CHAIN 1 148 Flavodoxin. FT /FTId=PRO_0000171621. FT DOMAIN 4 145 Flavodoxin-like. SQ SEQUENCE 148 AA; 15656 MW; 9D321268D04D89B4 CRC64; MANVLIVYGS TTGNTAWVAE TVGRDIAEAG HSVEIRDAGQ VEAEGLCEGR DLVLFGCSTW GDDEIELQDD FIHLYESLEA TGAGKGRAAC FGCGDSSYTY FCGPVDAIEE RLSGLGADIV ADSLKIDGDP RTMRDDVSAW AGRVVTAL // ID FLAV_ECO57 Reviewed; 176 AA. AC P61951; P23243; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 21. DE Flavodoxin-1. GN Name=fldA; OrderedLocusNames=Z0832, ECs0715; OS Escherichia coli O157:H7. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83334; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC; RX MEDLINE=21074935; PubMed=11206551; DOI=10.1038/35054089; RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., RA Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., RA Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., RA Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K., RA Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., RA Welch R.A., Blattner F.R.; RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."; RL Nature 409:529-533(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC; RX MEDLINE=21156231; PubMed=11258796; DOI=10.1093/dnares/8.1.11; RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., RA Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., RA Kuhara S., Shiba T., Hattori M., Shinagawa H.; RT "Complete genome sequence of enterohemorrhagic Escherichia coli RT O157:H7 and genomic comparison with a laboratory strain K-12."; RL DNA Res. 8:11-22(2001). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes (Potential). Involved in the reactivation of inactive CC cob(II)alamin in methionine synthase (By similarity). CC -!- COFACTOR: FMN (By similarity). CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE005174; AAG55007.1; -; Genomic_DNA. DR EMBL; BA000007; BAB34138.1; -; Genomic_DNA. DR PIR; C85568; C85568. DR PIR; C90718; C90718. DR SMR; P61951; 2-176. DR GenomeReviews; BA000007_GR; ECs0715. DR GenomeReviews; AE005174_GR; Z0832. DR KEGG; ece:Z0832; -. DR KEGG; ecs:ECs0715; -. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Complete proteome; Electron transport; Flavoprotein; FMN; Transport. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 176 Flavodoxin-1. FT /FTId=PRO_0000171624. FT DOMAIN 4 165 Flavodoxin-like. SQ SEQUENCE 176 AA; 19737 MW; 8878DA1A8EAA55BD CRC64; MAITGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAYDIL LLGIPTWYYG EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTAERVEKW VKQISEELHL DEILNA // ID FLAV_ECOL6 Reviewed; 176 AA. AC P61950; P23243; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 21. DE Flavodoxin-1. GN Name=fldA; OrderedLocusNames=c_0771; OS Escherichia coli O6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=217992; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC; RX MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799; RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.; RT "Extensive mosaic structure revealed by the complete genome sequence RT of uropathogenic Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes (Potential). Involved in the reactivation of inactive CC cob(II)alamin in methionine synthase (By similarity). CC -!- COFACTOR: FMN (By similarity). CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE014075; AAN79244.1; ALT_INIT; Genomic_DNA. DR SMR; P61950; 2-176. DR GenomeReviews; AE014075_GR; c_0771. DR KEGG; ecc:c0771; -. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Complete proteome; Electron transport; Flavoprotein; FMN; Transport. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 176 Flavodoxin-1. FT /FTId=PRO_0000171623. FT DOMAIN 4 165 Flavodoxin-like. SQ SEQUENCE 176 AA; 19737 MW; 8878DA1A8EAA55BD CRC64; MAITGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAYDIL LLGIPTWYYG EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTAERVEKW VKQISEELHL DEILNA // ID FLAV_ECOLI Reviewed; 176 AA. AC P61949; P23243; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 20-MAR-2007, entry version 39. DE Flavodoxin-1. GN Name=fldA; OrderedLocusNames=b0684, JW0671; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-15. RX MEDLINE=91154129; PubMed=1999390; RA Osborne C., Chen L.-M., Matthews R.G.; RT "Isolation, cloning, mapping, and nucleotide sequencing of the gene RT encoding flavodoxin in Escherichia coli."; RL J. Bacteriol. 173:1729-1737(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX MEDLINE=97061202; PubMed=8905232; DOI=10.1093/dnares/3.3.137; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., RA Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., RA Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., RA Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., RA Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., RA Yano M., Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP PROTEIN SEQUENCE OF 2-11. RX MEDLINE=95050480; PubMed=7961651; RA Jenkins C.M., Waterman M.R.; RT "Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli RT support bovine cytochrome P450c17 hydroxylase activities."; RL J. Biol. Chem. 269:27401-27408(1994). RN [6] RP FUNCTION IN COBALT REDUCTION OF COB(II)ALAMIN. RX PubMed=9730838; DOI=10.1021/bi9808565; RA Jarrett J.T., Hoover D.M., Ludwig M.L., Matthews R.G.; RT "The mechanism of adenosylmethionine-dependent activation of RT methionine synthase: a rapid kinetic analysis of intermediates in RT reductive methylation of Cob(II)alamin enzyme."; RL Biochemistry 37:12649-12658(1998). RN [7] RP STRUCTURE BY NMR. RX MEDLINE=97234567; PubMed=9119004; RA Ponstingl H., Otting G.; RT "NMR assignments, secondary structure and hydration of oxidized RT Escherichia coli flavodoxin."; RL Eur. J. Biochem. 244:384-399(1997). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX MEDLINE=98078562; PubMed=9416602; RA Hoover D.M., Ludwig M.L.; RT "A flavodoxin that is required for enzyme activation: the structure of RT oxidized flavodoxin from Escherichia coli at 1.8-A resolution."; RL Protein Sci. 6:2525-2537(1997). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes (Potential). Involved in the reactivation of inactive CC cob(II)alamin in methionine synthase. CC -!- COFACTOR: FMN. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M59426; AAA23789.1; -; Genomic_DNA. DR EMBL; U00096; AAC73778.1; -; Genomic_DNA. DR EMBL; AP009048; BAA35333.1; -; Genomic_DNA. DR PIR; A37319; A37319. DR PDB; 1AG9; X-ray; A/B=1-176. DR PDB; 1AHN; X-ray; @=1-176. DR IntAct; P61949; -. DR ECO2DBASE; A019.0; 6TH EDITION. DR GenomeReviews; U00096_GR; b0684. DR GenomeReviews; AP009048_GR; JW0671. DR KEGG; ecj:JW0671; -. DR KEGG; eco:b0684; -. DR EchoBASE; EB0314; -. DR EcoGene; EG10318; fldA. DR BioCyc; EcoCyc:FLAVODOXIN1-MONOMER; -. DR LinkHub; P61949; -. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW 3D-structure; Complete proteome; Direct protein sequencing; KW Electron transport; Flavoprotein; FMN; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 176 Flavodoxin-1. FT /FTId=PRO_0000171622. FT DOMAIN 4 165 Flavodoxin-like. FT STRAND 3 7 FT STRAND 10 12 FT HELIX 13 25 FT TURN 27 29 FT STRAND 30 34 FT HELIX 35 37 FT HELIX 40 44 FT STRAND 47 52 FT TURN 57 59 FT HELIX 63 72 FT STRAND 81 87 FT TURN 90 95 FT HELIX 99 108 FT TURN 109 112 FT STRAND 132 134 FT STRAND 137 143 FT TURN 145 147 FT TURN 149 151 FT HELIX 152 167 FT HELIX 169 172 SQ SEQUENCE 176 AA; 19737 MW; 8878DA1A8EAA55BD CRC64; MAITGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAYDIL LLGIPTWYYG EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTAERVEKW VKQISEELHL DEILNA // ID FLAV_ENTAG Reviewed; 177 AA. AC P28579; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 31-OCT-2006, entry version 40. DE Flavodoxin. GN Name=nifF; OS Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans). OG Plasmid pEA3. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Pantoea. OX NCBI_TaxID=549; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=333; RX MEDLINE=91217003; PubMed=1708766; RA Kreutzer R., Dayananda S., Klingmueller W.; RT "Cotranscription of the electron transport protein genes nifJ and nifF RT in Enterobacter agglomerans 333."; RL J. Bacteriol. 173:3252-3256(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21. RC STRAIN=333; RA Schwickerath O.; RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. NifF is the electron donor to nitrogenase. CC -!- COFACTOR: FMN. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M38221; AAA23385.1; -; Genomic_DNA. DR EMBL; X99694; CAA68010.1; -; Genomic_DNA. DR EMBL; X78558; CAA55301.1; -; Genomic_DNA. DR PIR; A39414; A39414. DR HSSP; P10340; 1D03. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Electron transport; Flavoprotein; FMN; Nitrogen fixation; Plasmid; KW Transport. FT CHAIN 1 177 Flavodoxin. FT /FTId=PRO_0000171631. FT DOMAIN 4 173 Flavodoxin-like. SQ SEQUENCE 177 AA; 19581 MW; 3D54F95F7EC60B41 CRC64; MATIGIFFGS DTGQTRKVAK LIHQKLDGIA DAPLDVRRAT REQFLSYPVL LLGTPTLGDG ELPGVEAGSQ YDSWQEFTNT LSEADLTGKT VALFGLGDQL NYSKNFVSAM RILYDLVIAR GACVVGNWPR EGYKFSFSAA LLENNEFVGL PLDQENQYDL TEERIDSWLE KLKPAVL // ID FLAV_HAEIN Reviewed; 174 AA. AC P44562; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 50. DE Flavodoxin. GN Name=fldA; OrderedLocusNames=HI0191; OS Haemophilus influenzae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=727; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX MEDLINE=95350630; PubMed=7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., RA Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes (By similarity). CC -!- COFACTOR: FMN (By similarity). CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42023; AAC21860.1; -; Genomic_DNA. DR PIR; C64053; C64053. DR HSSP; P23243; 1AHN. DR SMR; P44562; 2-173. DR GenomeReviews; L42023_GR; HI0191. DR KEGG; hin:HI0191; -. DR TIGR; HI0191; -. DR BioCyc; HINF71421:HI0191-MONOMER; -. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Complete proteome; Electron transport; Flavoprotein; FMN; Transport. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 174 Flavodoxin. FT /FTId=PRO_0000171633. FT DOMAIN 4 165 Flavodoxin-like. SQ SEQUENCE 174 AA; 19627 MW; 5E95E895F04BF3F8 CRC64; MAIVGLFYGS DTGNTENIAK QIQKQLGSDL IDIRDIAKSS KEDIEAYDFL LFGIPTWYYG EAQADWDDFF PTLEEIDFTD KLVGIFGCGD QEDYADYFCD AIGTVRDIIE PHGAIVVGNW PTEGYNFEAS KALLEDGTFI GLCIDEDRQP ELTAERVEKW CKQIYDEMCL AELA // ID FLAV_HELPY Reviewed; 164 AA. AC O25776; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 20-MAR-2007, entry version 46. DE Flavodoxin. GN Name=fldA; OrderedLocusNames=HP_1161; OS Helicobacter pylori (Campylobacter pylori). OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=210; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX MEDLINE=97394467; PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., RA Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., RA Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., RA Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., RA Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., RA Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., RA Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., RA Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes (By similarity). CC -!- COFACTOR: FMN (By similarity). CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000511; AAD08207.1; -; Genomic_DNA. DR PIR; A64665; A64665. DR PDB; 2BMV; X-ray; A=1-164. DR GenomeReviews; AE000511_GR; HP_1161. DR KEGG; hpy:HP1161; -. DR TIGR; HP_1161; -. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; FALSE_NEG. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW 3D-structure; Complete proteome; Electron transport; Flavoprotein; KW FMN; Transport. FT CHAIN 1 164 Flavodoxin. FT /FTId=PRO_0000171634. FT DOMAIN 4 160 Flavodoxin-like. FT STRAND 4 8 FT STRAND 11 13 FT HELIX 14 26 FT STRAND 28 33 FT HELIX 34 36 FT HELIX 39 42 FT STRAND 46 55 FT TURN 56 58 FT HELIX 62 68 FT HELIX 74 77 FT STRAND 79 86 FT TURN 89 91 FT TURN 96 98 FT HELIX 99 107 FT STRAND 110 112 FT STRAND 116 118 FT STRAND 133 139 FT TURN 141 143 FT HELIX 145 147 FT HELIX 148 159 FT TURN 160 162 SQ SEQUENCE 164 AA; 17492 MW; EBAD44D97964608C CRC64; MGKIGIFFGT DSGNAEAIAE KISKAIGNAE VVDVAKASKE QFNSFTKVIL VAPTAGAGDL QTDWEDFLGT LEASDFATKT IGLVGLGDQD TYSETFAEGI FHIYEKAKAG KVVGQTPTDG YHFEASKAVE GGKFVGLVID EDNQDDLTDE RISKWVEQVK GSFA // ID FLAV_KLEPN Reviewed; 176 AA. AC O07026; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 31-OCT-2006, entry version 35. DE Flavodoxin. GN Name=fldA; OS Klebsiella pneumoniae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Klebsiella. OX NCBI_TaxID=573; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION. RC STRAIN=ATCC 13883 / DSM 30104 / IFO 14940 / NCIMB 13281 / NCTC 9633; RX MEDLINE=97417492; PubMed=9272865; DOI=10.1016/S0378-1119(97)00168-6; RA Achenbach L.A., Genova E.G.; RT "Transcriptional regulation of a second flavodoxin gene from RT Klebsiella pneumoniae."; RL Gene 194:235-240(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-176. RC STRAIN=ATCC 13883 / DSM 30104 / IFO 14940 / NCIMB 13281 / NCTC 9633; RX MEDLINE=97208874; PubMed=9055816; DOI=10.1016/S0378-1119(96)00642-7; RA Achenbach L.A., Yang W.; RT "The fur gene from Klebsiella pneumoniae: characterization, genomic RT organization and phylogenetic analysis."; RL Gene 185:201-207(1997). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes (By similarity). CC -!- COFACTOR: FMN (By similarity). CC -!- INDUCTION: By low iron conditions and by heat shock. Iron CC regulation is mediated through the fur protein. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U67169; AAB65080.1; -; Genomic_DNA. DR EMBL; L23871; AAB51076.1; -; Genomic_DNA. DR HSSP; P23243; 1AHN. DR SMR; O07026; 2-176. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Electron transport; Flavoprotein; FMN; Transport. FT CHAIN 1 176 Flavodoxin. FT /FTId=PRO_0000171636. FT DOMAIN 4 165 Flavodoxin-like. SQ SEQUENCE 176 AA; 19765 MW; C40E5F80287D3636 CRC64; MAIIGIFFGS DTGNTENIAK MIQKQLGKDV ADVHDIAKSS KEDLEAHDIL LLGIPTWYYG EAQCDWDDFF PTLEEIDFNG KLVALFGCGD QEDYAEYFCD ALGTIRDIIE PRGATIVGHW PTAGYHFEAS KGLADDDHFV GLAIDEDRQP ELTNERVEKW VKQVAEELHL EEIKNA // ID FLS_MATIN Reviewed; 291 AA. AC O04395; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 31-OCT-2006, entry version 40. DE Flavonol synthase/flavanone 3-hydroxylase (EC 1.14.11.23) DE (EC 1.14.11.9) (FLS) (Fragment). OS Matthiola incana (Common stock). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC rosids; eurosids II; Brassicales; Brassicaceae; Matthiola. OX NCBI_TaxID=3724; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Flower bud, and Petal; RA Henkel J., Forkmann G.; RT "Cloning and expression of a flavonol synthase gene from common stock RT (Matthiola incana)."; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the formation of flavonols from CC dihydroflavonols. It can act on dihydrokaempferol to produce CC kaempferol, on dihydroquercetin to produce quercitin and on CC dihydromyricetin to produce myricetin. CC -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a CC flavonol + succinate + CO(2) + H(2)O. CC -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a CC dihydroflavonol + succinate + CO(2). CC -!- COFACTOR: Binds 1 ascorbate molecule per subunit. CC -!- COFACTOR: Binds 1 iron ion per subunit. CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF001391; AAB58800.1; -; mRNA. DR HSSP; Q96323; 1GP6. DR GO; GO:0045431; F:flavonol synthase activity; IEA:EC. DR GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC. DR InterPro; IPR005123; 2OG-FeII_Oase. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. KW Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; KW Oxidoreductase; Vitamin C. FT CHAIN <1 291 Flavonol synthase/flavanone 3- FT hydroxylase. FT /FTId=PRO_0000067295. FT METAL 175 175 Iron (By similarity). FT METAL 177 177 Iron (By similarity). FT METAL 231 231 Iron (By similarity). FT NON_TER 1 1 SQ SEQUENCE 291 AA; 33430 MW; 6B8E4E3D2834720A CRC64; QVPVVDLSCP DEELVARTVV KASEDWGVFQ VVNHGIPTEL IQRLQKVGRE FFELPEAEKR SCAREAGSVE GYGRRIELDI KKRKGIVDQI YLSTWPPSSV NYRYWPKSPP DYREVNEEYA RHVKTLSEKI MEWLSEGLGL GREAIKEVNG CWYVMNINHY PPYPHSDSFN GLEPHTDING LTLIITNEIP GLQVFKDDHW IEVEYIPSAI IVNIGDQIMM LSNGKYKNVL HKTTVDKEKT RMSWPVLVSP TYDMVVGPLP ELTSEDDPPK FKPIAYKDYV HNKITFLKNK S // ID FLAV_MEGEL Reviewed; 137 AA. AC P00321; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 20-MAR-2007, entry version 50. DE Flavodoxin. OS Megasphaera elsdenii. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Acidaminococcaceae; OC Megasphaera. OX NCBI_TaxID=907; RN [1] RP PROTEIN SEQUENCE. RC STRAIN=ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927; RX MEDLINE=73197809; PubMed=4711610; RA Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G., Massey V.; RT "The primary structure of Peptostreptococcus elsdenii flavodoxin."; RL J. Biol. Chem. 248:4354-4366(1973). RN [2] RP SEQUENCE REVISION TO 78-82. RX MEDLINE=74277393; PubMed=4843143; RA Tanaka M., Haniu M., Yasunobu K.T., Mayhew S.G., Massey V.; RT "Correction of the amino acid sequence of Peptostreptococcus elsdenii RT flavodoxin."; RL J. Biol. Chem. 249:4397-4397(1974). RN [3] RP PROTEIN SEQUENCE OF 1-41 AND 136-137. RC STRAIN=ATCC 25940 / DSM 20460 / JCM 1772 / NCIB 8927; RX MEDLINE=72062407; PubMed=5126921; DOI=10.1021/bi00792a009; RA Tanaka M., Haniu M., Matsueda G., Yasunobu K.T., Mayhew S., Massey V.; RT "Amino- and carboxyl-terminal amino acid sequences of the RT Peptostreptococcus eisdenii and Clostridium pasteurianum RT flavodoxins."; RL Biochemistry 10:3041-3046(1971). RN [4] RP STRUCTURE BY NMR. RX MEDLINE=90276429; PubMed=2161759; RA van Mierlo C.P.M., Mueller F., Vervoort J.; RT "Secondary and tertiary structure characteristics of Megasphaera RT elsdenii flavodoxin in the reduced state as determined by two- RT dimensional 1H NMR."; RL Eur. J. Biochem. 189:589-600(1990). RN [5] RP STRUCTURE BY NMR. RX MEDLINE=91071190; PubMed=2253614; RA van Mierlo C.P.M., Lijnzaad P., Vervoort J., Mueller F., RA Berendsen H.J.C., de Vlieg J.; RT "Tertiary structure of two-electron reduced Megasphaera elsdenii RT flavodoxin and some implications, as determined by two-dimensional 1H- RT NMR and restrained molecular dynamics."; RL Eur. J. Biochem. 194:185-198(1990). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. CC -!- COFACTOR: FMN. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PIR; A92137; FXME. DR PDB; 2FZ5; NMR; A=1-137. DR InterPro; IPR010087; Flav_short. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR TIGRFAMs; TIGR01753; flav_short; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW 3D-structure; Direct protein sequencing; Electron transport; KW Flavoprotein; FMN; Transport. FT CHAIN 1 137 Flavodoxin. FT /FTId=PRO_0000171639. FT DOMAIN 2 137 Flavodoxin-like. FT STRAND 2 6 FT STRAND 9 11 FT HELIX 12 26 FT STRAND 31 35 FT HELIX 41 45 FT STRAND 48 53 FT TURN 58 60 FT HELIX 64 74 FT HELIX 75 77 FT STRAND 82 91 FT HELIX 95 106 FT STRAND 110 123 FT HELIX 126 135 SQ SEQUENCE 137 AA; 14550 MW; 86BD744412D6F869 CRC64; MVEIVYWSGT GNTEAMANEI EAAVKAAGAD VESVRFEDTN VDDVASKDVI LLGCPAMGSE ELEDSVVEPF FTDLAPKLKG KKVGLFGSYG WGSGEWMDAW KQRTEDTGAT VIGTAIVNEM PDNAPECKEL GEAAAKA // ID FLAV_NOSSM Reviewed; 35 AA. AC P35707; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 31-OCT-2006, entry version 30. DE Flavodoxin (Fragment). OS Nostoc sp. (strain MAC). OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc. OX NCBI_TaxID=35822; RN [1] RP PROTEIN SEQUENCE. RA Takruri I.A.H., Boulter D., Fitzgerald M.P., Hutber G.N., Rogers L.J.; RT "N-terminal amino acid sequences of flavodoxins from Chondrus crispus RT and Nostoc strain MAC."; RL Phytochemistry 25:2113-2115(1986). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. CC -!- COFACTOR: FMN. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR HSSP; P11241; 1RCF. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Direct protein sequencing; Electron transport; Flavoprotein; FMN; KW Transport. FT CHAIN 1 >35 Flavodoxin. FT /FTId=PRO_0000171640. FT DOMAIN 4 >35 Flavodoxin-like. FT NON_TER 35 35 SQ SEQUENCE 35 AA; 3820 MW; B6EEB5CA7A45DDA6 CRC64; SKKIGLFYGT ZTGKTESVAE IIDEFGDEVV TLDID // ID FLS_PETHY Reviewed; 348 AA. AC Q07512; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 06-MAR-2007, entry version 43. DE Flavonol synthase/flavanone 3-hydroxylase (EC 1.14.11.23) DE (EC 1.14.11.9) (FLS). GN Name=FL; OS Petunia hybrida (Petunia). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia. OX NCBI_TaxID=4102; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Old Glory Blue; TISSUE=Petal; RX MEDLINE=94108485; PubMed=7904213; RA Holton T.A., Brugliera F., Tanaka Y.; RT "Cloning and expression of flavonol synthase from Petunia hybrida."; RL Plant J. 4:1003-1010(1993). CC -!- FUNCTION: Catalyzes the formation of flavonols from CC dihydroflavonols. It can act on dihydrokaempferol to produce CC kaempferol, on dihydroquercetin to produce quercitin and on CC dihydromyricetin to produce myricetin. CC -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a CC flavonol + succinate + CO(2) + H(2)O. CC -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a CC dihydroflavonol + succinate + CO(2). CC -!- COFACTOR: Binds 1 ascorbate molecule per subunit. CC -!- COFACTOR: Binds 1 iron ion per subunit. CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DEVELOPMENTAL STAGE: Expressed at highest level during the first CC stage of flower development. CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z22543; CAA80264.1; -; mRNA. DR PIR; S33510; S33510. DR HSSP; Q96323; 1GP6. DR GO; GO:0045431; F:flavonol synthase activity; IEA:EC. DR GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC. DR InterPro; IPR005123; 2OG-FeII_Oase. DR InterPro; IPR002283; IPN_synth. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. DR PRINTS; PR00682; IPNSYNTHASE. KW Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; KW Oxidoreductase; Vitamin C. FT CHAIN 1 348 Flavonol synthase/flavanone 3- FT hydroxylase. FT /FTId=PRO_0000067296. FT METAL 234 234 Iron (By similarity). FT METAL 236 236 Iron (By similarity). FT METAL 290 290 Iron (By similarity). SQ SEQUENCE 348 AA; 39427 MW; B39E1E4381DE6379 CRC64; MKTAQGVSAT LTMEVARVQA IASLSKCMDT IPSEYIRSEN EQPAATTLHG VVLQVPVIDL RDPDENKMVK LIADASKEWG IFQLINHGIP DEAIADLQKV GKEFFEHVPQ EEKELIAKTP GSNDIEGYGT SLQKEVEGKK GWVDHLFHKI WPPSAVNYRY WPKNPPSYRE ANEEYGKRMR EVVDRIFKSL SLGLGLEGHE MIEAAGGDEI VYLLKINYYP PCPRPDLALG VVAHTDMSYI TILVPNEVQG LQVFKDGHWY DVKYIPNALI VHIGDQVEIL SNGKYKSVYH RTTVNKDKTR MSWPVFLEPP SEHEVGPIPK LLSEANPPKF KTKKYKDYVY CKLNKLPQ // ID FLAV_RHOCA Reviewed; 182 AA. AC P52967; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 36. DE Flavodoxin. GN Name=nifF; OS Rhodobacter capsulatus (Rhodopseudomonas capsulata). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Rhodobacteraceae; Rhodobacter. OX NCBI_TaxID=1061; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 23782 / LMG 2373 / NCIB 11773 / SB1003 / St. Louis; RX MEDLINE=96272272; PubMed=8682802; RA Gennaro G., Huebner P., Sandmeier U., Yakunin A.F., Hallenbeck P.C.; RT "Cloning, characterization, and regulation of nifF from Rhodobacter RT capsulatus."; RL J. Bacteriol. 178:3949-3952(1996). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. NifF is the electron donor to nitrogenase. CC -!- COFACTOR: FMN. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L42290; AAC05792.1; -; Genomic_DNA. DR HSSP; P11241; 1OBO. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Electron transport; Flavoprotein; FMN; Nitrogen fixation; Transport. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 182 Flavodoxin. FT /FTId=PRO_0000171641. FT DOMAIN 4 173 Flavodoxin-like. SQ SEQUENCE 182 AA; 19820 MW; 95452D6EA538243E CRC64; MAKIGLFFGS DTGTTRKIAK QIKDMFDDEV MAKPLNVNRA DVADFMAYDF LILGTPTLGD GQLPGLSANA ASESWEEFLP RIADQDFSGK TIALFGLGDQ VTYPLEFVNA LFFLHEFFSD RGANVVGRWP AKGYGFEDSL AVVEGEFLGL ALDQDNQAAL TPERLKGWLS LIAADFGLVL PA // ID FLS_SOLTU Reviewed; 349 AA. AC Q41452; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 06-MAR-2007, entry version 40. DE Flavonol synthase/flavanone 3-hydroxylase (EC 1.14.11.23) DE (EC 1.14.11.9) (FLS). OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; OC Solanum. OX NCBI_TaxID=4113; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Pistil; RX MEDLINE=97177800; PubMed=9025306; RA van Eldik G.J., Ruiter R.K., Reijnen W.H., van Herpen M.M.A., RA Schrauwen J.A.M., Wullems G.J.; RT "Regulation of flavonol biosynthesis during anther and pistil RT development, and during pollen tube growth in Solanum tuberosum."; RL Plant J. 11:105-113(1997). CC -!- FUNCTION: Catalyzes the formation of flavonols from CC dihydroflavonols. It can act on dihydrokaempferol to produce CC kaempferol, on dihydroquercetin to produce quercitin and on CC dihydromyricetin to produce myricetin. CC -!- CATALYTIC ACTIVITY: A dihydroflavonol + 2-oxoglutarate + O(2) = a CC flavonol + succinate + CO(2) + H(2)O. CC -!- CATALYTIC ACTIVITY: A flavanone + 2-oxoglutarate + O(2) = a CC dihydroflavonol + succinate + CO(2). CC -!- COFACTOR: Binds 1 iron ion per subunit (By similarity). CC -!- COFACTOR: Binds 1 ascorbate molecule per subunit (By similarity). CC -!- PATHWAY: Secondary metabolite biosynthesis; flavonoid CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DEVELOPMENTAL STAGE: Temporally expressed during flower CC development. CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X92178; CAA63092.1; -; mRNA. DR PIR; T07373; T07373. DR HSSP; Q96323; 1GP6. DR GO; GO:0045431; F:flavonol synthase activity; IEA:EC. DR GO; GO:0045486; F:naringenin 3-dioxygenase activity; IEA:EC. DR InterPro; IPR005123; 2OG-FeII_Oase. DR InterPro; IPR002283; IPN_synth. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. DR PRINTS; PR00682; IPNSYNTHASE. KW Dioxygenase; Flavonoid biosynthesis; Iron; Metal-binding; KW Oxidoreductase; Vitamin C. FT CHAIN 1 349 Flavonol synthase/flavanone 3- FT hydroxylase. FT /FTId=PRO_0000067297. FT METAL 238 238 Iron (By similarity). FT METAL 240 240 Iron (By similarity). FT METAL 291 291 Iron (By similarity). SQ SEQUENCE 349 AA; 39728 MW; ADBBC3F6B10A0E05 CRC64; MKTIQGQSAT TALTMEVARV QAISSITKCM DTIPSEYIRS ENEQPAATTL QGVVLEVPVI DISNVDDDEE KLVKEIVEAS KEWGIFQVIN HGIPDEVIEN LQKVGKEFFE EVPQEEKELI AKKPGAQSLE GYGTSLQKEI EGKKGWVDHL FHKIWPPSAI NYRYWPKNPP SYREANEEYA KWLRKVADGI FRSLSLGLGL EGHEMMEAAG SEDIVYMLKI NYYPPCPRPD LALGVVAHTD MSYITLLVPN EVQVFKDGHW YDVNYIPNAI IVHIGDQVEI LSNGKYKSVY HRTTVNKYKT RMSWPVFLEP SSEHEVGPIP NLINEANPPK FKTKKYKDYV YCKLNKLPQ // ID FLAV_SYNP2 Reviewed; 170 AA. AC P31158; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 23-JAN-2007, entry version 39. DE Flavodoxin. GN Name=isiB; OS Synechococcus sp. (strain PCC 7002) (Agmenellum quadruplicatum). OC Bacteria; Cyanobacteria; Chroococcales; Synechococcus. OX NCBI_TaxID=32049; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92407507; PubMed=1527503; RA Leonhardt K.G., Straus N.A.; RT "An iron stress operon involved in photosynthetic electron transport RT in the marine cyanobacterium Synechococcus sp. PCC 7002."; RL J. Gen. Microbiol. 138:1613-1621(1992). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. CC -!- COFACTOR: FMN. CC -!- INDUCTION: By iron stress. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M88253; AAA27318.1; -; Genomic_DNA. DR HSSP; P10340; 1OFV. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Electron transport; Flavoprotein; FMN; Transport. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 170 Flavodoxin. FT /FTId=PRO_0000171643. FT DOMAIN 4 165 Flavodoxin-like. SQ SEQUENCE 170 AA; 18479 MW; FFBB605F69E701BA CRC64; MSKIGLFFGT QTGNTEELAQ AIQAAFGGSD IVELFDVAEV DIEALRDFDQ LIIGCPTWNV GELQSDWEAL YDDLDDVDFS GKTIAYFGAG DQVGYADNFQ DAMGVLEEKI TSLGGKTVGQ WPTAGYDHSE SKAERDGKFV GLAIDEDNQP ELTAERIQAW VAQLKPAFGL // ID FLAV_SYNP7 Reviewed; 170 AA. AC P10340; Q31MZ8; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 20-MAR-2007, entry version 64. DE Flavodoxin. GN Name=isiB; OrderedLocusNames=Synpcc7942_1541; OS Synechococcus sp. (strain PCC 7942) (Anacystis nidulans R2). OC Bacteria; Cyanobacteria; Chroococcales; Synechococcus. OX NCBI_TaxID=1140; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88086879; PubMed=3121586; RA Laudenbach D.E., Reith M.E., Straus N.A.; RT "Isolation, sequence analysis, and transcriptional studies of the RT flavodoxin gene from Anacystis nidulans R2."; RL J. Bacteriol. 170:258-265(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., RA Kyrpides N., Lykidis A., Richardson P.; RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC RT 7942."; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 2-56, AND X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX MEDLINE=83216115; PubMed=6406674; DOI=10.1016/S0022-2836(83)80277-0; RA Smith W.W., Pattridge K.A., Ludwig M.L., Petsko G.A., Tsernoglou D., RA Tanaka M., Yasunobu K.T.; RT "Structure of oxidized flavodoxin from Anacystis nidulans."; RL J. Mol. Biol. 165:737-753(1983). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). RX MEDLINE=20079529; PubMed=10610791; DOI=10.1006/jmbi.1999.3151; RA Drennan C.L., Pattridge K.A., Weber C.H., Metzger A.L., Hoover D.M., RA Ludwig M.L.; RT "Refined structures of oxidized flavodoxin from Anacystis nidulans."; RL J. Mol. Biol. 294:711-724(1999). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS). RX MEDLINE=20079530; PubMed=10610792; DOI=10.1006/jmbi.1999.3152; RA Hoover D.M., Drennan C.L., Metzger A.L., Osborne C., Weber C.H., RA Pattridge K.A., Ludwig M.L.; RT "Comparisons of wild-type and mutant flavodoxins from Anacystis RT nidulans. Structural determinants of the redox potentials."; RL J. Mol. Biol. 294:725-743(1999). RN [6] RP STRUCTURE BY NMR. RX MEDLINE=91329335; PubMed=1907844; DOI=10.1021/bi00245a008; RA Clubb R.T., Thanabal V., Osborne C., Wagner G.; RT "1H and 15N resonance assignments of oxidized flavodoxin from RT Anacystis nidulans with 3D NMR."; RL Biochemistry 30:7718-7730(1991). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. CC -!- COFACTOR: FMN. CC -!- INDUCTION: By iron stress. CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M19116; AAA22050.1; -; Genomic_DNA. DR EMBL; CP000100; ABB57571.1; -; Genomic_DNA. DR PDB; 1CZH; X-ray; A=1-170. DR PDB; 1CZK; X-ray; A=1-170. DR PDB; 1CZL; X-ray; A=1-170. DR PDB; 1CZN; X-ray; A=1-170. DR PDB; 1CZO; X-ray; A=1-170. DR PDB; 1CZR; X-ray; A=1-170. DR PDB; 1CZU; X-ray; A=1-170. DR PDB; 1D03; X-ray; A=1-170. DR PDB; 1D04; X-ray; A=1-170. DR PDB; 1OFV; X-ray; @=1-170. DR GenomeReviews; CP000100_GR; Synpcc7942_1541. DR KEGG; syf:Synpcc7942_1541; -. DR LinkHub; P10340; -. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW 3D-structure; Complete proteome; Direct protein sequencing; KW Electron transport; Flavoprotein; FMN; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 170 Flavodoxin. FT /FTId=PRO_0000171644. FT DOMAIN 4 165 Flavodoxin-like. FT CONFLICT 55 55 C -> S (in Ref. 3). FT STRAND 3 7 FT STRAND 10 12 FT HELIX 13 25 FT TURN 28 30 FT STRAND 31 35 FT HELIX 36 38 FT HELIX 41 46 FT STRAND 48 53 FT TURN 58 60 FT HELIX 64 69 FT HELIX 70 75 FT STRAND 82 88 FT TURN 91 96 FT HELIX 100 110 FT TURN 111 113 FT STRAND 120 122 FT STRAND 137 143 FT TURN 145 147 FT HELIX 149 151 FT HELIX 152 167 SQ SEQUENCE 170 AA; 18778 MW; 7291AEF23DCA0345 CRC64; MAKIGLFYGT QTGVTQTIAE SIQQEFGGES IVDLNDIANA DASDLNAYDY LIIGCPTWNV GELQSDWEGI YDDLDSVNFQ GKKVAYFGAG DQVGYSDNFQ DAMGILEEKI SSLGSQTVGY WPIEGYDFNE SKAVRNNQFV GLAIDEDNQP DLTKNRIKTW VSQLKSEFGL // ID FLAV_SYNY3 Reviewed; 170 AA. AC P27319; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 2. DT 23-JAN-2007, entry version 49. DE Flavodoxin. GN Name=isiB; OrderedLocusNames=sll0248; OS Synechocystis sp. (strain PCC 6803). OC Bacteria; Cyanobacteria; Chroococcales; Synechocystis. OX NCBI_TaxID=1148; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=94320780; PubMed=8045418; DOI=10.1016/0378-1119(94)90342-5; RA Poncelet M.G.M., Cassier-Chauvat C.J.S., Chauvat F.R.L.; RT "Sequence of the flavodoxin-encoding gene from the cyanobacterium RT Synechocystis PCC6803."; RL Gene 145:153-154(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=97061201; PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., RA Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the RT entire genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). RN [3] RP PROTEIN SEQUENCE OF 1-42. RX MEDLINE=92338182; PubMed=1633177; DOI=10.1016/0167-4838(92)90465-P; RA Bottin H., Lagoutte B.; RT "Ferredoxin and flavodoxin from the cyanobacterium Synechocystis sp RT PCC 6803."; RL Biochim. Biophys. Acta 1101:48-56(1992). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes. CC -!- COFACTOR: FMN. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Redox potential: CC E(0) are -433 mV and -238 mV; CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z27091; CAA81614.1; -; Genomic_DNA. DR EMBL; L25881; AAA27288.1; -; Genomic_DNA. DR EMBL; BA000022; BAA17947.1; -; Genomic_DNA. DR PIR; S38632; S38632. DR HSSP; P10340; 1OFV. DR SMR; P27319; 3-165. DR GenomeReviews; BA000022_GR; sll0248. DR KEGG; syn:sll0248; -. DR BioCyc; SSP1148:SLL0248-MONOMER; -. DR GO; GO:0009767; P:photosynthetic electron transport; NAS:UniProtKB. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001094; Flavdoxin_like. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR PRINTS; PR00369; FLAVODOXIN. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Complete proteome; Direct protein sequencing; Electron transport; KW Flavoprotein; FMN; Transport. FT CHAIN 1 170 Flavodoxin. FT /FTId=PRO_0000171645. FT DOMAIN 4 165 Flavodoxin-like. FT CONFLICT 2 2 Missing (in Ref. 3). FT CONFLICT 40 40 A -> AA (in Ref. 3). SQ SEQUENCE 170 AA; 18822 MW; B2937F347796BBD9 CRC64; MTKIGLFYGT QTGNTETIAE LIQKEMGGDS VVDMMDISQA DVDDFRQYSC LIIGCPTWNV GELQSDWEGF YDQLDEIDFN GKKVAYFGAG DQVGYADNFQ DAMGILEEKI SGLGGKTVGF WPTAGYDFDE SKAVKNGKFV GLALDEDNQP ELTELRVKTW VSEIKPILQS // ID FLAV_TREPA Reviewed; 146 AA. AC O83895; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 06-MAR-2007, entry version 37. DE Flavodoxin. GN Name=fldA; OrderedLocusNames=TP_0925; OS Treponema pallidum. OC Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema. OX NCBI_TaxID=160; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nichols; RX MEDLINE=98332770; PubMed=9665876; DOI=10.1126/science.281.5375.375; RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G., RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A., RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D., RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., RA Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D., RA Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M., RA Weidman J.F., Smith H.O., Venter J.C.; RT "Complete genome sequence of Treponema pallidum, the syphilis RT spirochete."; RL Science 281:375-388(1998). CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes (By similarity). CC -!- COFACTOR: FMN (By similarity). CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AE000520; AAC65882.1; -; Genomic_DNA. DR PIR; F71263; F71263. DR HSSP; P00322; 2FVX. DR GenomeReviews; AE000520_GR; TP_0925. DR KEGG; tpa:TP0925; -. DR TIGR; TP_0925; -. DR InterPro; IPR010087; Flav_short. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR TIGRFAMs; TIGR01753; flav_short; 1. DR PROSITE; PS00201; FLAVODOXIN; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Complete proteome; Electron transport; Flavoprotein; FMN; Transport. FT CHAIN 1 146 Flavodoxin. FT /FTId=PRO_0000171646. FT DOMAIN 4 145 Flavodoxin-like. SQ SEQUENCE 146 AA; 15793 MW; 398A7D7C8530F2CE CRC64; MAKVAVIFWS GTGHTETMAR CIVEGLNVGG AKADLFSVMD FDVGTFDSYD RFAFGCSAAG SEELESSEFE PFFTSIEGRL SGKKVALFGS YEWAGEGEGG EWMVNWVERC KAAGADVFEG KGEIAYDDPS EEAQASCKAF GERFAR // ID FLAV_TRIEI Reviewed; 171 AA. AC O52659; Q114Y7; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 2. DT 12-DEC-2006, entry version 33. DE Flavodoxin. GN Name=fld; OrderedLocusNames=Tery_1666; OS Trichodesmium erythraeum (strain IMS101). OC Bacteria; Cyanobacteria; Oscillatoriales; Trichodesmium. OX NCBI_TaxID=203124; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Kiss H., Munk A.C., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Kim E., Richardson P.; RT "Complete sequence of Trichodesmium erythraeum IMS101."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-146. RA Lin S., Carpenter E.J.; RT "Identification of a gene encoding flavodoxin in the marine RT cyanobacterium Trichodesmium."; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Low-potential electron donor to a number of redox CC enzymes (By similarity). CC -!- COFACTOR: FMN (By similarity). CC -!- SIMILARITY: Belongs to the flavodoxin family. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000393; ABG50937.1; -; Genomic_DNA. DR EMBL; AF044318; AAC02683.1; -; Genomic_DNA. DR HSSP; P11241; 1RCF. DR SMR; O52659; 1-144. DR GenomeReviews; CP000393_GR; Tery_1666. DR InterPro; IPR010086; Flav_long. DR InterPro; IPR001226; Flavodoxin. DR InterPro; IPR008254; Flavodoxin_1. DR Pfam; PF00258; Flavodoxin_1; 1. DR TIGRFAMs; TIGR01752; flav_long; 1. DR PROSITE; PS00201; FLAVODOXIN; FALSE_NEG. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. KW Complete proteome; Electron transport; Flavoprotein; FMN; Transport. FT CHAIN 1 171 Flavodoxin. FT /FTId=PRO_0000171647. FT DOMAIN 4 166 Flavodoxin-like. FT CONFLICT 4 4 I -> M (in Ref. 2; AAC02683). FT CONFLICT 8 8 V -> F (in Ref. 2; AAC02683). FT CONFLICT 130 130 E -> V (in Ref. 2; AAC02683). SQ SEQUENCE 171 AA; 18742 MW; 677F643438653126 CRC64; MSKIGLFVGT TTGKTEEAAE KIKEEFGGDD VVTIHDISEA SPEDFDGYQN VIIGCPTWDV GELQSDWSGF YSEELDNVKF TGKKVAYFGT GDQIGYADNF QDAMGILEEK ITGLGGTTIG SWSTEGYDHE DSKAVKNGKF VGLALDDDNQ ADLTDERIKE WVKQLKTEFG V // ID PAX1_HUMAN Reviewed; 440 AA. AC P15863; Q642X9; Q6NTC0; Q9Y558; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 3. DT 23-JAN-2007, entry version 69. DE Paired box protein Pax-1 (HUP48). GN Name=PAX1; Synonyms=HUP48; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., RA Nguyen C.P., Nguyen D.A., Poel C.L., Chambers S.W., Schackwitz W.S., RA Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A.; RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE OF 1-142. RX MEDLINE=89305521; PubMed=2501086; RA Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.; RT "Conservation of the paired domain in metazoans and its structure in RT three isolated human genes."; RL EMBO J. 8:1183-1190(1989). RN [5] RP VARIANT HIS-45. RX MEDLINE=97016531; PubMed=8863157; RA Hol F.A., Geurds M.P.A., Chatkupt S., Shugart Y.Y., Balling R., RA Schrander-Stumpel C.T.R.M., Johnson W.G., Hamel B.C.J., RA Mariman E.C.M.; RT "PAX genes and human neural tube defects: an amino acid substitution RT in PAX1 in a patient with spina bifida."; RL J. Med. Genet. 33:655-660(1996). CC -!- FUNCTION: This protein is a transcriptional activator. It may play CC a role in the formation of segmented structures of the embryo. May CC play an important role in the normal development of the vertebral CC column (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P15863-1; Sequence=Displayed; CC Name=2; CC IsoId=P15863-2; Sequence=VSP_012986, VSP_012987; CC -!- SIMILARITY: Contains 1 paired domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY740018; AAU21037.1; -; Genomic_DNA. DR EMBL; AL035562; CAB46996.1; -; Genomic_DNA. DR EMBL; BC069134; AAH69134.1; -; mRNA. DR EMBL; X15044; CAA33146.1; ALT_INIT; Genomic_DNA. DR PIR; S06961; S06961. DR UniGene; Hs.349082; -. DR HSSP; Q02548; 1K78. DR SMR; P15863; 8-130. DR TRANSFAC; T00398; -. DR Ensembl; ENSG00000125813; Homo sapiens. DR KEGG; hsa:5075; -. DR HGNC; HGNC:8615; PAX1. DR MIM; 167411; gene. DR ArrayExpress; P15863; -. DR GermOnline; ENSG00000125813; Homo sapiens. DR RZPD-ProtExp; T1074; -. DR GO; GO:0001501; P:skeletal development; TAS:ProtInc. DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. DR InterPro; IPR009057; Homeodomain_like. DR InterPro; IPR001523; Paired_box_N. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2. DR Pfam; PF00292; PAX; 1. DR PRINTS; PR00027; PAIREDBOX. DR SMART; SM00351; PAX; 1. DR PROSITE; PS00034; PAIRED_1; 1. DR PROSITE; PS51057; PAIRED_2; 1. KW Activator; Alternative splicing; Developmental protein; DNA-binding; KW Nuclear protein; Paired box; Polymorphism; Transcription; KW Transcription regulation. FT CHAIN 1 440 Paired box protein Pax-1. FT /FTId=PRO_0000050172. FT DOMAIN 4 130 Paired. FT VAR_SEQ 330 361 PSREGSLPAPAARPRTPSVAYTDCPSRPRPPR -> REGTD FT RKPPSSGSKAPDALSSLHGLPIPASTS (in isoform FT 2). FT /FTId=VSP_012986. FT VAR_SEQ 362 440 Missing (in isoform 2). FT /FTId=VSP_012987. FT VARIANT 45 45 Q -> H (in a patient with neural tube FT defects, but not clearly linked to the FT disease). FT /FTId=VAR_003787. FT CONFLICT 1 1 M -> A (in Ref. 4). SQ SEQUENCE 440 AA; 46295 MW; 500B7155C81616F9 CRC64; MEQTYGEVNQ LGGVFVNGRP LPNAIRLRIV ELAQLGIRPC DISRQLRVSH GCVSKILARY NETGSILPGA IGGSKPRVTT PNVVKHIRDY KQGDPGIFAW EIRDRLLADG VCDKYNVPSV SSISRILRNK IGSLAQPGPY EASKQPPSQP TLPYNHIYQY PYPSPVSPTG AKMGSHPGVP GTAGHVSIPR SWPSAHSVSN ILGIRTFMEQ TGALAGSEGT AYSPKMEDWA GVNRTAFPAT PAVNGLEKPA LEADIKYTQS ASTLSAVGGF LPACAYPASN QHGVYSAPGG GYLAPGPPWP PAQGPPLAPP GAGVAVHGGE LAAAMTFKHP SREGSLPAPA ARPRTPSVAY TDCPSRPRPP RGSSPRTRAR RERQADPGAQ VCAAAPAIGT GRIGGLAEEE ASAGPRGARP ASPQAQPCLW PDPPHFLYWS GFLGFSELGF // ID PAX2_HUMAN Reviewed; 416 AA. AC Q02962; Q15105; Q15110; Q15837; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 3. DT 20-FEB-2007, entry version 77. DE Paired box protein Pax-2. GN Name=PAX2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=96299768; PubMed=8661132; DOI=10.1006/geno.1996.0350; RA Sanyanusin P., Norrish J.H., Ward T.A., Nebel A., McNoe L.A., RA Eccles M.R.; RT "Genomic structure of the human PAX2 gene."; RL Genomics 35:258-261(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Kidney; RX MEDLINE=92338102; PubMed=1378753; RA Eccles M.R., Wallis L.J., Fidler A.E., Spurr N.K., Goodfellow P.J., RA Reeve A.E.; RT "Expression of the PAX2 gene in human fetal kidney and Wilms' tumor."; RL Cell Growth Differ. 3:279-289(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136. RX MEDLINE=95072651; PubMed=7981748; DOI=10.1038/ng0493-292; RA Stapleton P., Weith A., Urbanek P., Kozmik Z., Busslinger M.; RT "Chromosomal localization of seven PAX genes and cloning of a novel RT family member, PAX-9."; RL Nat. Genet. 3:292-298(1993). RN [4] RP NUCLEOTIDE SEQUENCE, AND ALTERNATIVE SPLICING. RC TISSUE=Kidney cortex; RA Ward T.A., Nebel A., Eccles M.R.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. RN [5] RP VARIANTS RCS GLU-THR-75 INS AND SER-76. RX MEDLINE=98430997; PubMed=9760197; DOI=10.1007/s004390050798; RA Devriendt K., Matthijs G., van Damme B., van Caesbroeck D., RA Eccles M.R., Vanrenterghem Y., Fryns J.-P., Leys A.; RT "Missense mutation and hexanucleotide duplication in the PAX2 gene in RT two unrelated families with renal-coloboma syndrome (MIM 120330)."; RL Hum. Genet. 103:149-153(1998). RN [6] RP VARIANT VAL-334. RX MEDLINE=21113232; PubMed=11180607; RX DOI=10.1002/1098-1004(200102)17:2<155::AID-HUMU16>3.0.CO;2-9; RA Gelb A.C., Manligas G.S., Gharaybeh S., Schimmenti L.A.; RT "Identification of two novel polymorphisms (g.903C>T and g.1544C>T) in RT the PAX2 gene."; RL Hum. Mutat. 17:155-155(2001). RN [7] RP VARIANT OMN 39-GLN-ARG-40 DEL. RX MEDLINE=21105676; PubMed=11168927; RX DOI=10.1046/j.1523-1755.2001.059002457.x; RA Salomon R., Tellier A.-L., Attie-Bitach T., Amiel J., Vekemans M., RA Lyonnet S., Dureau P., Niaudet P., Gubler M.-C., Broyer M.; RT "PAX2 mutations in oligomeganephronia."; RL Kidney Int. 59:457-462(2001). CC -!- FUNCTION: Probable transcription factor that may have a role in CC kidney cell differentiation. Has a critical role in the CC development of the urogenital tract, the eyes, and the CNS. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q02962-1; Sequence=Displayed; CC Name=2; Synonyms=Fetal kidney; CC IsoId=Q02962-2; Sequence=VSP_002346; CC Name=3; CC IsoId=Q02962-3; Sequence=VSP_002345; CC -!- TISSUE SPECIFICITY: Expressed in primitive cells of the kidney, CC ureter, eye, ear and central nervous system. CC -!- DEVELOPMENTAL STAGE: Mainly in fetal kidney and juvenile CC nephrogenic rests. CC -!- DISEASE: Defects in PAX2 are the cause of renal-coloboma syndrome CC (RCS) [MIM:120330]; also known as papillorenal syndrome or optic CC nerve coloboma with renal disease. RCS is an autosomal dominant CC disease characterized by the association of renal hypoplasia, CC vesicoureteral reflux and dysplasia of the retina and optic disk. CC -!- DISEASE: Defects in PAX2 may be responsible for isolated renal CC hypoplasia as observed in oligomeganephronia (OMN). OMN is a rare CC congenital and usually sporadic anomaly characterized by bilateral CC renal hypoplasia, with a reduced number of enlarged nephrons and CC without urinary tract abnormalities. CC -!- SIMILARITY: Contains 1 paired domain. CC -!- WEB RESOURCE: NAME=PAX2 mutation db; CC URL="http://www.hgu.mrc.ac.uk/Softdata/PAX2/". CC -!- WEB RESOURCE: NAME=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/PAX2ID41642ch10q24.html". CC -!- WEB RESOURCE: NAME=GeneReviews; CC URL="http://www.genetests.org/query?gene=PAX2". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U45255; AAC63385.1; -; Genomic_DNA. DR EMBL; U45245; AAC63385.1; JOINED; Genomic_DNA. DR EMBL; U45246; AAC63385.1; JOINED; Genomic_DNA. DR EMBL; U45247; AAC63385.1; JOINED; Genomic_DNA. DR EMBL; U45248; AAC63385.1; JOINED; Genomic_DNA. DR EMBL; U45249; AAC63385.1; JOINED; Genomic_DNA. DR EMBL; U45250; AAC63385.1; JOINED; Genomic_DNA. DR EMBL; U45251; AAC63385.1; JOINED; Genomic_DNA. DR EMBL; U45253; AAC63385.1; JOINED; Genomic_DNA. DR EMBL; U45254; AAC63385.1; JOINED; Genomic_DNA. DR EMBL; M89470; AAA60024.1; -; mRNA. DR EMBL; L09747; AAC41711.1; -; Genomic_DNA. DR EMBL; L09748; AAC41711.1; JOINED; Genomic_DNA. DR EMBL; L09746; AAC41711.1; JOINED; Genomic_DNA. DR EMBL; L25597; AAA36417.1; -; mRNA. DR PIR; A49008; A49008. DR UniGene; Hs.155644; -. DR HSSP; Q02548; 1K78. DR SMR; Q02962; 19-142. DR TRANSFAC; T01823; -. DR Ensembl; ENSG00000075891; Homo sapiens. DR KEGG; hsa:5076; -. DR HGNC; HGNC:8616; PAX2. DR MIM; 120330; phenotype. DR MIM; 167409; gene. DR ArrayExpress; Q02962; -. DR GermOnline; ENSG00000075891; Homo sapiens. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. DR GO; GO:0007409; P:axonogenesis; TAS:ProtInc. DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. DR InterPro; IPR009057; Homeodomain_like. DR InterPro; IPR001523; Paired_box_N. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2. DR Pfam; PF00292; PAX; 1. DR PRINTS; PR00027; PAIREDBOX. DR SMART; SM00351; PAX; 1. DR PROSITE; PS00034; PAIRED_1; 1. DR PROSITE; PS51057; PAIRED_2; 1. KW Alternative splicing; Developmental protein; Differentiation; KW Disease mutation; DNA-binding; Nuclear protein; Paired box; KW Polymorphism; Transcription; Transcription regulation. FT CHAIN 1 416 Paired box protein Pax-2. FT /FTId=PRO_0000050175. FT DOMAIN 16 142 Paired. FT VAR_SEQ 206 228 Missing (in isoform 3). FT /FTId=VSP_002345. FT VAR_SEQ 364 416 GSEFSGNPYSHPQYTAYNEAWRFSNPALLSSPYYYSAAPRS FT APAARAAAYDRH -> EAAVGPSSSLMSKPGRKLAEVPPCV FT QPTGASSPATRTATPSTRPTTRLGDSATPPY (in FT isoform 2). FT /FTId=VSP_002346. FT VARIANT 39 40 Missing (in OMN; with bilateral FT coloboma). FT /FTId=VAR_012442. FT VARIANT 75 75 T -> TET (in RCS). FT /FTId=VAR_003788. FT VARIANT 76 76 G -> S (in RCS). FT /FTId=VAR_003789. FT VARIANT 334 334 A -> V. FT /FTId=VAR_012443. FT CONFLICT 15 16 PG -> R (in Ref. 3). SQ SEQUENCE 416 AA; 44734 MW; 88A42F5D8307F80E CRC64; MDMHCKADPF SAMHPGHGGV NQLGGVFVNG RPLPDVVRQR IVELAHQGVR PCDISRQLRV SHGCVSKILG RYYETGSIKP GVIGGSKPKV ATPKVVDKIA EYKRQNPTMF AWEIRDRLLA EGICDNDTVP SVSSINRIIR TKVQQPFHPT PDGAGTGVTA PGHTIVPSTA SPPVSSASND PVGSYSINGI LGIPRSNGEK RKRDEVEVYT DPAHIRGGGG LHLVWTLRDV SEGSVPNGDS QSGVDSLRKH LRADTFTQQQ LEALDRVFER PSYPDVFQAS EHIKSEQGNE YSLPALTPGL DEVKSSLSAS TNPELGSNVS GTQTYPVVTG RDMASTTLPG YPPHVPPTGQ GSYPTSTLAG MVPGSEFSGN PYSHPQYTAY NEAWRFSNPA LLSSPYYYSA APRSAPAARA AAYDRH // ID PAX3_HUMAN Reviewed; 479 AA. AC P23760; Q16448; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 20-MAR-2007, entry version 86. DE Paired box protein Pax-3 (HUP2). GN Name=PAX3; Synonyms=HUP2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29 AND 197-479. RX MEDLINE=95301273; PubMed=7782066; DOI=10.1016/0888-7543(95)80076-X; RA Macina R.A., Barr F.G., Galili N., Riethman H.C.; RT "Genomic organization of the human PAX3 gene: DNA sequence analysis of RT the region disrupted in alveolar rhabdomyosarcoma."; RL Genomics 26:1-8(1995). RN [2] RP NUCLEOTIDE SEQUENCE OF 30-195. RX MEDLINE=89305521; PubMed=2501086; RA Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.; RT "Conservation of the paired domain in metazoans and its structure in RT three isolated human genes."; RL EMBO J. 8:1183-1190(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 196-392, AND VARIANTS WS1 LEU-45 RP AND ASP-99. RX MEDLINE=95072569; PubMed=7981674; DOI=10.1093/hmg/3.7.1069; RA Tassabehji M., Newton V.E., Leverton K., Turnbull K., Seemanova E., RA Kunze J., Sperling K., Strachan T., Read A.P.; RT "PAX3 gene structure and mutations: close analogies between RT Waardenburg syndrome and the Splotch mouse."; RL Hum. Mol. Genet. 3:1069-1074(1994). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (PAX3A AND PAX3B). RX MEDLINE=94171226; PubMed=7545913; DOI=10.1007/BF00212021; RA Tsukamoto K., Nakamura Y., Niikawa N.; RT "Isolation of two isoforms of the PAX3 gene transcripts and their RT tissue-specific alternative expression in human adult tissues."; RL Hum. Genet. 93:270-274(1994). RN [5] RP NUCLEOTIDE SEQUENCE OF 1-319, AND CHROMOSOMAL TRANSLOCATION WITH RP NCOA1. RX PubMed=15313887; DOI=10.1158/0008-5472.CAN-04-0844; RA Wachtel M., Dettling M., Koscielniak E., Stegmaier S., Treuner J., RA Simon-Klingenstein K., Buehlmann P., Niggli F.K., Schaefer B.W.; RT "Gene expression signatures identify rhabdomyosarcoma subtypes and RT detect a novel t(2;2)(q35;p23) translocation fusing PAX3 to NCOA1."; RL Cancer Res. 64:5539-5545(2004). RN [6] RP NUCLEOTIDE SEQUENCE OF 56-74, AND VARIANT WS1 63-ALA--ILE-67 DEL. RX MEDLINE=92168113; PubMed=1347148; DOI=10.1038/355635a0; RA Tassabehji M., Read A.P., Newton V.E., Harris R., Balling R., RA Gruss P., Strachan T.; RT "Waardenburg's syndrome patients have mutations in the human homologue RT of the Pax-3 paired box gene."; RL Nature 355:635-636(1992). RN [7] RP NUCLEOTIDE SEQUENCE OF 265-319. RA Lalwani A.K., Ploplis B., Fex J., Grundfast K.M., San Agustin T.B., RA Wilcox E.R.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. RN [8] RP CHROMOSOMAL TRANSLOCATION WITH FOXO1A. RX MEDLINE=94100975; PubMed=8275086; DOI=10.1038/ng1193-230; RA Galili N., Davis R.J., Fredericks W.J., Mukhopadhyay S., RA Rauscher F.J. III, Emanuel B.S., Rovera G., Barr F.G.; RT "Fusion of a fork head domain gene to PAX3 in the solid tumour RT alveolar rhabdomyosarcoma."; RL Nat. Genet. 5:230-235(1993). RN [9] RP INTERACTION WITH DAXX. RX MEDLINE=99321757; PubMed=10393185; DOI=10.1093/emboj/18.13.3702; RA Hollenbach A.D., Sublett J.E., McPherson C.J., Grosveld G.; RT "The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated RT repressor hDaxx."; RL EMBO J. 18:3702-3711(1999). RN [10] RP INVOLVEMENT IN WS1. RX PubMed=1303193; DOI=10.1093/hmg/1.4.243; RA Morell R., Friedman T.B., Moeljopawiro S., Hartono S., Asher J.H. Jr.; RT "A frameshift mutation in the HuP2 paired domain of the probable human RT homolog of murine Pax-3 is responsible for Waardenburg syndrome type 1 RT in an Indonesian family."; RL Hum. Mol. Genet. 1:243-247(1992). RN [11] RP VARIANT WS1 LEU-50. RX MEDLINE=92168114; PubMed=1347149; DOI=10.1038/355637a0; RA Baldwin C.T., Hoth C.F., Amos J.A., Da-Silva E.O., Milunsky A.; RT "An exonic mutation in the HuP2 paired domain gene causes RT Waardenburg's syndrome."; RL Nature 355:637-638(1992). RN [12] RP VARIANT WS1 ALA-81. RX MEDLINE=93258399; PubMed=8490648; DOI=10.1038/ng0193-26; RA Tassabehji M., Read A.P., Newton V.E., Patton M., Gruss P., Harris R., RA Strachan T.; RT "Mutations in the PAX3 gene causing Waardenburg syndrome type 1 and RT type 2."; RL Nat. Genet. 3:26-30(1993). RN [13] RP VARIANTS WS3 HIS-47 AND WS1 LEU-56. RX MEDLINE=93190976; PubMed=8447316; RA Hoth C.F., Milunsky A., Lipsky N., Sheffer R., Clarren S.K., RA Baldwin C.T.; RT "Mutations in the paired domain of the human PAX3 gene cause Klein- RT Waardenburg syndrome (WS-III) as well as Waardenburg syndrome type I RT (WS-I)."; RL Am. J. Hum. Genet. 52:455-462(1993). RN [14] RP VARIANT WS1 VAL-62. RX MEDLINE=95135456; PubMed=7833953; RA Pierpont J.W., Doolan L.D., Amann K., Snead G.R., Erickson R.P.; RT "A single base pair substitution within the paired box of PAX3 in an RT individual with Waardenburg syndrome type 1 (WS1)."; RL Hum. Mutat. 4:227-228(1994). RN [15] RP VARIANTS WS1 PHE-265 AND GLY-271. RX MEDLINE=95126143; PubMed=7825605; RA Lalwani A.K., Brister J.R., Fex J., Grundfast K.M., Ploplis B., RA San Agustin T.B., Wilcox E.R.; RT "Further elucidation of the genomic structure of PAX3, and RT identification of two different point mutations within the PAX3 RT homeobox that cause Waardenburg syndrome type 1 in two families."; RL Am. J. Hum. Genet. 56:75-83(1995). RN [16] RP VARIANT WS3 PHE-84. RX MEDLINE=95243235; PubMed=7726174; RA Zlotogora J., Lerer I., Bar-David S., Ergaz Z., Abeliovich D.; RT "Homozygosity for Waardenburg syndrome."; RL Am. J. Hum. Genet. 56:1173-1178(1995). RN [17] RP VARIANTS WS1 MET-60; GLU-85 AND SER-238. RX MEDLINE=96042708; PubMed=8533800; RA Baldwin C.T., Hoth C.F., Macina R.A., Milunsky A.; RT "Mutations in PAX3 that cause Waardenburg syndrome type I: ten new RT mutations and review of the literature."; RL Am. J. Med. Genet. 58:115-122(1995). RN [18] RP VARIANTS WS1 MET-78; ALA-81; ASP-99; CYS-266; CYS-270; CYS-271 AND RP HIS-271, AND VARIANT LYS-315. RX MEDLINE=96154685; PubMed=8589691; DOI=10.1093/hmg/4.11.2131; RA Tassabehji M., Newton V.E., Liu X.-Z., Brady A., Donnai D., RA Krajewska-Walasek M., Murday V., Norman A., Obersztyn E., Reardon W., RA Rice J.C., Trembath R., Wieacker P., Whiteford M., Winter R., RA Read A.P.; RT "The mutational spectrum in Waardenburg syndrome."; RL Hum. Mol. Genet. 4:2131-2137(1995). RN [19] RP VARIANTS WS1 ARG-48; CYS-270 AND HIS-271, AND VARIANTS LYS-273 AND RP LYS-315. RX PubMed=8845842; DOI=10.1093/hmg/5.4.497; RA Pandya A., Xia X.-J., Landa B.L., Arnos K.S., Israel J., Lloyd J., RA James A.L., Diehl S.R., Blanton S.H., Nance W.E.; RT "Phenotypic variation in Waardenburg syndrome: mutational RT heterogeneity, modifier genes or polygenic background?"; RL Hum. Mol. Genet. 5:497-502(1996). RN [20] RP VARIANT CDHS LYS-47. RX MEDLINE=96263735; PubMed=8664898; RX DOI=10.1002/(SICI)1098-1004(1996)7:1<30::AID-HUMU4>3.3.CO;2-H; RA Asher J.H. Jr., Sommer A., Morell R., Friedman T.B.; RT "Missense mutation in the paired domain of PAX3 causes craniofacial- RT deafness-hand syndrome."; RL Hum. Mutat. 7:30-35(1996). RN [21] RP VARIANT LYS-315. RX MEDLINE=97016531; PubMed=8863157; RA Hol F.A., Geurds M.P.A., Chatkupt S., Shugart Y.Y., Balling R., RA Schrander-Stumpel C.T.R.M., Johnson W.G., Hamel B.C.J., RA Mariman E.C.M.; RT "PAX genes and human neural tube defects: an amino acid substitution RT in PAX1 in a patient with spina bifida."; RL J. Med. Genet. 33:655-660(1996). RN [22] RP VARIANT WS1 PHE-59. RX MEDLINE=97220597; PubMed=9067759; RX DOI=10.1002/(SICI)1098-1004(1997)9:2<177::AID-HUMU11>3.3.CO;2-Z; RA Soejima H., Fujimoto M., Tsukamoto K., Matsumoto N., Yoshiura K., RA Fukushima Y., Jinno Y., Niikawa N.; RT "Three novel PAX3 mutations observed in patients with Waardenburg RT syndrome type 1."; RL Hum. Mutat. 9:177-180(1997). RN [23] RP VARIANT WS1 VAL-62. RX MEDLINE=98112449; PubMed=9452070; RA Hol F.A., Geurds M.P.A., Cremers C.W.R.J., Hamel B.C.J., RA Mariman E.C.M.; RT "Identification of two PAX3 mutations causing Waardenburg syndrome, RT one within the paired domain (M62V) and the other downstream of the RT homeodomain (Q282X)."; RL Hum. Mutat. Suppl. 1:S145-S147(1998). RN [24] RP VARIANT WS1 HIS-391. RX MEDLINE=98200183; PubMed=9541113; RA Carey M.L., Friedman T.B., Asher J.H. Jr., Innis J.W.; RT "Septo-optic dysplasia and WS1 in the proband of a WS1 family RT segregating for a novel mutation in PAX3 exon 7."; RL J. Med. Genet. 35:248-250(1998). RN [25] RP VARIANT LYS-315. RX MEDLINE=98250826; PubMed=9584079; DOI=10.1006/mcpr.1997.0149; RA Wang C., Kim E., Attaie A., Smith T.N., Wilcox E.R., Lalwani A.K.; RT "A PAX3 polymorphism (T315K) in a family exhibiting Waardenburg RT syndrome type 2."; RL Mol. Cell. Probes 12:55-57(1998). RN [26] RP VARIANT WS1 ASN-59. RA Markova T.G., Shevtsov S.P., Moskolenko L.N., Lantsov A.A., RA Schwartz E.I.; RT "A novel missense mutation Ile59Asn in the PAX3 gene in a family with RT Waardenburg syndrome type I."; RL Hum. Mutat. 13:85-85(1999). RN [27] RP VARIANT WS3 CYS-270. RA Bottani A., Antonarakis S.E., Blouin J.-L.; RL Unpublished observations (MAY-1999). RN [28] RP VARIANT WS1 LEU-73. RX MEDLINE=20243823; PubMed=10779847; RX DOI=10.1076/1381-6810(200003)21:1;1-I;FT025; RA Sotirova V.N., Rezaie T.M., Khoshsorour M.M., Sarfarazi M.; RT "Identification of a novel mutation in the paired domain of PAX3 in an RT Iranian family with waardenburg syndrome type I."; RL Ophthalmic Genet. 21:25-28(2000). RN [29] RP VARIANT WS1 MET-60, AND VARIANT WS3 HIS-90. RX MEDLINE=22829208; PubMed=12949970; DOI=10.1002/ajmg.a.20260; RA Wollnik B., Tukel T., Uyguner O., Ghanbari A., Kayserili H., RA Emiroglu M., Yuksel-Apak M.; RT "Homozygous and heterozygous inheritance of PAX3 mutations causes RT different types of Waardenburg syndrome."; RL Am. J. Med. Genet. A 122:42-45(2003). CC -!- FUNCTION: Probable transcription factor associated with CC development of alveolar rhabdomyosarcoma. CC -!- SUBUNIT: Can bind to DNA as a heterodimer with PAX7. Interacts CC with DAXX. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Pax3; CC IsoId=P23760-1; Sequence=Displayed; CC Name=Pax3A; CC IsoId=P23760-2; Sequence=VSP_002355, VSP_002356; CC Name=Pax3B; CC IsoId=P23760-3; Sequence=VSP_002357, VSP_002358; CC -!- DISEASE: Defects in PAX3 are the cause of Waardenburg syndrome CC type I (WS1) [MIM:193500]. WS1 is an autosomal dominant disorder CC characterized by wide bridge of nose owing to lateral displacement CC of the inner canthus of each eye (dystopia canthorum), pigmentary CC disturbances such as frontal white blaze of hair, heterochromia of CC irides, white eyelashes, leukoderma and sensorineural deafness. CC The syndrome shows variable clinical expression and some affected CC individuals do not manifest hearing impairment. CC -!- DISEASE: Defects in PAX3 are the cause of Waardenburg syndrome CC type III (WS3) [MIM:148820]; also known as Klein-Waardenburg CC syndrome or Waardenburg syndrome with upper limb anomalies or CC white forelock with malformations. WS3 is a very rare autosomal CC dominant disorder, which shares many of the characteristics of CC WS1. Patients additionally present with musculoskeletal CC abnormalities. CC -!- DISEASE: Defects in PAX3 are the cause of craniofacial-deafness- CC hand syndrome (CDHS) [MIM:122880]. CDHS is thought to be an CC autosomal dominant disease which comprises absence or hypoplasia CC of the nasal bones, hypoplastic maxilla, small and short nose with CC thin nares, limited movement of the wrist, short palpebral CC fissures, ulnar deviation of the fingers, hypertelorism and CC profound sensory-neural deafness. CC -!- DISEASE: A chromosomal aberration involving PAX3 is a cause of CC rhabdomyosarcoma 2 (RMS2) [MIM:268220]; also known as alveolar CC rhabdomyosarcoma. Translocation (2;13)(q35;q14) with FOXO1A. The CC resulting protein is a transcriptional activator. CC -!- DISEASE: A chromosomal aberration involving PAX3 is a cause of CC rhabdomyosarcoma. Translocation t(2;2)(q35;p23) with NCOA1 CC generates the NCOA1-PAX3 oncogene consisting of the N-terminus CC part of PAX3 and the C-terminus part of NCOA1. The fusion protein CC acts as a transcriptional activator. Rhabdomyosarcoma is the most CC common soft tissue carcinoma in childhood, representing 5-8% of CC all malignancies in children. CC -!- SIMILARITY: Belongs to the paired homeobox family. CC -!- SIMILARITY: Contains 1 homeobox DNA-binding domain. CC -!- SIMILARITY: Contains 1 paired domain. CC -!- WEB RESOURCE: NAME=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/PAX3ID70ch2q35.html". CC -!- WEB RESOURCE: NAME=GeneReviews; CC URL="http://www.genetests.org/query?gene=PAX3". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U12263; AAA80573.1; -; Genomic_DNA. DR EMBL; U12259; AAA80574.1; -; Genomic_DNA. DR EMBL; U12258; AAA80574.1; JOINED; Genomic_DNA. DR EMBL; U12260; AAA80574.1; JOINED; Genomic_DNA. DR EMBL; U12262; AAA80574.1; JOINED; Genomic_DNA. DR EMBL; X15043; CAA33145.1; -; Genomic_DNA. DR EMBL; X15252; CAA33145.1; JOINED; Genomic_DNA. DR EMBL; X15253; CAA33145.1; JOINED; Genomic_DNA. DR EMBL; Z29972; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z29973; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z29974; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; S69369; AAB30167.1; -; mRNA. DR EMBL; S69370; AAB30168.1; -; mRNA. DR EMBL; S83614; AAB21476.1; -; Genomic_DNA. DR EMBL; L10614; AAA91849.1; -; Genomic_DNA. DR PIR; I54276; I54276. DR PIR; I68547; I68547. DR PIR; S06960; S06960. DR UniGene; Hs.42146; -. DR HSSP; P06601; 1FJL. DR SMR; P23760; 38-161, 218-277. DR TRANSFAC; T00679; -. DR TRANSFAC; T01812; -. DR TRANSFAC; T01813; -. DR Ensembl; ENSG00000135903; Homo sapiens. DR KEGG; hsa:5077; -. DR HGNC; HGNC:8617; PAX3. DR MIM; 122880; phenotype. DR MIM; 148820; phenotype. DR MIM; 193500; phenotype. DR MIM; 268220; phenotype. DR MIM; 606597; gene. DR LinkHub; P23760; -. DR ArrayExpress; P23760; -. DR GermOnline; ENSG00000135903; Homo sapiens. DR GO; GO:0003700; F:transcription factor activity; TAS:ProtInc. DR GO; GO:0006915; P:apoptosis; TAS:ProtInc. DR GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc. DR GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc. DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR012287; Homeodomain-rel. DR InterPro; IPR009057; Homeodomain_like. DR InterPro; IPR001523; Paired_box_N. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2. DR Pfam; PF00046; Homeobox; 1. DR Pfam; PF00292; PAX; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00027; PAIREDBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00351; PAX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00034; PAIRED_1; 1. DR PROSITE; PS51057; PAIRED_2; 1. KW Alternative splicing; Chromosomal rearrangement; Deafness; KW Developmental protein; Disease mutation; DNA-binding; Homeobox; KW Nuclear protein; Paired box; Polymorphism; Proto-oncogene; KW Transcription; Transcription regulation; Waardenburg syndrome. FT CHAIN 1 479 Paired box protein Pax-3. FT /FTId=PRO_0000050178. FT DOMAIN 34 161 Paired. FT DNA_BIND 219 278 Homeobox. FT SITE 319 320 Breakpoint for translocation to form FT PAX3-NCOA1 oncogene. FT VAR_SEQ 196 215 ASAPQSDEGSDIDSEPDLPL -> GKRWRLGRRTCWVTWRA FT SAS (in isoform Pax3A). FT /FTId=VSP_002355. FT VAR_SEQ 196 206 ASAPQSDEGSD -> GKALVSGVSSH (in isoform FT Pax3B). FT /FTId=VSP_002357. FT VAR_SEQ 207 479 Missing (in isoform Pax3B). FT /FTId=VSP_002358. FT VAR_SEQ 216 479 Missing (in isoform Pax3A). FT /FTId=VSP_002356. FT VARIANT 45 45 F -> L (in WS1). FT /FTId=VAR_003790. FT VARIANT 47 47 N -> H (in WS3). FT /FTId=VAR_003791. FT VARIANT 47 47 N -> K (in CDHS). FT /FTId=VAR_003792. FT VARIANT 48 48 G -> R (in WS1). FT /FTId=VAR_017533. FT VARIANT 50 50 P -> L (in WS1; important hearing loss). FT /FTId=VAR_003793. FT VARIANT 56 56 R -> L (in WS1; associated with FT meningomyelocele). FT /FTId=VAR_003794. FT VARIANT 59 59 I -> F (in WS1). FT /FTId=VAR_003795. FT VARIANT 59 59 I -> N (in WS1). FT /FTId=VAR_003796. FT VARIANT 60 60 V -> M (in WS1). FT /FTId=VAR_003797. FT VARIANT 62 62 M -> V (in WS1). FT /FTId=VAR_003798. FT VARIANT 63 67 Missing (in WS1). FT /FTId=VAR_003799. FT VARIANT 73 73 S -> L (in WS1). FT /FTId=VAR_013640. FT VARIANT 78 78 V -> M (in WS1). FT /FTId=VAR_017534. FT VARIANT 81 81 G -> A (in WS1; originally classified as FT Waardenburg syndrome type 2). FT /FTId=VAR_003800. FT VARIANT 84 84 S -> F (in WS3). FT /FTId=VAR_003801. FT VARIANT 85 85 K -> E (in WS1). FT /FTId=VAR_003802. FT VARIANT 90 90 Y -> H (in WS3). FT /FTId=VAR_017535. FT VARIANT 99 99 G -> D (in WS1). FT /FTId=VAR_003803. FT VARIANT 238 238 F -> S (in WS1). FT /FTId=VAR_003804. FT VARIANT 265 265 V -> F (in WS1). FT /FTId=VAR_003805. FT VARIANT 266 266 W -> C (in WS1). FT /FTId=VAR_017536. FT VARIANT 270 270 R -> C (in WS1 and WS3). FT /FTId=VAR_013619. FT VARIANT 271 271 R -> C (in WS1). FT /FTId=VAR_017537. FT VARIANT 271 271 R -> G (in WS1). FT /FTId=VAR_003806. FT VARIANT 271 271 R -> H (in WS1; associated with Lys-273 FT in one family). FT /FTId=VAR_017538. FT VARIANT 273 273 R -> K (associated with His-271 in one FT Waardenburg syndrome type I family). FT /FTId=VAR_017539. FT VARIANT 315 315 T -> K (in dbSNP:rs2234675). FT /FTId=VAR_003807. FT VARIANT 391 391 Q -> H (in WS1). FT /FTId=VAR_013641. FT CONFLICT 108 108 Missing (in Ref. 5). SQ SEQUENCE 479 AA; 52968 MW; 8AFCA674E3ACB4FE CRC64; MTTLAGAVPR MMRPGPGQNY PRSGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPKQVT TPDVEKKIEE YKRENPGMFS WEIRDKLLKD AVCDRNTVPS VSSISRILRS KFGKGEEEEA DLERKEAEES EKKAKHSIDG ILSERASAPQ SDEGSDIDSE PDLPLKRKQR RSRTTFTAEQ LEELERAFER THYPDIYTRE ELAQRAKLTE ARVQVWFSNR RARWRKQAGA NQLMAFNHLI PGGFPPTAMP TLPTYQLSET SYQPTSIPQA VSDPSSTVHR PQPLPPSTVH QSTIPSNPDS SSAYCLPSTR HGFSSYTDSF VPPSGPSNPM NPTIGNGLSP QVMGLLTNHG GVPHQPQTDY ALSPLTGGLE PTTTVSASCS QRLDHMKSLD SLPTSQSYCP PTYSTTGYSM DPVTGYQYGQ YGQSKPWTF // ID PAX4_HUMAN Reviewed; 350 AA. AC O43316; O95161; Q6B0H0; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 20-FEB-2007, entry version 61. DE Paired box protein Pax-4. GN Name=PAX4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98102804; PubMed=9439631; DOI=10.1006/bbrc.1997.7935; RA Matsushita T., Yamaoka T., Otsuka S., Moritani M., Matsumoto T., RA Itakura M.; RT "Molecular cloning of mouse paired-box-containing gene (Pax-4) from an RT islet beta cell line and deduced sequence of human Pax-4."; RL Biochem. Biophys. Res. Commun. 242:176-180(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Placenta; RX MEDLINE=98424228; PubMed=9753306; RA Tao T., Wasson J., Bernal-Mizrachi E., Behn P.S., Chayen S., RA Duprat L., Meyer J., Glaser B., Permutt M.A.; RT "Isolation and characterization of the human PAX4 gene."; RL Diabetes 47:1650-1653(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP ALTERNATIVE SPLICING (ISOFORM PAX4V). RC TISSUE=Insulinoma; RX MEDLINE=21164695; PubMed=11263967; DOI=10.1006/bbrc.2001.4552; RA Miyamoto T., Kakizawa T., Ichikawa K., Nishio S., Kajikawa S., RA Hashizume K.; RT "Expression of dominant negative form of PAX4 in human insulinoma."; RL Biochem. Biophys. Res. Commun. 282:34-40(2001). CC -!- FUNCTION: Plays an important role in the differentiation and CC development of pancreatic islet beta cells. Transcriptional CC repressor that binds to a common element in the glucagon, insulin CC and somatostatin promoters. Competes with PAX6 for this same CC promoter binding site. The Pax4v isoform appears to be a dominant CC negative form antagonizing PAX4 transcriptional activity. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Pax4; CC IsoId=O43316-1; Sequence=Displayed; CC Name=Pax4V; CC IsoId=O43316-2; Sequence=VSP_002359, VSP_002360; CC Name=3; CC IsoId=O43316-3; Sequence=VSP_012925; CC -!- SIMILARITY: Belongs to the paired homeobox family. CC -!- SIMILARITY: Contains 1 homeobox DNA-binding domain. CC -!- SIMILARITY: Contains 1 paired domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB008913; BAA24506.1; -; mRNA. DR EMBL; AF043978; AAD02289.1; ALT_INIT; mRNA. DR EMBL; BC074761; AAH74761.1; ALT_INIT; mRNA. DR PIR; JC5828; JC5828. DR UniGene; Hs.129706; -. DR HSSP; P26367; 6PAX. DR SMR; O43316; 7-135. DR TRANSFAC; T02982; -. DR KEGG; hsa:5078; -. DR HGNC; HGNC:8618; PAX4. DR MIM; 167413; gene. DR ArrayExpress; O43316; -. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. DR GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR012287; Homeodomain-rel. DR InterPro; IPR009057; Homeodomain_like. DR InterPro; IPR001523; Paired_box_N. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2. DR Pfam; PF00046; Homeobox; 1. DR Pfam; PF00292; PAX; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00027; PAIREDBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00351; PAX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00034; PAIRED_1; 1. DR PROSITE; PS51057; PAIRED_2; 1. KW Alternative splicing; Developmental protein; Differentiation; KW DNA-binding; Homeobox; Nuclear protein; Paired box; Repressor; KW Transcription; Transcription regulation. FT CHAIN 1 350 Paired box protein Pax-4. FT /FTId=PRO_0000050180. FT DOMAIN 5 131 Paired. FT DNA_BIND 170 229 Homeobox. FT REGION 278 350 Transcription repression. FT VAR_SEQ 239 257 Missing (in isoform Pax4V). FT /FTId=VSP_002359. FT VAR_SEQ 258 350 QSPGSVPTAALPALEPLGPSCYQLCWATAPERCLSDTPPKA FT CLKPCWDCGSFLLPVIAPSCVDVAWPCLDASLAHHLIGGAG FT KATPTHFSHWP -> AVPWQCAHSSPACPGTTGSLLLSAVL FT GNSTRKVSE (in isoform Pax4V). FT /FTId=VSP_002360. FT VAR_SEQ 305 350 DCGSFLLPVIAPSCVDVAWPCLDASLAHHLIGGAGKATPTH FT FSHWP -> GHLPPQPNSLDSGLLCLPCPSSHCPLASLSGS FT QALLWPGCPLLYGLE (in isoform 3). FT /FTId=VSP_012925. SQ SEQUENCE 350 AA; 37833 MW; 2C2343AF16AEAAAC CRC64; MHQDGISSMN QLGGLFVNGR PLPLDTRQQI VRLAVSGMRP CDISRILKVS NGCVSKILGR YYRTGVLEPK GIGGSKPRLA TPPVVARIAQ LKGECPALFA WEIQRQLCAE GLCTQDKTPS VSSINRVLRA LQEDQGLPCT RLRSPAVLAP AVLTPHSGSE TPRGTHPGTG HRNRTIFSPS QAEALEKEFQ RGQYPDSVAR GKLATATSLP EDTVRVWFSN RRAKWRRQEK LKWEMQLPGA SQGLTVPRVA PGIISAQQSP GSVPTAALPA LEPLGPSCYQ LCWATAPERC LSDTPPKACL KPCWDCGSFL LPVIAPSCVD VAWPCLDASL AHHLIGGAGK ATPTHFSHWP // ID PAX5_HUMAN Reviewed; 391 AA. AC Q02548; O75933; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 20-MAR-2007, entry version 65. DE Paired box protein Pax-5 (B-cell-specific transcription factor) DE (BSAP). GN Name=PAX5; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92387536; PubMed=1516825; RA Adams B., Doerfler P., Aguzzi A., Kozmik Z., Urbanek P., RA Maurer-Fogy I., Busslinger M.; RT "Pax-5 encodes the transcription factor BSAP and is expressed in B RT lymphocytes, the developing CNS, and adult testis."; RL Genes Dev. 6:1589-1607(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 62-197. RX MEDLINE=98416211; PubMed=9742255; DOI=10.1093/nar/26.19.4497; RA Verkoczy L.K., Berinstein N.L.; RT "Isolation of genes negatively or positively co-expressed with human RT recombination activating gene 1 (RAG1) by differential display PCR (DD RT RT-PCR)."; RL Nucleic Acids Res. 26:4497-4507(1998). RN [3] RP INTERACTION WITH TLE4. RX MEDLINE=20271869; PubMed=10811620; DOI=10.1093/emboj/19.10.2292; RA Eberhard D., Jimenez G., Heavey B., Busslinger M.; RT "Transcriptional repression by Pax5 (BSAP) through interaction with RT corepressors of the Groucho family."; RL EMBO J. 19:2292-2303(2000). CC -!- FUNCTION: May play an important role in B-cell differentiation as CC well as neural development and spermatogenesis. Involved in the CC regulation of the CD19 gene, a B-lymphoid-specific target gene. CC -!- SUBUNIT: Interacts with DAXX (By similarity). Binds DNA as a CC monomer. Binds TLE4. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- DEVELOPMENTAL STAGE: Expressed at early B-cell differentiation, in CC the developing CNS and in adult testis. CC -!- PTM: O-glycosylated (Probable). CC -!- SIMILARITY: Contains 1 paired domain. CC -!- WEB RESOURCE: NAME=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/PAX5ID62.htm". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M96944; AAA58397.1; -; mRNA. DR EMBL; AF080573; AAC35286.1; -; mRNA. DR PIR; A44063; A44063. DR UniGene; Hs.591091; -. DR PDB; 1K78; X-ray; A/E/I=1-149. DR PDB; 1MDM; X-ray; A=1-149. DR IntAct; Q02548; -. DR TRANSFAC; T00070; -. DR Ensembl; ENSG00000196092; Homo sapiens. DR KEGG; hsa:5079; -. DR HGNC; HGNC:8619; PAX5. DR HPA; CAB001449; -. DR MIM; 167414; gene. DR LinkHub; Q02548; -. DR ArrayExpress; Q02548; -. DR GermOnline; ENSG00000196092; Homo sapiens. DR GO; GO:0006959; P:humoral immune response; TAS:ProtInc. DR GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc. DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. DR InterPro; IPR009057; Homeodomain_like. DR InterPro; IPR001523; Paired_box_N. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2. DR Pfam; PF00292; PAX; 1. DR PRINTS; PR00027; PAIREDBOX. DR SMART; SM00351; PAX; 1. DR PROSITE; PS00034; PAIRED_1; 1. DR PROSITE; PS51057; PAIRED_2; 1. KW 3D-structure; Developmental protein; Differentiation; DNA-binding; KW Glycoprotein; Neurogenesis; Nuclear protein; Paired box; KW Spermatogenesis; Transcription; Transcription regulation. FT CHAIN 1 391 Paired box protein Pax-5. FT /FTId=PRO_0000050183. FT DOMAIN 16 142 Paired. FT CONFLICT 99 99 I -> F (in Ref. 2). FT CONFLICT 141 143 TKV -> PKL (in Ref. 2). FT HELIX 35 46 FT HELIX 51 58 FT HELIX 62 75 FT STRAND 89 91 FT HELIX 93 105 FT HELIX 111 120 FT TURN 126 128 FT HELIX 132 140 SQ SEQUENCE 391 AA; 42149 MW; DB37E6EACD9F993A CRC64; MDLEKNYPTP RTSRTGHGGV NQLGGVFVNG RPLPDVVRQR IVELAHQGVR PCDISRQLRV SHGCVSKILG RYYETGSIKP GVIGGSKPKV ATPKVVEKIA EYKRQNPTMF AWEIRDRLLA ERVCDNDTVP SVSSINRIIR TKVQQPPNQP VPASSHSIVS TGSVTQVSSV STDSAGSSYS ISGILGITSP SADTNKRKRD EGIQESPVPN GHSLPGRDFL RKQMRGDLFT QQQLEVLDRV FERQHYSDIF TTTEPIKPEQ TTEYSAMASL AGGLDDMKAN LASPTPADIG SSVPGPQSYP IVTGRDLAST TLPGYPPHVP PAGQGSYSAP TLTGMVPGSE FSGSPYSHPQ YSSYNDSWRF PNPGLLGSPY YYSAAARGAA PPAAATAYDR H // ID PAX6_HUMAN Reviewed; 422 AA. AC P26367; Q6N006; Q99413; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 20-MAR-2007, entry version 91. DE Paired box protein Pax-6 (Oculorhombin) (Aniridia type II protein). GN Name=PAX6; Synonyms=AN2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=92103673; PubMed=1684738; DOI=10.1016/0092-8674(91)90284-6; RA Ton C.C.T., Hirvonen H., Miwa H., Weil M.M., Monaghan P., Jordan T., RA van Heyningen V., Hastie N.D., Meijers-Heijboer H., Drechsler M., RA Royer-Pokora B., Collins F.S., Swaroop A., Strong L.C., Saunders G.F.; RT "Positional cloning and characterization of a paired box- and RT homeobox-containing gene from the aniridia region."; RL Cell 67:1059-1074(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=94258210; PubMed=1345175; DOI=10.1038/ng1192-232; RA Glaser T., Walton D.S., Maas R.L.; RT "Genomic structure, evolutionary conservation and aniridia mutations RT in the human PAX6 gene."; RL Nat. Genet. 2:232-239(1992). RN [3] RP NUCLEOTIDE SEQUENCE (ISOFORM PAX6). RA Liu J., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5A). RC TISSUE=Cerebellum; RG The German cDNA consortium; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 5A). RA Wilkinson J.; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP ALTERNATIVE SPLICING, AND DNA-BINDING. RX MEDLINE=95047352; PubMed=7958875; RA Epstein J.A., Glaser T., Cai J., Jepeal L., Walton D.S., Maas R.L.; RT "Two independent and interactive DNA-binding subdomains of the Pax6 RT paired domain are regulated by alternative splicing."; RL Genes Dev. 8:2022-2034(1994). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 4-136. RX PubMed=10346815; RA Xu H.E., Rould M.A., Xu W., Epstein J.A., Maas R.L., Pabo C.O.; RT "Crystal structure of the human Pax-6 paired domain-DNA complex RT reveals specific roles for the linker region and carboxyl-terminal RT subdomain in DNA binding."; RL Genes Dev. 13:1263-1275(1999). RN [9] RP REVIEW ON VARIANTS. RX MEDLINE=98141676; PubMed=9482572; RX DOI=10.1002/(SICI)1098-1004(1998)11:2<93::AID-HUMU1>3.3.CO;2-J; RA Prosser J., van Heyningen V.; RT "PAX6 mutations reviewed."; RL Hum. Mutat. 11:93-108(1998). RN [10] RP VARIANT AN2 TRP-208. RX MEDLINE=93372853; PubMed=8364574; DOI=10.1093/hmg/2.7.915; RA Hanson I.M., Seawright A., Hardman K., Hodgson S., Zaletayev D., RA Fekete G., van Heyningen V.; RT "PAX6 mutations in aniridia."; RL Hum. Mol. Genet. 2:915-920(1993). RN [11] RP VARIANT PETERS ANOMALY GLY-26. RX MEDLINE=94214497; PubMed=8162071; DOI=10.1038/ng0294-168; RA Hanson I.M., Fletcher J.M., Jordan T., Brown A., Taylor D., RA Adams R.J., Punnet H.H., van Heyningen V.; RT "Mutations at the PAX6 locus are found in heterogeneous anterior RT segment malformations including Peters' anomaly."; RL Nat. Genet. 6:168-173(1994). RN [12] RP VARIANTS FOVEAL HYPOPLASIA CYS-125 AND CYS-128. RX MEDLINE=96225435; PubMed=8640214; DOI=10.1038/ng0696-141; RA Azuma N., Nishina S., Yanagisawa H., Okuyama T., Yamada M.; RT "PAX6 missense mutation in isolated foveal hypoplasia."; RL Nat. Genet. 13:141-142(1996). RN [13] RP VARIANT AN2 ARG-87, AND VARIANT GLY-26. RX MEDLINE=97227282; PubMed=9147640; DOI=10.1093/hmg/6.3.381; RA Tang H.K., Chao L.-Y., Saunders G.F.; RT "Functional analysis of paired box missense mutations in the PAX6 RT gene."; RL Hum. Mol. Genet. 6:381-386(1997). RN [14] RP VARIANT AN2 22-PRO--ARG-26 DEL. RX MEDLINE=97428347; PubMed=9281415; DOI=10.1006/mcpr.1997.0117; RA Axton R., Hanson I.M., Love J., Seawright A., Prosser J., RA van Heyningen V.; RT "Combined SSCP/heteroduplex analysis in the screening for PAX6 RT mutations."; RL Mol. Cell. Probes 11:287-292(1997). RN [15] RP VARIANT AN2 TRP-18. RX MEDLINE=99006892; PubMed=9792406; RX DOI=10.1002/(SICI)1098-1004(1998)12:5<304::AID-HUMU3>3.3.CO;2-Y; RA Wolf M.T.F., Lorenz B., Winterpacht A., Drechsler M., Schumacher V., RA Royer-Pokora B., Blankenagel A., Zabel B., Wildhardt G.; RT "Ten novel mutations found in Aniridia."; RL Hum. Mutat. 12:304-313(1998). RN [16] RP VARIANT EYE MALFORMATIONS ARG-422. RX MEDLINE=98199717; PubMed=9538891; RA Azuma N., Yamada M.; RT "Missense mutation at the C-terminus of the PAX6 gene in ocular RT anterior segment anomalies."; RL Invest. Ophthalmol. Vis. Sci. 39:828-830(1998). RN [17] RP VARIANTS AN2 SER-17; VAL-29; GLN-44 AND HIS-178. RX MEDLINE=99072581; PubMed=9856761; RA Azuma N., Hotta Y., Tanaka H., Yamada M.; RT "Missense mutations in the PAX6 gene in aniridia."; RL Invest. Ophthalmol. Vis. Sci. 39:2524-2528(1998). RN [18] RP VARIANT EYE MALFORMATIONS ASP-53. RX MEDLINE=99375017; PubMed=10441571; DOI=10.1086/302529; RA Azuma N., Yamaguchi Y., Handa H., Hayakawa M., Kanai A., Yamada M.; RT "Missense mutation in the alternative splice region of the PAX6 gene RT in eye anomalies."; RL Am. J. Hum. Genet. 65:656-663(1999). RN [19] RP ALTERNATIVE SPLICING, AND VARIANTS AN2 SER-42; LEU-53; PRO-63; GLU-79 RP AND GLN-208. RX MEDLINE=99250762; PubMed=10234503; DOI=10.1038/sj.ejhg.5200308; RA Groenskov K., Rosenberg T., Sand A., Broendum-Nielsen K.; RT "Mutational analysis of PAX6: 16 novel mutations including 5 missense RT mutations with a mild aniridia phenotype."; RL Eur. J. Hum. Genet. 7:274-286(1999). RN [20] RP VARIANTS AN2 PRO-33 AND PRO-43, VARIANT FOVEAL HYPOPLASIA VAL-64, AND RP VARIANT ECTOPIA PUPILLAE ASP-126. RX MEDLINE=99135896; PubMed=9931324; DOI=10.1093/hmg/8.2.165; RA Hanson I.M., Churchill A., Love J., Axton R., Moore T., Clarke M., RA Meire F., van Heyningen V.; RT "Missense mutations in the most ancient residues of the PAX6 paired RT domain underlie a spectrum of human congenital eye malformations."; RL Hum. Mol. Genet. 8:165-172(1999). RN [21] RP VARIANTS AN2 SER-29; ARG-119 AND ALA-353. RA Wildhardt G.; RL Unpublished observations (APR-1999). RN [22] RP VARIANT AN2 37-ALA--PRO-39 DEL. RA Saunders G.F.; RL Unpublished observations (AUG-1999). RN [23] RP VARIANT NYSTAGMUS ARG-118. RX MEDLINE=20410622; PubMed=10955655; DOI=10.1007/s004170000124; RA Sonoda S., Isashiki Y., Tabata Y., Kimura K., Kakiuchi T., Ohba N.; RT "A novel PAX6 gene mutation (P118R) in a family with congenital RT nystagmus associated with a variant form of aniridia."; RL Graefes Arch. Clin. Exp. Ophthalmol. 238:552-558(2000). RN [24] RP VARIANTS AN2 GLN-375 AND ARG-422. RX MEDLINE=21205761; PubMed=11309364; DOI=10.1093/hmg/10.9.911; RA Singh S., Chao L.-Y., Mishra R., Davies J., Saunders G.F.; RT "Missense mutation at the C-terminus of PAX6 negatively modulates RT homeodomain function."; RL Hum. Mol. Genet. 10:911-918(2001). RN [25] RP VARIANT MORNING GLORY DISK ANOMALY SER-68, VARIANT OCULAR COLOBOMA RP SER-258, VARIANT PETERS ANOMALY PRO-363, AND VARIANTS OPTIC NERVE RP HYPOPLASIA/APLASIA ILE-292; ARG-378; VAL-381 AND ALA-391. RX MEDLINE=22633032; PubMed=12721955; DOI=10.1086/375555; RA Azuma N., Yamaguchi Y., Handa H., Tadokoro K., Asaka A., Kawase E., RA Yamada M.; RT "Mutations of the PAX6 gene detected in patients with a variety of RT optic-nerve malformations."; RL Am. J. Hum. Genet. 72:1565-1570(2003). CC -!- FUNCTION: Transcription factor with important functions in the CC development of the eye, nose, central nervous system and pancreas. CC Required for the differentiation of pancreatic islet alpha cells CC (By similarity). Competes with PAX4 in binding to a common element CC in the glucagon, insulin and somatostatin promoters (By CC similarity). Isoform 5a appears to function as a molecular switch CC that specifies target genes. CC -!- INTERACTION: CC P63168:Dynll1 (xeno); NbExp=2; IntAct=EBI-747278, EBI-349121; CC Q9NSC5:HOMER3; NbExp=2; IntAct=EBI-747278, EBI-748420; CC Q96F44:TRIM11; NbExp=2; IntAct=EBI-747278, EBI-851809; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P26367-1; Sequence=Displayed; CC Name=5a; Synonyms=Pax6-5a; CC IsoId=P26367-2; Sequence=VSP_002366; CC Name=3; Synonyms=Pax6-5A,6*; CC IsoId=P26367-3; Sequence=Not described; CC -!- TISSUE SPECIFICITY: Fetal eye, brain, spinal cord and olfactory CC epithelium. Isoform 5a is less abundant than the PAX6 shorter CC form. CC -!- DEVELOPMENTAL STAGE: Expressed in the developing eye and brain. CC -!- DISEASE: Defects in PAX6 are the cause of aniridia type II (AN2) CC [MIM:106210]. AN2 is a bilateral panocular disorder characterized CC by complete or partial absence of the iris, absence of the fovea CC and malformations of the lens and anterior chamber. Severe age- CC related corneal degeneration is a frequent complication which CC contributes to a poor visual prognostis in aniridia. About one CC third of the cases are sporadic, and two thirds are familial, with CC autosomal dominant inheritance and high penetrance. Nearly one CC third of sporadic AN patients develop Wilms tumor in association CC with genitourinary anomalies and mental retardation (WAGR CC syndrome) as a consequence of heterozygous (sub)microscopic CC deletions of chromosome 11p13. CC -!- DISEASE: Defects in PAX6 are a cause of Peters anomaly CC [MIM:604229]. Peters anomaly consists of a central corneal CC leukoma, absence of the posterior corneal stroma and Descemet CC membrane, and a variable degree of iris and lenticular attachments CC to the central aspect of the posterior cornea. CC -!- DISEASE: Defects in PAX6 are a cause of ectopia pupillae CC [MIM:129750]. It is a congenital eye malformation in which the CC pupils are displaced from their normal central position. CC -!- DISEASE: Defects in PAX6 are a cause of foveal hypoplasia CC [MIM:136520]. Foveal hypoplasia can be isolated or associated with CC presenile cataract. Inheritance is autosomal dominant. CC -!- DISEASE: Defects in PAX6 are a cause of autosomal dominant CC keratitis [MIM:148190]. It is an eye disorder characterized by CC corneal opacification and vascularization, and by foveal CC hypoplasia. CC -!- DISEASE: Defects in PAX6 are a cause of ocular coloboma CC [MIM:120200]; also known as uveoretinal coloboma or coloboma of CC iris, choroid and retina. Ocular colobomas are a set of CC malformations resulting from abnormal morphogenesis of the optic CC cup and stalk, and the fusion of the fetal fissure (optic CC fissure). Severe colobomatous malformations may cause as much as CC 10% of the childhood blindness. The clinical presentation of CC ocular coloboma is variable. Some individuals may present with CC minimal defects in the anterior iris leaf without other ocular CC defects. More complex malformations create a combination of iris, CC uveoretinal and/or optic nerve defects without or with CC microphthalmia or even anophthalmia. CC -!- DISEASE: Defects in PAX6 are a cause of coloboma of optic nerve CC [MIM:120430]. CC -!- DISEASE: Defects in PAX6 are a cause of bilateral optic nerve CC hypoplasia [MIM:165550]; also known as bilateral optic nerve CC aplasia. Inheritance is autosomal dominant. CC -!- SIMILARITY: Belongs to the paired homeobox family. CC -!- SIMILARITY: Contains 1 homeobox DNA-binding domain. CC -!- SIMILARITY: Contains 1 paired domain. CC -!- WEB RESOURCE: NAME=Human PAX6 allelic variant database web site; CC URL="http://pax6.hgu.mrc.ac.uk/". CC -!- WEB RESOURCE: NAME=GeneReviews; CC URL="http://www.genetests.org/query?gene=PAX6". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M77844; AAA59963.1; -; mRNA. DR EMBL; M77844; AAA59962.1; -; mRNA. DR EMBL; M93650; AAA36416.1; -; mRNA. DR EMBL; AY047583; AAK95849.1; -; mRNA. DR EMBL; BX640762; CAE45868.1; -; mRNA. DR EMBL; Z95332; CAG38363.1; -; Genomic_DNA. DR EMBL; Z83307; CAG38363.1; JOINED; Genomic_DNA. DR EMBL; Z83307; CAG38087.1; -; Genomic_DNA. DR EMBL; Z95332; CAG38087.1; JOINED; Genomic_DNA. DR EMBL; BC011953; AAH11953.1; -; mRNA. DR PIR; A56674; A56674. DR UniGene; Hs.591993; -. DR PDB; 2CUE; NMR; A=211-277. DR PDB; 6PAX; X-ray; A=4-136. DR IntAct; P26367; -. DR TRANSFAC; T01122; -. DR TRANSFAC; T01814; -. DR Ensembl; ENSG00000007372; Homo sapiens. DR KEGG; hsa:5080; -. DR H-InvDB; HIX0009529; -. DR HGNC; HGNC:8620; PAX6. DR MIM; 106210; phenotype. DR MIM; 120200; phenotype. DR MIM; 120430; phenotype. DR MIM; 129750; phenotype. DR MIM; 136520; phenotype. DR MIM; 148190; phenotype. DR MIM; 165550; phenotype. DR MIM; 604229; phenotype. DR MIM; 607108; gene. DR ArrayExpress; P26367; -. DR GermOnline; ENSG00000007372; Homo sapiens. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0003700; F:transcription factor activity; TAS:ProtInc. DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc. DR GO; GO:0001654; P:eye development; TAS:ProtInc. DR GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR012287; Homeodomain-rel. DR InterPro; IPR009057; Homeodomain_like. DR InterPro; IPR001523; Paired_box_N. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2. DR Pfam; PF00046; Homeobox; 1. DR Pfam; PF00292; PAX; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00027; PAIREDBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00351; PAX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00034; PAIRED_1; 1. DR PROSITE; PS51057; PAIRED_2; 1. KW 3D-structure; Alternative splicing; Developmental protein; KW Differentiation; Disease mutation; DNA-binding; Homeobox; KW Nuclear protein; Paired box; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 422 Paired box protein Pax-6. FT /FTId=PRO_0000050185. FT DOMAIN 4 130 Paired. FT DNA_BIND 210 269 Homeobox. FT COMPBIAS 131 209 Gln/Gly-rich. FT COMPBIAS 279 422 Pro/Ser/Thr-rich. FT VAR_SEQ 47 47 Q -> QTHADAKVQVLDNQN (in isoform 5a). FT /FTId=VSP_002366. FT VARIANT 17 17 N -> S (in AN2). FT /FTId=VAR_003808. FT VARIANT 18 18 G -> W (in AN2 and Peters anomaly). FT /FTId=VAR_003809. FT VARIANT 22 26 Missing (in AN2; sporadic form). FT /FTId=VAR_008693. FT VARIANT 26 26 R -> G (in Peters anomaly). FT /FTId=VAR_003810. FT VARIANT 29 29 I -> S (in AN2; sporadic form). FT /FTId=VAR_008694. FT VARIANT 29 29 I -> V (in AN2). FT /FTId=VAR_003811. FT VARIANT 33 33 A -> P (in AN2; sporadic form). FT /FTId=VAR_008695. FT VARIANT 37 39 Missing (in AN2; sporadic form). FT /FTId=VAR_008696. FT VARIANT 42 42 I -> S (in AN2; mild). FT /FTId=VAR_008697. FT VARIANT 43 43 S -> P (in AN2; sporadic form). FT /FTId=VAR_008698. FT VARIANT 44 44 R -> Q (in AN2). FT /FTId=VAR_003812. FT VARIANT 53 53 V -> D (in Peters anomaly, congenital FT cataract and foveal hypoplasia; Japanese FT pedigrees). FT /FTId=VAR_008700. FT VARIANT 53 53 V -> L (in AN2; mild). FT /FTId=VAR_008699. FT VARIANT 63 63 T -> P (in AN2; mild). FT /FTId=VAR_008701. FT VARIANT 64 64 G -> V (in foveal hypoplasia; associated FT with presenile cataract syndrome). FT /FTId=VAR_008702. FT VARIANT 68 68 P -> S (in morning glory disk anomaly; FT significant impairment of transcriptional FT activation ability). FT /FTId=VAR_017540. FT VARIANT 79 79 A -> E (in AN2; mild). FT /FTId=VAR_008703. FT VARIANT 87 87 I -> R (in AN2; loss of activity). FT /FTId=VAR_003813. FT VARIANT 118 118 P -> R (in nystagmus associated with a FT variant form of aniridia). FT /FTId=VAR_015065. FT VARIANT 119 119 S -> R (in AN2; sporadic form). FT /FTId=VAR_008704. FT VARIANT 125 125 R -> C (in foveal hypoplasia; isolated). FT /FTId=VAR_017541. FT VARIANT 126 126 V -> D (in ectopia pupillae). FT /FTId=VAR_008705. FT VARIANT 128 128 R -> C (in foveal hypoplasia; isolated). FT /FTId=VAR_003814. FT VARIANT 178 178 Q -> H (in AN2). FT /FTId=VAR_003815. FT VARIANT 208 208 R -> Q (in AN2; mild). FT /FTId=VAR_008706. FT VARIANT 208 208 R -> W (in AN2). FT /FTId=VAR_003816. FT VARIANT 258 258 F -> S (in ocular coloboma; significant FT impairment of transcriptional activation FT ability). FT /FTId=VAR_017542. FT VARIANT 292 292 S -> I (in bilateral optic nerve FT hypoplasia; significant impairment of FT transcriptional activation ability). FT /FTId=VAR_017543. FT VARIANT 353 353 S -> A (in AN2; familial form). FT /FTId=VAR_008707. FT VARIANT 363 363 S -> P (in Peters anomaly). FT /FTId=VAR_017544. FT VARIANT 375 375 P -> Q (in AN2; reduced DNA binding FT ability). FT /FTId=VAR_015066. FT VARIANT 378 378 Q -> R (in optic nerve aplasia). FT /FTId=VAR_017545. FT VARIANT 381 381 M -> V (in bilateral optic nerve FT hypoplasia). FT /FTId=VAR_017546. FT VARIANT 391 391 T -> A (in bilateral optic nerve FT aplasia). FT /FTId=VAR_017547. FT VARIANT 422 422 Q -> R (in AN2 and ocular anterior FT segment anomalies; loss of DNA binding FT ability). FT /FTId=VAR_008708. FT CONFLICT 317 317 R -> L (in Ref. 1). FT CONFLICT 369 369 Y -> C (in Ref. 4). FT STRAND 6 8 FT STRAND 14 16 FT HELIX 23 34 FT HELIX 39 46 FT HELIX 50 63 FT STRAND 77 79 FT HELIX 81 93 FT HELIX 99 108 FT TURN 114 116 FT HELIX 120 133 FT HELIX 219 229 FT HELIX 237 246 FT HELIX 251 275 SQ SEQUENCE 422 AA; 46683 MW; C33CDD2C1B13C397 CRC64; MQNSHSGVNQ LGGVFVNGRP LPDSTRQKIV ELAHSGARPC DISRILQVSN GCVSKILGRY YETGSIRPRA IGGSKPRVAT PEVVSKIAQY KRECPSIFAW EIRDRLLSEG VCTNDNIPSV SSINRVLRNL ASEKQQMGAD GMYDKLRMLN GQTGSWGTRP GWYPGTSVPG QPTQDGCQQQ EGGGENTNSI SSNGEDSDEA QMRLQLKRKL QRNRTSFTQE QIEALEKEFE RTHYPDVFAR ERLAAKIDLP EARIQVWFSN RRAKWRREEK LRNQRRQASN TPSHIPISSS FSTSVYQPIP QPTTPVSSFT SGSMLGRTDT ALTNTYSALP PMPSFTMANN LPMQPPVPSQ TSSYSCMLPT SPSVNGRSYD TYTPPHMQTH MNSQPMGTSG TTSTGLISPG VSVPVQVPGS EPDMSQYWPR LQ // ID PAX7_HUMAN Reviewed; 520 AA. AC P23759; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 3. DT 20-FEB-2007, entry version 74. DE Paired box protein Pax-7 (HUP1). GN Name=PAX7; Synonyms=HUP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING. RX MEDLINE=97480728; PubMed=9339373; DOI=10.1006/geno.1997.4915; RA Vorobyov E., Mertsalov I., Dockhorn-Dworniczak B., Dworniczak B., RA Horst J.; RT "The genomic organization and the full coding region of the human PAX7 RT gene."; RL Genomics 45:168-174(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R., Dunham I., RA Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-467 (ISOFORM LONG). RX MEDLINE=95075634; PubMed=7527137; DOI=10.1093/nar/22.22.4574; RA Schaefer B.W., Czerny T., Bernasconi M., Genini M., Busslinger M.; RT "Molecular cloning and characterization of a human PAX-7 cDNA RT expressed in normal and neoplastic myocytes."; RL Nucleic Acids Res. 22:4574-4582(1994). RN [4] RP NUCLEOTIDE SEQUENCE OF 30-195 (ISOFORM SHORT). RX MEDLINE=89305521; PubMed=2501086; RA Burri M., Tromvoukis Y., Bopp D., Frigerio G., Noll M.; RT "Conservation of the paired domain in metazoans and its structure in RT three isolated human genes."; RL EMBO J. 8:1183-1190(1989). CC -!- FUNCTION: Probable transcription factor. May have a role in CC myogenesis. CC -!- SUBUNIT: Can bind to DNA as a heterodimer with PAX3. Interacts CC with DAXX. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P23759-1; Sequence=Displayed; CC Name=Short; CC IsoId=P23759-2; Sequence=VSP_002370; CC -!- DISEASE: A chromosomal aberration involving PAX7 is a cause of CC rhabdomyosarcoma 2 (RMS2) [MIM:268220]; also known as alveolar CC rhabdomyosarcoma. Translocation t(1;13)(p36;q14) with FOXO1A. The CC resulting protein is a transcriptional activator. CC -!- SIMILARITY: Belongs to the paired homeobox family. CC -!- SIMILARITY: Contains 1 homeobox DNA-binding domain. CC -!- SIMILARITY: Contains 1 paired domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X96743; CAA65520.1; -; mRNA. DR EMBL; X96744; CAA65521.1; -; Genomic_DNA. DR EMBL; X15042; CAA65521.1; JOINED; Genomic_DNA. DR EMBL; X15250; CAA65521.1; JOINED; Genomic_DNA. DR EMBL; X15251; CAA65521.1; JOINED; Genomic_DNA. DR EMBL; X96745; CAA65521.1; JOINED; Genomic_DNA. DR EMBL; X96746; CAA65521.1; JOINED; Genomic_DNA. DR EMBL; X96747; CAA65521.1; JOINED; Genomic_DNA. DR EMBL; X96748; CAA65521.1; JOINED; Genomic_DNA. DR EMBL; X96744; CAA65522.1; -; Genomic_DNA. DR EMBL; X15042; CAA65522.1; JOINED; Genomic_DNA. DR EMBL; X15250; CAA65522.1; JOINED; Genomic_DNA. DR EMBL; X15251; CAA65522.1; JOINED; Genomic_DNA. DR EMBL; X96745; CAA65522.1; JOINED; Genomic_DNA. DR EMBL; X96746; CAA65522.1; JOINED; Genomic_DNA. DR EMBL; X96747; CAA65522.1; JOINED; Genomic_DNA. DR EMBL; X96748; CAA65522.1; JOINED; Genomic_DNA. DR EMBL; AL021528; CAA16432.1; -; Genomic_DNA. DR EMBL; Z35141; CAA84513.1; -; mRNA. DR PIR; S78502; S78502. DR UniGene; Hs.113253; -. DR HSSP; P06601; 1FJL. DR SMR; P23759; 38-163, 216-275. DR TRANSFAC; T00396; -. DR Ensembl; ENSG00000009709; Homo sapiens. DR KEGG; hsa:5081; -. DR HGNC; HGNC:8621; PAX7. DR MIM; 167410; gene. DR MIM; 268220; phenotype. DR ArrayExpress; P23759; -. DR GermOnline; ENSG00000009709; Homo sapiens. DR RZPD-ProtExp; Z0758; -. DR GO; GO:0003700; F:transcription factor activity; TAS:ProtInc. DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc. DR GO; GO:0006916; P:anti-apoptosis; TAS:ProtInc. DR InterPro; IPR001356; Homeobox. DR InterPro; IPR012287; Homeodomain-rel. DR InterPro; IPR009057; Homeodomain_like. DR InterPro; IPR001523; Paired_box_N. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2. DR Pfam; PF00046; Homeobox; 1. DR Pfam; PF00292; PAX; 1. DR PRINTS; PR00024; HOMEOBOX. DR PRINTS; PR00027; PAIREDBOX. DR ProDom; PD000010; Homeobox; 1. DR SMART; SM00389; HOX; 1. DR SMART; SM00351; PAX; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS00034; PAIRED_1; 1. DR PROSITE; PS51057; PAIRED_2; 1. KW Alternative splicing; Chromosomal rearrangement; KW Developmental protein; DNA-binding; Homeobox; Nuclear protein; KW Paired box; Proto-oncogene; Transcription; Transcription regulation. FT CHAIN 1 520 Paired box protein Pax-7. FT /FTId=PRO_0000050194. FT DOMAIN 34 163 Paired. FT DNA_BIND 217 276 Homeobox. FT COMPBIAS 340 346 Poly-Ala. FT VAR_SEQ 151 152 Missing (in isoform Short). FT /FTId=VSP_002370. SQ SEQUENCE 520 AA; 56896 MW; 3B0F8CC99D65699C CRC64; MAALPGTVPR MMRPAPGQNY PRTGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPRQVA TPDVEKKIEE YKRENPGMFS WEIRDRLLKD GHCDRSTVPS GLVSSISRVL RIKFGKKEEE DEADKKEDDG EKKAKHSIDG ILGDKGNRLD EGSDVESEPD LPLKRKQRRS RTTFTAEQLE ELEKAFERTH YPDIYTREEL AQRTKLTEAR VQVWFSNRRA RWRKQAGANQ LAAFNHLLPG GFPPTGMPTL PPYQLPDSTY PTTTISQDGG STVHRPQPLP PSTMHQGGLA AAAAAADTSS AYGARHSFSS YSDSFMNPAA PSNHMNPVSN GLSPQVMSIL GNPSAVPPQP QADFSISPLH GGLDSATSIS ASCSQRADSI KPGDSLPTSQ AYCPPTYSTT GYSVDPVAGY QYGQYGQSEC LVPWASPVPI PSPTPRASCL FMESYKVVSG WGMSISQMEK LKSSQMEQFT // ID PAX9_HUMAN Reviewed; 341 AA. AC P55771; Q99582; Q9UQR4; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 3. DT 06-FEB-2007, entry version 63. DE Paired box protein Pax-9. GN Name=PAX9; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=20461864; PubMed=10899593; DOI=10.1016/S0167-4781(00)00130-5; RA Hetzer-Egger C., Schorpp M., Boehm T.; RT "Evolutionary conservation of gene structures of the Pax1/9 gene RT family."; RL Biochim. Biophys. Acta 1492:517-521(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-211. RX MEDLINE=95072651; PubMed=7981748; DOI=10.1038/ng0493-292; RA Stapleton P., Weith A., Urbanek P., Kozmik Z., Busslinger M.; RT "Chromosomal localization of seven PAX genes and cloning of a novel RT family member, PAX-9."; RL Nat. Genet. 3:292-298(1993). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-339. RC TISSUE=Oesophagus; RX MEDLINE=97179475; PubMed=9021154; DOI=10.1007/s003359900351; RA Peters H., Schuster G., Neubueser A., Richter T., Hoefler H.; RT "Isolation of the Pax9 cDNA from adult human esophagus."; RL Mamm. Genome 8:62-64(1997). RN [5] RP VARIANT OLIGODENTIA SER-51. RX MEDLINE=22671556; PubMed=12786960; RX DOI=10.1034/j.1600-0722.2003.00036.x; RA Mostowska A., Kobielak A., Biedziak B., Trzeciak W.H.; RT "Novel mutation in the paired box sequence of PAX9 gene in a sporadic RT form of oligodontia."; RL Eur. J. Oral Sci. 111:272-276(2003). CC -!- FUNCTION: Transcription factor required for normal development of CC thymus, parathyroid glands, ultimobranchial bodies, teeth, CC skeletal elements of skull and larynx as well as distal limbs (By CC similarity). CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- DISEASE: Defects in PAX9 are a cause of oligodontia [MIM:604625]. CC It is a form of familial or selective tooth agenesis. Oligodontia CC is defined as the agenesis of 6 or more permanent teeth without CC associated systemic disorders. Agenesis of one or more teeth CC constitutes one of the most common developmental anomalies in man. CC Reported incidences vary from 1.6% to 9.6%, excluding third molar CC (Wisdom tooth) agenesis, which occurs in 20% of the population. CC -!- SIMILARITY: Contains 1 paired domain. CC -!- WEB RESOURCE: NAME=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/PAX9ID41644ch14q12.html". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ238381; CAB41533.1; -; Genomic_DNA. DR EMBL; AJ238382; CAB41533.1; JOINED; Genomic_DNA. DR EMBL; AJ238383; CAB41533.1; JOINED; Genomic_DNA. DR EMBL; BC001159; AAH01159.1; -; mRNA. DR EMBL; L09745; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X92850; CAA63436.1; -; mRNA. DR UniGene; Hs.132576; -. DR HSSP; Q02548; 1K78. DR SMR; P55771; 8-130. DR TRANSFAC; T02986; -. DR Ensembl; ENSG00000198807; Homo sapiens. DR KEGG; hsa:5083; -. DR H-InvDB; HIX0011606; -. DR HGNC; HGNC:8623; PAX9. DR MIM; 167416; gene. DR MIM; 604625; phenotype. DR ArrayExpress; P55771; -. DR GermOnline; ENSG00000198807; Homo sapiens. DR RZPD-ProtExp; IOH4822; -. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB. DR GO; GO:0007275; P:multicellular organismal development; NAS:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; NAS:UniProtKB. DR InterPro; IPR009057; Homeodomain_like. DR InterPro; IPR001523; Paired_box_N. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2. DR Pfam; PF00292; PAX; 1. DR PRINTS; PR00027; PAIREDBOX. DR SMART; SM00351; PAX; 1. DR PROSITE; PS00034; PAIRED_1; 1. DR PROSITE; PS51057; PAIRED_2; 1. KW Developmental protein; Disease mutation; DNA-binding; Nuclear protein; KW Paired box; Transcription; Transcription regulation. FT CHAIN 1 341 Paired box protein Pax-9. FT /FTId=PRO_0000050203. FT DOMAIN 4 130 Paired. FT VARIANT 51 51 G -> S (in oligodontia). FT /FTId=VAR_015698. FT CONFLICT 211 211 V -> G (in Ref. 3). SQ SEQUENCE 341 AA; 36310 MW; F5E6B0BC991E7C1D CRC64; MEPAFGEVNQ LGGVFVNGRP LPNAIRLRIV ELAQLGIRPC DISRQLRVSH GCVSKILARY NETGSILPGA IGGSKPRVTT PTVVKHIRTY KQRDPGIFAW EIRDRLLADG VCDKYNVPSV SSISRILRNK IGNLAQQGHY DSYKQHQPTP QPALPYNHIY SYPSPITAAA AKVPTPPGVP AIPGSVAMPR TWPSSHSVTD ILGIRSITDQ VSDSSPYHSP KVEEWSSLGR NNFPAAAPHA VNGLEKGALE QEAKYGQAPN GLPAVGSFVS ASSMAPYPTP AQVSPYMTYS AAPSGYVAGH GWQHAGGTSL SPHNCDIPAS LAFKGMQAAR EGSHSVTASA L // ID PAXI_HUMAN Reviewed; 591 AA. AC P49023; O14970; O14971; O60360; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2003, sequence version 2. DT 20-FEB-2007, entry version 71. DE Paxillin. GN Name=PXN; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA). RX MEDLINE=95197488; PubMed=7534286; DOI=10.1074/jbc.270.10.5039; RA Salgia R., Li J.-L., Lo S.H., Brunkhorst B., Kansas G.S., RA Sobhany E.S., Sun Y., Pisick E., Hallek M., Ernst T., Tantravahi R., RA Chen L.B., Griffin J.D.; RT "Molecular cloning of human paxillin, a focal adhesion protein RT phosphorylated by P210BCR/ABL."; RL J. Biol. Chem. 270:5039-5047(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V., RA Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M., RA Lathrop M., Cox R.D., Bell G.I.; RT "Transcription map of the 5cM region surrounding the hepatocyte RT nuclear factor-1a/MODY3 gene on chromosome 12."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA AND GAMMA). RC TISSUE=Placenta; RX MEDLINE=97207310; PubMed=9054445; DOI=10.1074/jbc.272.11.7437; RA Mazaki Y., Hashimoto S., Sabe H.; RT "Monocyte cells and cancer cells express novel paxillin isoforms with RT different binding properties to focal adhesion proteins."; RL J. Biol. Chem. 272:7437-7444(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [5] RP INTERACTION WITH ITGA4. RX PubMed=10604475; DOI=10.1038/45264; RA Liu S., Thomas S.M., Woodside D.G., Rose D.M., Kiosses W.B., Pfaff M., RA Ginsberg M.H.; RT "Binding of paxillin to alpha4 integrins modifies integrin-dependent RT biological responses."; RL Nature 402:676-681(1999). RN [6] RP INTERACTION WITH GIT1. RX PubMed=10938112; DOI=10.1128/MCB.20.17.6354-6363.2000; RA Zhao Z.-S., Manser E., Loo T.-H., Lim L.; RT "Coupling of PAK-interacting exchange factor PIX to GIT1 promotes RT focal complex disassembly."; RL Mol. Cell. Biol. 20:6354-6363(2000). RN [7] RP INTERACTION WITH DDEF2. RX MEDLINE=20214823; PubMed=10749932; RA Kondo A., Hashimoto S., Yano H., Nagayama K., Mazaki Y., Sabe H.; RT "A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an RT ADP-ribosylation factor GTPase-activating protein activity, is RT involved in paxillin recruitment to focal adhesions and cell RT migration."; RL Mol. Biol. Cell 11:1315-1327(2000). RN [8] RP PHOSPHORYLATION AT TYR-31; TYR-118 AND TYR-181. RX MEDLINE=21634701; PubMed=11774284; DOI=10.1002/ijc.1609; RA Iwasaki T., Nakata A., Mukai M., Shinkai K., Yano H., Sabe H., RA Schaefer E., Tatsuta M., Tsujimura T., Terada N., Kakishita E., RA Akedo H.; RT "Involvement of phosphorylation of Tyr-31 and Tyr-118 of paxillin in RT MM1 cancer cell migration."; RL Int. J. Cancer 97:330-335(2002). RN [9] RP INTERACTION WITH RNF5. RX PubMed=12861019; DOI=10.1128/MCB.23.15.5331-5345.2003; RA Didier C., Broday L., Bhoumik A., Israeli S., Takahashi S., RA Nakayama K., Thomas S.M., Turner C.E., Henderson S., Sabe H., RA Ronai Z.; RT "RNF5, a RING finger protein that regulates cell motility by targeting RT paxillin ubiquitination and altered localization."; RL Mol. Cell. Biol. 23:5331-5345(2003). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-88 AND TYR-118, AND MASS RP SPECTROMETRY. RX PubMed=16212419; DOI=10.1021/pr050134h; RA Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.; RT "Phosphoproteome analysis of HeLa cells using stable isotope labeling RT with amino acids in cell culture (SILAC)."; RL J. Proteome Res. 4:1661-1671(2005). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND MASS RP SPECTROMETRY. RX PubMed=15951569; DOI=10.1074/mcp.M500089-MCP200; RA Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., RA Lauffenburger D.A., White F.M.; RT "Time-resolved mass spectrometry of tyrosine phosphorylation sites in RT the epidermal growth factor receptor signaling network reveals dynamic RT modules."; RL Mol. Cell. Proteomics 4:1240-1250(2005). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND MASS RP SPECTROMETRY. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118, AND MASS RP SPECTROMETRY. RX PubMed=16094384; DOI=10.1038/nmeth776; RA Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., RA Bodenmiller B., Watts J.D., Hood L., Aebersold R.; RT "Quantitative phosphoproteome analysis using a dendrimer conjugation RT chemistry and tandem mass spectrometry."; RL Nat. Methods 2:591-598(2005). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-118 AND SER-303, AND RP MASS SPECTROMETRY. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS RP SPECTROMETRY. RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). CC -!- FUNCTION: Cytoskeletal protein involved in actin-membrane CC attachment at sites of cell adhesion to the extracellular matrix CC (focal adhesion). CC -!- SUBUNIT: Binds in vitro to vinculin as well as to the SH3 domain CC of c-SRC and, when tyrosine phosphorylated, to the SH2 domain of CC V-CRK. Isoform beta binds to focal adhesion kinase but weakly to CC vinculin. Isoform gamma binds to vinculin but only weakly to focal CC adhesion kinase. Interacts with GIT1 and NUDT16L1/SDOS. Component CC of cytoplasmic complexes, which also contain GIT1, ARHGEF6 and CC PAK1 (By similarity). Binds DDEF2. Interacts with unphosphorylated CC ITGA4. Interacts with RNF5. CC -!- INTERACTION: CC Q09463:rnf-5 (xeno); NbExp=2; IntAct=EBI-702209, EBI-963421; CC Q99942:RNF5; NbExp=3; IntAct=EBI-702209, EBI-348482; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Beta; CC IsoId=P49023-1; Sequence=Displayed; CC Name=Alpha; CC IsoId=P49023-2; Sequence=VSP_003114; CC Name=Gamma; CC IsoId=P49023-3; Sequence=VSP_003115; CC -!- PTM: Phosphorylated on tyrosine residues during integrin-mediated CC cell adhesion, embryonic development, fibroblast transformation CC and following stimulation of cells by mitogens. CC -!- SIMILARITY: Contains 4 LIM zinc-binding domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U14588; AAC50104.1; -; mRNA. DR EMBL; U87946; AAD00648.1; -; Genomic_DNA. DR EMBL; U87941; AAD00648.1; JOINED; Genomic_DNA. DR EMBL; U87942; AAD00648.1; JOINED; Genomic_DNA. DR EMBL; U87943; AAD00648.1; JOINED; Genomic_DNA. DR EMBL; U87944; AAD00648.1; JOINED; Genomic_DNA. DR EMBL; U87945; AAD00648.1; JOINED; Genomic_DNA. DR EMBL; D86862; BAA18997.1; -; mRNA. DR EMBL; D86863; BAA18998.1; -; mRNA. DR EMBL; AC004263; AAC05175.1; -; Genomic_DNA. DR PIR; A55933; A55933. DR UniGene; Hs.446336; -. DR PDB; 1KKY; Model; A=142-157. DR PDB; 1KL0; Model; B=142-157. DR IntAct; P49023; -. DR Ensembl; ENSG00000089159; Homo sapiens. DR KEGG; hsa:5829; -. DR HGNC; HGNC:9718; PXN. DR HPA; CAB003841; -. DR MIM; 602505; gene. DR ArrayExpress; P49023; -. DR GermOnline; ENSG00000089159; Homo sapiens. DR RZPD-ProtExp; D0240; -. DR RZPD-ProtExp; IOH10180; -. DR RZPD-ProtExp; IOH29384; -. DR GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc. DR GO; GO:0017166; F:vinculin binding; IPI:UniProtKB. DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc. DR GO; GO:0007172; P:signal complex formation; TAS:ProtInc. DR InterPro; IPR001781; LIM_Zn_bd. DR InterPro; IPR001904; Paxillin. DR Pfam; PF00412; LIM; 4. DR Pfam; PF03535; Paxillin; 1. DR PRINTS; PR00832; PAXILLIN. DR ProDom; PD000094; LIM; 4. DR SMART; SM00132; LIM; 4. DR PROSITE; PS00478; LIM_DOMAIN_1; 4. DR PROSITE; PS50023; LIM_DOMAIN_2; 4. KW 3D-structure; Alternative splicing; Cell adhesion; Cytoskeleton; KW LIM domain; Metal-binding; Phosphorylation; Repeat; Zinc. FT CHAIN 1 591 Paxillin. FT /FTId=PRO_0000075853. FT DOMAIN 356 415 LIM zinc-binding 1. FT DOMAIN 416 473 LIM zinc-binding 2. FT DOMAIN 474 533 LIM zinc-binding 3. FT DOMAIN 534 591 LIM zinc-binding 4. FT COMPBIAS 46 53 Pro-rich. FT MOD_RES 31 31 Phosphotyrosine. FT MOD_RES 88 88 Phosphotyrosine. FT MOD_RES 106 106 Phosphoserine. FT MOD_RES 109 109 Phosphoserine (By similarity). FT MOD_RES 118 118 Phosphotyrosine. FT MOD_RES 181 181 Phosphotyrosine. FT MOD_RES 303 303 Phosphoserine. FT VAR_SEQ 278 311 Missing (in isoform Alpha). FT /FTId=VSP_003114. FT VAR_SEQ 278 311 IQDLEQRADGERCWAAGWPRDGGRSSPGGQDEGG -> GSW FT PLEEVVLLVSISSSVQEGEKYPHPCAARHRTPSLRSPDQPP FT PCPQ (in isoform Gamma). FT /FTId=VSP_003115. FT CONFLICT 73 73 G -> S (in Ref. 4). FT HELIX 143 155 SQ SEQUENCE 591 AA; 64533 MW; 0FFDC07047E96636 CRC64; MDDLDALLAD LESTTSHISK RPVFLSEETP YSYPTGNHTY QEIAVPPPVP PPPSSEALNG TILDPLDQWQ PSGSRFIHQQ PQSSSPVYGS SAKTSSVSNP QDSVGSPCSR VGEEEHVYSF PNKQKSAEPS PTVMSTSLGS NLSELDRLLL ELNAVQHNPP GFPADEANSS PPLPGALSPL YGVPETNSPL GGKAGPLTKE KPKRNGGRGL EDVRPSVESL LDELESSVPS PVPAITVNQG EMSSPQRVTS TQQQTRISAS SATRELDELM ASLSDFKIQD LEQRADGERC WAAGWPRDGG RSSPGGQDEG GFMAQGKTGS SSPPGGPPKP GSQLDSMLGS LQSDLNKLGV ATVAKGVCGA CKKPIAGQVV TAMGKTWHPE HFVCTHCQEE IGSRNFFERD GQPYCEKDYH NLFSPRCYYC NGPILDKVVT ALDRTWHPEH FFCAQCGAFF GPEGFHEKDG KAYCRKDYFD MFAPKCGGCA RAILENYISA LNTLWHPECF VCRECFTPFV NGSFFEHDGQ PYCEVHYHER RGSLCSGCQK PITGRCITAM AKKFHPEHFV CAFCLKQLNK GTFKEQNDKP YCQNCFLKLF C // ID OPSD_XENLA Reviewed; 354 AA. AC P29403; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 28-NOV-2006, entry version 52. DE Rhodopsin. GN Name=rho; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93287804; PubMed=8510503; DOI=10.1016/0169-328X(93)90016-I; RA Saha M.S., Grainger R.M.; RT "Early opsin expression in Xenopus embryos precedes photoreceptor RT differentiation."; RL Brain Res. Mol. Brain Res. 17:307-318(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX MEDLINE=96216396; PubMed=8621718; DOI=10.1074/jbc.271.6.3179; RA Batni S., Scalzetti L.C., Moody S.A., Knox B.E.; RT "Characterization of the Xenopus rhodopsin gene."; RL J. Biol. Chem. 271:3179-3186(1996). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Rod shaped photoreceptor cells which mediates CC vision in dim light. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; S62229; AAB27128.2; -; mRNA. DR EMBL; L04692; AAB59950.1; -; mRNA. DR EMBL; L07770; AAC42232.1; -; mRNA. DR EMBL; U23808; AAC59901.1; -; Genomic_DNA. DR PIR; I51200; I51200. DR HSSP; P02699; 1F88. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR000732; Rhodopsin. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00579; RHODOPSIN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Lipoprotein; KW Membrane; Palmitate; Phosphorylation; Photoreceptor protein; Receptor; KW Retinal protein; Sensory transduction; Transducer; Transmembrane; KW Vision. FT CHAIN 1 354 Rhodopsin. FT /FTId=PRO_0000197727. FT TOPO_DOM 1 36 Extracellular. FT TRANSMEM 37 61 1 (Potential). FT TOPO_DOM 62 73 Cytoplasmic. FT TRANSMEM 74 98 2 (Potential). FT TOPO_DOM 99 113 Extracellular. FT TRANSMEM 114 133 3 (Potential). FT TOPO_DOM 134 152 Cytoplasmic. FT TRANSMEM 153 176 4 (Potential). FT TOPO_DOM 177 202 Extracellular. FT TRANSMEM 203 230 5 (Potential). FT TOPO_DOM 231 252 Cytoplasmic. FT TRANSMEM 253 276 6 (Potential). FT TOPO_DOM 277 284 Extracellular. FT TRANSMEM 285 309 7 (Potential). FT TOPO_DOM 310 354 Cytoplasmic. FT BINDING 296 296 Retinal chromophore (covalent). FT LIPID 322 322 S-palmitoyl cysteine (By similarity). FT LIPID 323 323 S-palmitoyl cysteine (By similarity). FT CARBOHYD 2 2 N-linked (GlcNAc...) (By similarity). FT CARBOHYD 15 15 N-linked (GlcNAc...) (By similarity). FT DISULFID 110 187 By similarity. FT CONFLICT 107 107 P -> Q (in Ref. 2). FT CONFLICT 137 137 I -> M (in Ref. 2). FT CONFLICT 241 241 L -> A (in Ref. 2). SQ SEQUENCE 354 AA; 39787 MW; CD18F49EC63D8FFE CRC64; MNGTEGPNFY VPMSNKTGVV RSPFDYPQYY LAEPWQYSAL AAYMFLLILL GLPINFMTLF VTIQHKKLRT PLNYILLNLV FANHFMVLCG FTVTMYTSMH GYFIFGPTGC YIEGFFATLG GEVALWSLVV LAVERYIVVC KPMANFRFGE NHAIMGVAFT WIMALSCAAP PLFGWSRYIP EGMQCSCGVD YYTLKPEVNN ESFVIYMFIV HFTIPLIVIF FCYGRLLCTV KEAAAQQQES LTTQKAEKEV TRMVVIMVVF FLICWVPYAY VAFYIFTHQG SNFGPVFMTV PAFFAKSSAI YNPVIYIVLN KQFRNCLITT LCCGKNPFGD EDGSSAATSK TEASSVSSSQ VSPA // ID OPS2_DROME Reviewed; 381 AA. AC P08099; Q9VE29; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 03-APR-2007, entry version 73. DE Opsin Rh2 (Ocellar opsin). GN Name=Rh2; ORFNames=CG16740; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=86133563; PubMed=2936466; DOI=10.1016/0092-8674(86)90836-6; RA Cowman A.F., Zuker C.S., Rubin G.M.; RT "An opsin gene expressed in only one photoreceptor cell type of the RT Drosophila eye."; RL Cell 44:705-710(1986). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., RA Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP LOCALIZATION OF OPSIN RH2, AND BIOPHYSICOCHEMICAL PROPERTIES. RX MEDLINE=88261498; PubMed=2455230; DOI=10.1038/333737a0; RA Feiler R., Harris W.A., Kirschfeld K., Wehrhahn C., Zuker C.S.; RT "Targeted misexpression of a Drosophila opsin gene leads to altered RT visual function."; RL Nature 333:737-741(1988). RN [5] RP LOCALIZATION OF OPSIN RH2. RX MEDLINE=88261503; PubMed=2968518; DOI=10.1038/333779a0; RA Pollock J.A., Benzer S.; RT "Transcript localization of four opsin genes in the three visual RT organs of Drosophila; RH2 is ocellus specific."; RL Nature 333:779-782(1988). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=420 nm; CC -!- INTERACTION: CC Q9VL06:CG5604; NbExp=1; IntAct=EBI-162315, EBI-173559; CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Predominant opsin expressed in the dorsal CC ocelli. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M12896; AAA28734.1; -; Genomic_DNA. DR EMBL; AE014297; AAF55601.1; -; Genomic_DNA. DR PIR; A24058; OOFF2. DR UniGene; Dm.2404; -. DR HSSP; P02699; 1EDV. DR DIP; DIP:22447N; -. DR IntAct; P08099; -. DR Ensembl; CG16740; Drosophila melanogaster. DR KEGG; dme:Dmel_CG16740; -. DR FlyBase; FBgn0003248; Rh2. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-012289-MONOMER; -. DR GermOnline; CG16740; Drosophila melanogaster. DR GO; GO:0008020; F:G-protein coupled photoreceptor activity; IDA:FlyBase. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0007602; P:phototransduction; IGI:FlyBase. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR001735; Opsin_RH1/RH2. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00576; OPSINRH1RH2. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; Complete proteome; G-protein coupled receptor; KW Glycoprotein; Membrane; Phosphorylation; Photoreceptor protein; KW Receptor; Retinal protein; Sensory transduction; Transducer; KW Transmembrane; Vision. FT CHAIN 1 381 Opsin Rh2. FT /FTId=PRO_0000197625. FT TOPO_DOM 1 56 Extracellular. FT TRANSMEM 57 81 1 (Potential). FT TOPO_DOM 82 93 Cytoplasmic. FT TRANSMEM 94 119 2 (Potential). FT TOPO_DOM 120 133 Extracellular. FT TRANSMEM 134 153 3 (Potential). FT TOPO_DOM 154 172 Cytoplasmic. FT TRANSMEM 173 196 4 (Potential). FT TOPO_DOM 197 220 Extracellular. FT TRANSMEM 221 248 5 (Potential). FT TOPO_DOM 249 283 Cytoplasmic. FT TRANSMEM 284 307 6 (Potential). FT TOPO_DOM 308 314 Extracellular. FT TRANSMEM 315 339 7 (Potential). FT TOPO_DOM 340 381 Cytoplasmic. FT BINDING 326 326 Retinal chromophore (covalent). FT CARBOHYD 27 27 N-linked (GlcNAc...) (Probable). FT DISULFID 130 207 Potential. SQ SEQUENCE 381 AA; 42722 MW; 628322D228396F9D CRC64; MERSHLPETP FDLAHSGPRF QAQSSGNGSV LDNVLPDMAH LVNPYWSRFA PMDPMMSKIL GLFTLAIMII SCCGNGVVVY IFGGTKSLRT PANLLVLNLA FSDFCMMASQ SPVMIINFYY ETWVLGPLWC DIYAGCGSLF GCVSIWSMCM IAFDRYNVIV KGINGTPMTI KTSIMKILFI WMMAVFWTVM PLIGWSAYVP EGNLTACSID YMTRMWNPRS YLITYSLFVY YTPLFLICYS YWFIIAAVAA HEKAMREQAK KMNVKSLRSS EDCDKSAEGK LAKVALTTIS LWFMAWTPYL VICYFGLFKI DGLTPLTTIW GATFAKTSAV YNPIVYGISH PKYRIVLKEK CPMCVFGNTD EPKPDAPASD TETTSEADSK A // ID OPS2_DROPS Reviewed; 381 AA. AC P28679; Q298F1; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 13-JUN-2006, sequence version 3. DT 06-MAR-2007, entry version 52. DE Opsin Rh2 (Ocellar opsin). GN Name=Rh2; ORFNames=GA14120; OS Drosophila pseudoobscura (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7237; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Apple Hill; RX MEDLINE=93012921; PubMed=1398053; RA Carulli J.P., Hartl D.L.; RT "Variable rates of evolution among Drosophila opsin genes."; RL Genetics 132:193-204(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MV2-25; RX PubMed=15632085; DOI=10.1101/gr.3059305; RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., RA Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., RA van Batenburg M.F., Howells S.L., Scherer S.E., Sodergren E., RA Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D., RA Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D., RA Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R., RA Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L., RA Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F., RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M., RA Weinstock G.M., Gibbs R.A.; RT "Comparative genome sequencing of Drosophila pseudoobscura: RT chromosomal, gene, and cis-element evolution."; RL Genome Res. 15:1-18(2005). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=420 nm; CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Some or all of the Ser/Thr residues present in the C-terminal CC part may be phosphorylated. CC -!- MISCELLANEOUS: Opsin Rh2 is the predominant opsin expressed in the CC dorsal ocelli. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC -!- CAUTION: Ref.2 sequence differs from that shown due to erroneous CC gene model prediction. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X65878; CAA46709.1; -; Genomic_DNA. DR EMBL; CM000070; EAL28004.1; ALT_SEQ; Genomic_DNA. DR PIR; S40692; S40692. DR HSSP; P02699; 1EDV. DR FlyBase; FBgn0012708; Dpse\Rh2. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR001735; Opsin_RH1/RH2. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00576; OPSINRH1RH2. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; Complete proteome; G-protein coupled receptor; KW Glycoprotein; Membrane; Phosphorylation; Photoreceptor protein; KW Receptor; Retinal protein; Sensory transduction; Transducer; KW Transmembrane; Vision. FT CHAIN 1 381 Opsin Rh2. FT /FTId=PRO_0000197626. FT TOPO_DOM 1 56 Extracellular. FT TRANSMEM 57 81 1 (Potential). FT TOPO_DOM 82 93 Cytoplasmic. FT TRANSMEM 94 119 2 (Potential). FT TOPO_DOM 120 133 Extracellular. FT TRANSMEM 134 153 3 (Potential). FT TOPO_DOM 154 172 Cytoplasmic. FT TRANSMEM 173 196 4 (Potential). FT TOPO_DOM 197 220 Extracellular. FT TRANSMEM 221 248 5 (Potential). FT TOPO_DOM 249 283 Cytoplasmic. FT TRANSMEM 284 307 6 (Potential). FT TOPO_DOM 308 314 Extracellular. FT TRANSMEM 315 339 7 (Potential). FT TOPO_DOM 340 381 Cytoplasmic. FT BINDING 326 326 Retinal chromophore (covalent). FT CARBOHYD 27 27 N-linked (GlcNAc...) (Probable). FT DISULFID 130 207 Potential. FT CONFLICT 45 45 Y -> H (in Ref. 1). FT CONFLICT 342 343 KY -> ND (in Ref. 1). FT CONFLICT 358 358 S -> T (in Ref. 1). FT CONFLICT 381 381 A -> D (in Ref. 1). SQ SEQUENCE 381 AA; 42733 MW; 2033C05C4503FEAF CRC64; MERSLLPEPP LAMALLGPRF EAQTGGNRSV LDNVLPDMAP LVNPYWSRFA PMDPTMSKIL GLFTLVILII SCCGNGVVVY IFGGTKSLRT PANLLVLNLA FSDFCMMASQ SPVMIINFYY ETWVLGPLWC DIYAACGSLF GCVSIWSMCM IAFDRYNVIV KGINGTPMTI KTSIMKIAFI WMMAVFWTIM PLIGWSSYVP EGNLTACSID YMTRQWNPRS YLITYSLFVY YTPLFMICYS YWFIIATVAA HEKAMRDQAK KMNVKSLRSS EDCDKSAENK LAKVALTTIS LWFMAWTPYL IICYFGLFKI DGLTPLTTIW GATFAKTSAV YNPIVYGISH PKYRLVLKEK CPMCVCGSTD EPKPDAPPSD TETTSEAESK A // ID OPSC2_HEMSA Reviewed; 377 AA. AC Q25158; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 31-OCT-2006, entry version 40. DE Compound eye opsin BCRH2. OS Hemigrapsus sanguineus (Crab). OC Eukaryota; Metazoa; Arthropoda; Crustacea; Malacostraca; OC Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Brachyura; OC Eubrachyura; Grapsoidea; Varunidae; Hemigrapsus. OX NCBI_TaxID=40176; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Eye; RX PubMed=9318091; RA Sakamoto K., Hisatomi O., Tokunaga F., Eguchi E.; RT "Two opsins from the compound eye of the crab Hemigrapsus RT sanguineus."; RL J. Exp. Biol. 199:441-450(1996). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. This opsin produces visual pigments with CC maximal absorption in the blue-green region of the spectrum. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed in all of the seven retinular cells CC (R1-R7) forming the main rhabdom in each ommatidium. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D50584; BAA09133.1; -; mRNA. DR HSSP; P02699; 1L9H. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR000856; Opsin_RH3/RH4. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00577; OPSINRH3RH4. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Membrane; KW Phosphorylation; Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane; Vision. FT CHAIN 1 377 Compound eye opsin BCRH2. FT /FTId=PRO_0000197750. FT TOPO_DOM 1 53 Extracellular. FT TRANSMEM 54 78 1 (Potential). FT TOPO_DOM 79 90 Cytoplasmic. FT TRANSMEM 91 115 2 (Potential). FT TOPO_DOM 116 131 Extracellular. FT TRANSMEM 132 151 3 (Potential). FT TOPO_DOM 152 170 Cytoplasmic. FT TRANSMEM 171 194 4 (Potential). FT TOPO_DOM 195 218 Extracellular. FT TRANSMEM 219 246 5 (Potential). FT TOPO_DOM 247 281 Cytoplasmic. FT TRANSMEM 282 305 6 (Potential). FT TOPO_DOM 306 313 Extracellular. FT TRANSMEM 314 338 7 (Potential). FT TOPO_DOM 339 377 Cytoplasmic. FT BINDING 325 325 Retinal chromophore (covalent) (By FT similarity). FT CARBOHYD 3 3 N-linked (GlcNAc...) (Potential). FT DISULFID 128 205 By similarity. SQ SEQUENCE 377 AA; 42114 MW; FD6CC2E0E199A256 CRC64; MTNATGPQMA YYGAASMDFG YPEGVSIVDF VRPEIKPYVH QHWYNYPPVN PMWHYLLGVI YLFLGTVSIF GNGLVIYLFN KSAALRTPAN ILVVNLALSD LIMLTTNVPF FTYNCFSGGV WMFSPQYCEI YACLGAITGV CSIWLLCMIS FDRYNIICNG FNGPKLTTGK AVVFALISWV IAIGCALPPF FGWGNYILEG ILDSCSYDYL TQDFNTFSYN IFIFVFDYFL PAAIIVFSYV FIVKAIFAHE AAMRAQAKKM NVSTLRSNEA DAQRAEIRIA KTALVNVSLW FICWTPYALI SLKGVMGDTS GITPLVSTLP ALLAKSCSCY NPFVYAISHP KYRLAITQHL PWFCVHETET KSNDDSQSNS TVAQDKA // ID OPSO_LIMPO Reviewed; 376 AA. AC P35361; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 31-OCT-2006, entry version 41. DE Ocellar opsin. OS Limulus polyphemus (Atlantic horseshoe crab). OC Eukaryota; Metazoa; Arthropoda; Chelicerata; Merostomata; Xiphosura; OC Limulidae; Limulus. OX NCBI_TaxID=6850; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Median ocelli; RX MEDLINE=93317641; PubMed=8327495; RA Smith W.C., Price D.A., Greenberg R.M., Battelle B.-A.; RT "Opsins from the lateral eyes and ocelli of the horseshoe crab, RT Limulus polyphemus."; RL Proc. Natl. Acad. Sci. U.S.A. 90:6150-6154(1993). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=530 nm; CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Ocellar cells; median ocelli. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L03792; AAA28274.1; -; mRNA. DR EMBL; L03782; AAA02499.1; -; mRNA. DR PIR; A48197; A48197. DR HSSP; P02699; 1EDV. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR001391; Opsin_lateye. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00578; OPSINLTRLEYE. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Membrane; KW Phosphorylation; Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane; Vision. FT CHAIN 1 376 Ocellar opsin. FT /FTId=PRO_0000197752. FT TOPO_DOM 1 46 Extracellular. FT TRANSMEM 47 71 1 (Potential). FT TOPO_DOM 72 83 Cytoplasmic. FT TRANSMEM 84 108 2 (Potential). FT TOPO_DOM 109 123 Extracellular. FT TRANSMEM 124 143 3 (Potential). FT TOPO_DOM 144 162 Cytoplasmic. FT TRANSMEM 163 186 4 (Potential). FT TOPO_DOM 187 210 Extracellular. FT TRANSMEM 211 238 5 (Potential). FT TOPO_DOM 239 274 Cytoplasmic. FT TRANSMEM 275 298 6 (Potential). FT TOPO_DOM 299 306 Extracellular. FT TRANSMEM 307 331 7 (Potential). FT TOPO_DOM 332 376 Cytoplasmic. FT BINDING 318 318 Retinal chromophore (covalent) (By FT similarity). FT CARBOHYD 17 17 N-linked (GlcNAc...) (Potential). FT CARBOHYD 193 193 N-linked (GlcNAc...) (Potential). FT DISULFID 120 197 By similarity. SQ SEQUENCE 376 AA; 42112 MW; FA9647C40531CBF8 CRC64; MANQLSYSSL GWPYQPNASV VDTMPKEMLY MIHEHWYAFP PMNPLWYSIL GVAMIILGII CVLGNGMVIY LMMTTKSLRT PTNLLVVNLA FSDFCMMAFM MPTMASNCFA ETWILGPFMC EVYGMAGSLF GCASIWSMVM ITLDRYNVIV RGMAAAPLTH KKATLLLLFV WIWSGGWTIL PFFGWSRYVP EGNLTSCTVD YLTKDWSSAS YVIIYGLAVY FLPLITMIYC YFFIVHAVAE HEKQLREQAK KMNVASLRAN ADQQKQSAEC RLAKVAMMTV GLWFMAWTPY LIIAWAGVFS SGTRLTPLAT IWGSVFAKAN SCYNPIVYGI SHPRYKAALY QRFPSLACGS GESGSDVKSE ASATMTMEEK PKSPEA // ID OPSD2_PATYE Reviewed; 399 AA. AC O15974; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 31-OCT-2006, entry version 38. DE Rhodopsin, G0-coupled (G0-rhodopsin). GN Name=SCOP2; OS Patinopecten yessoensis (Ezo giant scallop) (Yesso scallop). OC Eukaryota; Metazoa; Mollusca; Bivalvia; Pteriomorphia; Pectinoida; OC Pectinoidea; Pectinidae; Mizuhopecten. OX NCBI_TaxID=6573; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Eye; RX MEDLINE=97435252; PubMed=9287291; DOI=10.1074/jbc.272.37.22979; RA Kojima D., Terakita A., Ishikawa T., Tsukahara Y., Maeda A., RA Shichida Y.; RT "A novel Go-mediated phototransduction cascade in scallop visual RT cells."; RL J. Biol. Chem. 272:22979-22982(1997). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Retina. Expressed in the hyperpolarizing cell CC layer of the photoreceptor cells with its photoreceptive region CC adjacent to the lens. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB006455; BAA22218.1; -; mRNA. DR HSSP; P02699; 1F88. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR002962; Peropsin. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR01244; PEROPSIN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; FALSE_NEG. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Membrane; KW Phosphorylation; Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane; Vision. FT CHAIN 1 399 Rhodopsin, G0-coupled. FT /FTId=PRO_0000197736. FT TOPO_DOM 1 17 Extracellular. FT TRANSMEM 18 43 1 (Potential). FT TOPO_DOM 44 55 Cytoplasmic. FT TRANSMEM 56 81 2 (Potential). FT TOPO_DOM 82 95 Extracellular. FT TRANSMEM 96 115 3 (Potential). FT TOPO_DOM 116 134 Cytoplasmic. FT TRANSMEM 135 158 4 (Potential). FT TOPO_DOM 159 182 Extracellular. FT TRANSMEM 183 210 5 (Potential). FT TOPO_DOM 211 240 Cytoplasmic. FT TRANSMEM 241 263 6 (Potential). FT TOPO_DOM 264 271 Extracellular. FT TRANSMEM 272 295 7 (Potential). FT TOPO_DOM 296 399 Cytoplasmic. FT BINDING 282 282 Retinal chromophore (covalent). FT CARBOHYD 6 6 N-linked (GlcNAc...) (Potential). FT DISULFID 92 169 By similarity. SQ SEQUENCE 399 AA; 45097 MW; 5AA6857ABC912100 CRC64; MPFPLNRTDT ALVISPSEFR IIGIFISICC IIGVLGNLLI IIVFAKRRSV RRPINFFVLN LAVSDLIVAL LGYPMTAASA FSNRWIFDNI GCKIYAFLCF NSGVISIMTH AALSFCRYII ICQYGYRKKI TQTTVLRTLF SIWSFAMFWT LSPLFGWSSY VIEVVPVSCS VNWYGHGLGD VSYTISVIVA VYVFPLSIIV FSYGMILQEK VCKDSRKNGI RAQQRYTPRF IQDIEQRVTF ISFLMMAAFM VAWTPYAIMS ALAIGSFNVE NSFAALPTLF AKASCAYNPF IYAFTNANFR DTVVEIMAPW TTRRVGVSTL PWPQVTYYPR RRTSAVNTTD IEFPDDNIFI VNSSVNGPTV KREKIVQRNP INVRLGIKIE PRDSRAATEN TFTADFSVI // ID OPS2_SCHGR Reviewed; 380 AA. AC Q26495; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 31-OCT-2006, entry version 40. DE Opsin-2. GN Name=Lo2; OS Schistocerca gregaria (Desert locust). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Orthopteroidea; Orthoptera; Caelifera; Acridomorpha; OC Acridoidea; Acrididae; Cyrtacanthacridinae; Schistocerca. OX NCBI_TaxID=7010; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=97301174; PubMed=9156194; DOI=10.1016/S0042-6989(96)00198-8; RA Towner P., Harris P., Wolstenholme A.J., Hill C., Worm K., Gartner W.; RT "Primary structure of locust opsins: a speculative model which may RT account for ultraviolet wavelength light detection."; RL Vision Res. 37:495-503(1997). CC -!- FUNCTION: Visual pigments are the light-absorbing molecules that CC mediate vision. They consist of an apoprotein, opsin, covalently CC linked to cis-retinal. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- PTM: Phosphorylated on some or all of the serine and threonine CC residues present in the C-terminal region (By similarity). CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC Opsin subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X80072; CAA56378.1; -; mRNA. DR HSSP; P02699; 1F88. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR001760; Opsin. DR InterPro; IPR000856; Opsin_RH3/RH4. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR00238; OPSIN. DR PRINTS; PR00577; OPSINRH3RH4. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR PROSITE; PS00238; OPSIN; 1. KW Chromophore; G-protein coupled receptor; Glycoprotein; Membrane; KW Phosphorylation; Photoreceptor protein; Receptor; Retinal protein; KW Sensory transduction; Transducer; Transmembrane; Vision. FT CHAIN 1 380 Opsin-2. FT /FTId=PRO_0000197636. FT TOPO_DOM 1 51 Extracellular. FT TRANSMEM 52 76 1 (Potential). FT TOPO_DOM 77 88 Cytoplasmic. FT TRANSMEM 89 115 2 (Potential). FT TOPO_DOM 116 128 Extracellular. FT TRANSMEM 129 148 3 (Potential). FT TOPO_DOM 149 166 Cytoplasmic. FT TRANSMEM 167 191 4 (Potential). FT TOPO_DOM 192 215 Extracellular. FT TRANSMEM 216 243 5 (Potential). FT TOPO_DOM 244 279 Cytoplasmic. FT TRANSMEM 280 303 6 (Potential). FT TOPO_DOM 304 311 Extracellular. FT TRANSMEM 312 336 7 (Potential). FT TOPO_DOM 337 380 Cytoplasmic. FT BINDING 323 323 Retinal chromophore (covalent) (By FT similarity). FT CARBOHYD 3 3 N-linked (GlcNAc...) (Potential). FT DISULFID 125 202 Potential. SQ SEQUENCE 380 AA; 42531 MW; 113504F71027C07A CRC64; MVNTTDFYPV PAAMAYESSV GLPLLGWNVP TEHLDLVHPH WRSFQVPNKY WHFGLAFVYF MLMCMSSLGN GIVLWIYATT KSIRTPSNMF IVNLALFDVL MLLEMPMLVV SSLFYQRPVG WELGCDIYAA LGSVAGIGSA INNAAIAFDR YRTISCPIDG RLTQGQVLAL IAGTWVWTLP FTLMPLLRIW SRFTAEGFLT TCSFDYLTDD EDTKVFVGCI FAWSYAFPLC LICCFYYRLI GAVREHEKML RDQAKKMNVK SLQSNADTEA QSAEIRIAKV ALTIFFLFLC SWTPYAVVAM IGAFGNRAAL TPLSTMIPAV TAKIVSCIDP WVYAINHPRF RAEVQKRMKW LHLGEDARSS KSDTSSTATD RTVGNVSASA // ID AQP1_HUMAN Reviewed; 269 AA. AC P29972; Q8TBI5; Q8TDC1; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 20-MAR-2007, entry version 85. DE Aquaporin-1 (AQP-1) (Aquaporin-CHIP) (Water channel protein for red DE blood cells and kidney proximal tubule) (Urine water channel). GN Name=AQP1; Synonyms=CHIP28; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RX MEDLINE=92107900; PubMed=1722319; RA Preston G.M., Agre P.; RT "Isolation of the cDNA for erythrocyte integral membrane protein of 28 RT kilodaltons: member of an ancient channel family."; RL Proc. Natl. Acad. Sci. U.S.A. 88:11110-11114(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=93340184; PubMed=8340403; RA Moon C., Preston G.M., Griffin C.A., Jabs E.W., Agre P.; RT "The human aquaporin-CHIP gene. Structure, organization, and RT chromosomal localization."; RL J. Biol. Chem. 268:15772-15778(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Retinal pigment epithelium; RX MEDLINE=96326579; PubMed=8703970; DOI=10.1016/0005-2736(96)00076-4; RA Ruiz A.C., Bok D.; RT "Characterization of the 3' UTR sequence encoded by the AQP-1 gene in RT human retinal pigment epithelium."; RL Biochim. Biophys. Acta 1282:174-178(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Uterus; RX MEDLINE=94290349; PubMed=7517253; RA Li X., Yu H., Koide S.S.; RT "The water channel gene in human uterus."; RL Biochem. Mol. Biol. Int. 32:371-377(1994). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-45 AND ASP-165. RA Rieder M.J., Johanson E.J., da Ponte S.H., Hastings N.C., Ahearn M.O., RA Bertucci C.B., Wong M.W., Yi Q., Nickerson D.A.; RT "SeattleSNPs. NHLBI HL66682 program for genomic applications, UW- RT FHCRC, Seattle, WA (URL: http://pga.gs.washington.edu)."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE OF 5-269. RC TISSUE=Articular cartilage; RA Trujillo E., Gonzalez T., Martin-Vasallo P., Marples D., Mobasheri A.; RT "Human chondrocytes in situ express aquaporin water channels: changes RT in AQP1 abundance in pathologies of articular cartilage."; RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases. RN [9] RP PROTEIN SEQUENCE OF 2-36. RX PubMed=2007592; RA Smith B.L., Agre P.; RT "Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit RT oligomer similar to channel proteins."; RL J. Biol. Chem. 266:6407-6415(1991). RN [10] RP FUNCTION. RX MEDLINE=92229472; PubMed=1373524; RA Preston G.M., Carroll T.P., Guggino W.B., Agre P.; RT "Appearance of water channels in Xenopus oocytes expressing red cell RT CHIP28 protein."; RL Science 256:385-387(1992). RN [11] RP TARGET OF MERCURY INHIBITION. RX MEDLINE=93106996; PubMed=7677994; RA Preston G.M., Jung J.S., Guggino W.B., Agre P.; RT "The mercury-sensitive residue at cysteine 189 in the CHIP28 water RT channel."; RL J. Biol. Chem. 268:17-20(1993). RN [12] RP TOPOLOGY. RX MEDLINE=94124503; PubMed=7507481; RA Preston G.M., Jung J.S., Guggino W.B., Agre P.; RT "Membrane topology of aquaporin CHIP. Analysis of functional epitope- RT scanning mutants by vectorial proteolysis."; RL J. Biol. Chem. 269:1668-1673(1994). RN [13] RP STRUCTURE BY ELECTRON MICROSCOPY (1.6 ANGSTROMS). RX MEDLINE=94313979; PubMed=7518771; RA Walz T., Smith B.L., Agre P., Engel A.; RT "The three-dimensional structure of human erythrocyte aquaporin RT CHIP."; RL EMBO J. 13:2985-2993(1994). RN [14] RP STRUCTURE BY ELECTRON MICROSCOPY (6 ANGSTROMS). RX MEDLINE=97320502; PubMed=9177353; DOI=10.1038/42512; RA Walz T., Hirai T., Murata K., Heymann J.B., Mitsuoka K., Fujiyoshi Y., RA Smith B.L., Agre P., Engel A.; RT "The three-dimensional structure of aquaporin-1."; RL Nature 387:624-627(1997). RN [15] RP STRUCTURE BY ELECTRON MICROSCOPY (3.8 ANGSTROMS). RX MEDLINE=20487015; PubMed=11034202; DOI=10.1038/35036519; RA Murata K., Mitsuoka K., Hirai T., Walz T., Agre P., Heymann J.B., RA Engel A., Fujiyoshi Y.; RT "Structural determinants of water permeation through aquaporin-1."; RL Nature 407:599-605(2000). RN [16] RP STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS). RX MEDLINE=21423577; PubMed=11532455; DOI=10.1016/S0014-5793(01)02743-0; RA de Groot B.L., Engel A., Grubmueller H.; RT "A refined structure of human aquaporin-1."; RL FEBS Lett. 504:206-211(2001). RN [17] RP STRUCTURE BY ELECTRON MICROSCOPY (3.7 ANGSTROMS). RX PubMed=11171962; DOI=10.1073/pnas.041489198; RA Ren G., Reddy V.S., Cheng A., Melnyk P., Mitra A.K.; RT "Visualization of a water-selective pore by electron crystallography RT in vitreous ice."; RL Proc. Natl. Acad. Sci. U.S.A. 98:1398-1403(2001). RN [18] RP VARIANT BLOOD GROUP COLTON VAL-45. RX MEDLINE=94365170; PubMed=7521882; RA Smith B.L., Preston G.M., Spring F., Anstee D.J., Agre P.; RT "Human red cell aquaporin CHIP. I. Molecular characterization of ABH RT and Colton blood group antigens."; RL J. Clin. Invest. 94:1043-1049(1994). RN [19] RP VARIANT LEU-38. RX MEDLINE=94360246; PubMed=7521540; RA Preston G.M., Smith B.L., Zeidel M.L., Moulds J.J., Agre P.; RT "Mutations in aquaporin-1 in phenotypically normal humans without RT functional CHIP water channels."; RL Science 265:1585-1587(1994). CC -!- FUNCTION: Forms a water-specific channel that provides the plasma CC membranes of red cells and kidney proximal tubules with high CC permeability to water, thereby permitting water to move in the CC direction of an osmotic gradient. CC -!- SUBUNIT: Homotetramer. CC -!- SUBCELLULAR LOCATION: Membrane; multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed in a number of tissues including CC erythrocytes, renal tubules, retinal pigment epithelium, heart, CC lung, skeletal muscle, kidney and pancreas. Weakly expressed in CC brain, placenta and liver. CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing CC three membrane-spanning domains and a pore-forming loop with the CC signature motif Asn-Pro-Ala (NPA). CC -!- POLYMORPHISM: AQP1 is responsible for the Colton blood group CC system. Approximately 92% of Caucasians are Co(A+B-) (Ala-46), CC approximately 8% are Co(A+B+), and only 0.2% are Co(A-B+) (Val- CC 46). Co(A-B-) which is very rare, is due to a complete absence of CC AQP1. CC -!- MISCELLANEOUS: Pharmacologically inhibited by submillimolar CC concentrations of mercury. CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. CC -!- WEB RESOURCE: NAME=BGMUT; CC NOTE=Blood group antigen gene mutation database"; CC URL="http://www.ncbi.nlm.nih.gov/projects/mhc/xslcgi.fcgi?cmd=bgmut/systems_info&system=colton". CC -!- WEB RESOURCE: NAME=Protein Spotlight; CC NOTE=Liquid states - Issue 36 of July 2003; CC URL="http://www.expasy.org/spotlight/back_issues/sptlt036.shtml". CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M77829; AAA58425.1; -; mRNA. DR EMBL; U41517; AAC50648.1; -; mRNA. DR EMBL; U41518; AAC50649.1; -; mRNA. DR EMBL; S73482; AAB31193.1; -; mRNA. DR EMBL; AC004691; AAC16481.1; -; Genomic_DNA. DR EMBL; AC005155; AAC23788.1; -; Genomic_DNA. DR EMBL; AY953319; AAX24129.1; -; Genomic_DNA. DR EMBL; BC022486; AAH22486.1; -; mRNA. DR EMBL; AF480415; AAL87136.1; -; Genomic_DNA. DR PIR; A41616; A41616. DR UniGene; Hs.312228; -. DR UniGene; Hs.76152; -. DR PDB; 1FQY; EM; A=1-269. DR PDB; 1H6I; EM; A=1-269. DR PDB; 1IH5; EM; A=1-269. DR Ensembl; ENSG00000106125; Homo sapiens. DR KEGG; hsa:358; -. DR H-InvDB; HIX0006573; -. DR HGNC; HGNC:633; AQP1. DR HPA; CAB001707; -. DR MIM; 107776; gene. DR MIM; 110450; phenotype. DR ArrayExpress; P29972; -. DR GermOnline; ENSG00000106125; Homo sapiens. DR RZPD-ProtExp; RZPDo839D02147; -. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0005372; F:water transporter activity; TAS:ProtInc. DR GO; GO:0007588; P:excretion; TAS:ProtInc. DR GO; GO:0006833; P:water transport; TAS:ProtInc. DR InterPro; IPR012269; AQP. DR InterPro; IPR000425; MIP. DR Gene3D; G3DSA:1.20.1080.10; MIP; 1. DR Pfam; PF00230; MIP; 1. DR PIRSF; PIRSF002276; AQP; 1. DR PRINTS; PR00783; MINTRINSICP. DR ProDom; PD000295; MIP; 1. DR TIGRFAMs; TIGR00861; MIP; 1. DR PROSITE; PS00221; MIP; 1. KW 3D-structure; Blood group antigen; Direct protein sequencing; KW Glycoprotein; Membrane; Polymorphism; Repeat; Transmembrane; KW Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 269 Aquaporin-1. FT /FTId=PRO_0000063920. FT TOPO_DOM 2 7 Cytoplasmic. FT TRANSMEM 8 36 Helix 1. FT TOPO_DOM 37 48 Extracellular. FT TRANSMEM 49 66 Helix 2. FT TOPO_DOM 67 70 Cytoplasmic. FT TOPO_DOM 71 76 In membrane. FT TRANSMEM 77 84 Helix B. FT TOPO_DOM 85 94 Cytoplasmic. FT TRANSMEM 95 115 Helix 3. FT TOPO_DOM 116 136 Extracellular. FT TRANSMEM 137 155 Helix 4. FT TOPO_DOM 156 166 Cytoplasmic. FT TRANSMEM 167 183 Helix 5. FT TOPO_DOM 184 186 Extracellular. FT TOPO_DOM 187 192 In membrane. FT TRANSMEM 193 200 Helix E. FT TOPO_DOM 201 207 Extracellular. FT TRANSMEM 208 228 Helix 6. FT TOPO_DOM 229 269 Cytoplasmic. FT MOTIF 76 78 NPA 1. FT MOTIF 192 194 NPA 2. FT COMPBIAS 159 162 Poly-Arg. FT SITE 56 56 Substrate discrimination. FT SITE 180 180 Substrate discrimination. FT SITE 189 189 Hg(2+)-sensitive residue. FT SITE 195 195 Substrate discrimination. FT CARBOHYD 42 42 N-linked (GlcNAc...). FT CARBOHYD 205 205 N-linked (GlcNAc...) (Potential). FT VARIANT 38 38 P -> L (in Co(A-B-) antigen; non FT functional AQP1; red cells show low FT osmotic water permeability). FT /FTId=VAR_013279. FT VARIANT 45 45 A -> V (in Co(A-B+) antigen). FT /FTId=VAR_004400. FT VARIANT 165 165 G -> D. FT /FTId=VAR_022318. FT CONFLICT 45 45 A -> T (in Ref. 7; AAH22486). FT HELIX 8 35 FT STRAND 37 42 FT HELIX 48 65 FT STRAND 68 71 FT HELIX 76 83 FT HELIX 94 114 FT TURN 119 122 FT STRAND 132 135 FT HELIX 136 154 FT HELIX 166 182 FT TURN 183 185 FT HELIX 192 199 FT HELIX 207 227 SQ SEQUENCE 269 AA; 28526 MW; BA204D82FB26352E CRC64; MASEFKKKLF WRAVVAEFLA TTLFVFISIG SALGFKYPVG NNQTAVQDNV KVSLAFGLSI ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS IFRALMYIIA QCVGAIVATA ILSGITSSLT GNSLGRNDLA DGVNSGQGLG IEIIGTLQLV LCVLATTDRR RRDLGGSAPL AIGLSVALGH LLAIDYTGCG INPARSFGSA VITHNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDLTD RVKVWTSGQV EEYDLDADDI NSRVEMKPK // ID IFNA2_HUMAN Reviewed; 188 AA. AC P01563; P01564; Q14606; Q96KI6; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 20-FEB-2007, entry version 79. DE Interferon alpha-2 precursor (Interferon alpha-A) (LeIF A). GN Name=IFNA2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX MEDLINE=81052322; PubMed=6159538; DOI=10.1038/287411a0; RA Goeddel D.V., Yelverton E., Ullrich A., Heyneker H.L., Miozzari G., RA Holmes W., Seeburg P.H., Dull T.J., May L., Stebbing N., Crea R., RA Maeda S., McCandliss R., Sloma A., Tabor J.M., Gross M., RA Familletti P.C., Pestka S.; RT "Human leukocyte interferon produced by E. coli is biologically RT active."; RL Nature 287:411-416(1980). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX MEDLINE=81148795; PubMed=6163083; DOI=10.1038/290020a0; RA Goeddel D.V., Leung D.W., Dull T.J., Gross M., Lawn R.M., RA McCandliss R., Seeburg P.H., Ullrich A., Yelverton E., Gray P.W.; RT "The structure of eight distinct cloned human leukocyte interferon RT cDNAs."; RL Nature 290:20-26(1981). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX MEDLINE=82060261; PubMed=6170983; RA Lawn R.M., Gross M., Houck C.M., Franke A.E., Gray P.V., Goeddel D.V.; RT "DNA sequence of a major human leukocyte interferon gene."; RL Proc. Natl. Acad. Sci. U.S.A. 78:5435-5439(1981). RN [4] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Bone marrow tumor; RX MEDLINE=86069501; PubMed=3906813; RA Oliver G., Balbas P., Valle F., Soberon X., Bolivar F.; RT "Cloning of human leukocyte interferon cDNA and a strategy for its RT production in E. coli."; RL Rev. Latinoam. Microbiol. 27:141-150(1985). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Placenta; RX MEDLINE=98357449; PubMed=9694076; RA Austruy E., Bagnis C., Carbuccia N., Maroc C., Birg F., Dubreuil P., RA Mannoni P., Chabannon C.; RT "A defective retroviral vector encoding human interferon alpha 2 can RT transduce human leukemic cell lines."; RL Cancer Gene Ther. 5:247-256(1998). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 7-188. RX MEDLINE=81015442; PubMed=6158094; RA Streuli M., Nagata S., Weissmann C.; RT "At least three human type alpha interferons: structure of alpha 2."; RL Science 209:1343-1347(1980). RN [7] RP NUCLEOTIDE SEQUENCE OF 24-188. RX MEDLINE=83299241; PubMed=6310510; DOI=10.1093/nar/11.16.5661; RA Weber H., Weissmann C.; RT "Formation of genes coding for hybrid proteins by recombination RT between related, cloned genes in E. coli."; RL Nucleic Acids Res. 11:5661-5669(1983). RN [8] RP PROTEIN SEQUENCE OF 24-112 AND 136-188. RX MEDLINE=81052321; PubMed=6159537; DOI=10.1038/287408a0; RA Allen G., Fantes K.H.; RT "A family of structural genes for human lymphoblastoid (leukocyte- RT type) interferon."; RL Nature 287:408-411(1980). RN [9] RP PROTEIN SEQUENCE OF 24-58. RX MEDLINE=98087498; PubMed=9425112; RA Nyman T.A., Toeloe H., Parkkinen J., Kalkkinen N.; RT "Identification of nine interferon-alpha subtypes produced by Sendai RT virus-induced human peripheral blood leucocytes."; RL Biochem. J. 329:295-302(1998). RN [10] RP DISULFIDE BONDS. RX MEDLINE=81123083; PubMed=6162107; DOI=10.1038/289606a0; RA Wetzel R.; RT "Assignment of the disulphide bonds of leukocyte interferon."; RL Nature 289:606-607(1981). RN [11] RP GLYCOSYLATION AT THR-129, AND VARIANTS ALPHA-2B AND ALPHA-2C. RX MEDLINE=91264809; PubMed=2049076; RA Adolf G.R., Kalsner I., Ahorn H., Maurer-Fogy I., Cantell K.; RT "Natural human interferon-alpha 2 is O-glycosylated."; RL Biochem. J. 276:511-518(1991). RN [12] RP POLYMORPHISM. RX MEDLINE=95353982; PubMed=7627809; RA Lee N., Ni D., Brissette R., Chou M., Hussain M., Gill D.S., RA Liao M.-J., Testa D.; RT "Interferon-alpha 2 variants in the human genome."; RL J. Interferon Cytokine Res. 15:341-349(1995). RN [13] RP 3D-STRUCTURE MODELING. RX MEDLINE=94052087; PubMed=8234245; DOI=10.1002/prot.340170109; RA Murgolo N.J., Windsor W.T., Hruza A., Reichert P., Tsarbopoulos A., RA Baldwin S., Huang E., Pramanik B., Ealick S., Trotta P.P.; RT "A homology model of human interferon alpha-2."; RL Proteins 17:62-74(1993). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). RX MEDLINE=97148339; PubMed=8994971; DOI=10.1016/S0969-2126(96)00152-9; RA Radhakrishnan R., Walter L.J., Hruza A., Reichert P., Trotta P.P., RA Nagabhushan T.L., Walter M.R.; RT "Zinc mediated dimer of human interferon-alpha 2b revealed by X-ray RT crystallography."; RL Structure 4:1453-1463(1996). RN [15] RP STRUCTURE BY NMR. RX MEDLINE=98118493; PubMed=9417943; DOI=10.1006/jmbi.1997.1396; RA Klaus W., Gsell B., Labhardt A.M., Wipf B., Senn H.; RT "The three-dimensional high resolution structure of human interferon RT alpha-2a determined by heteronuclear NMR spectroscopy in solution."; RL J. Mol. Biol. 274:661-675(1997). CC -!- FUNCTION: Produced by macrophages, IFN-alpha have antiviral CC activities. Interferon stimulates the production of two enzymes: a CC protein kinase and an oligoadenylate synthetase. CC -!- SUBCELLULAR LOCATION: Secreted protein. CC -!- POLYMORPHISM: Three forms exist; alpha-2a (shown here), alpha-2b CC and alpha-2c. CC -!- PHARMACEUTICAL: Available under the names Roferon-A (Roche) or CC Intron-A (Schering-Plough). Used as an anticancer drug for its CC antiproliferative activity. CC -!- SIMILARITY: Belongs to the alpha/beta interferon family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J00207; AAB59402.1; -; Genomic_DNA. DR EMBL; V00544; CAA23805.1; -; mRNA. DR EMBL; V00548; CAA23809.1; -; mRNA. DR EMBL; V00549; CAA23810.1; -; mRNA. DR EMBL; Y11834; CAA72532.1; -; Genomic_DNA. DR EMBL; M54886; AAA59181.1; -; mRNA. DR EMBL; M29883; AAA52715.1; -; Genomic_DNA. DR EMBL; A04970; CAA00410.1; -; Unassigned_DNA. DR PIR; A93234; IVHUA2. DR PIR; I78570; I78570. DR UniGene; Hs.211575; -. DR PDB; 1ITF; NMR; @=24-188. DR PDB; 1RH2; X-ray; A/B/C/D/E/F=24-188. DR PDB; 2HIE; Model; @=24-188. DR DIP; DIP:3784N; -. DR DIP; DIP:481N; -. DR GlycoSuiteDB; P01563; -. DR Ensembl; ENSG00000188379; Homo sapiens. DR KEGG; hsa:3440; -. DR HGNC; HGNC:5423; IFNA2. DR MIM; 147562; gene. DR LinkHub; P01563; -. DR ArrayExpress; P01563; -. DR GermOnline; ENSG00000188379; Homo sapiens. DR RZPD-ProtExp; A0813; -. DR RZPD-ProtExp; IOH35221; -. DR RZPD-ProtExp; RZPDo834E0933; -. DR GO; GO:0005132; F:interferon-alpha/beta receptor binding; TAS:ProtInc. DR GO; GO:0007166; P:cell surface receptor linked signal transdu...; TAS:ProtInc. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0006917; P:induction of apoptosis; TAS:ProtInc. DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. DR InterPro; IPR009079; 4_helix_cytokine. DR InterPro; IPR000471; Interferon_abd. DR Gene3D; G3DSA:1.20.120.210; Interferon_abd; 1. DR PANTHER; PTHR11691; Interferon_abd; 1. DR Pfam; PF00143; Interferon; 1. DR PRINTS; PR00266; INTERFERONAB. DR ProDom; PD000550; Interferon_abd; 1. DR SMART; SM00076; IFabd; 1. DR PROSITE; PS00252; INTERFERON_A_B_D; 1. KW 3D-structure; Antiviral defense; Cytokine; Direct protein sequencing; KW Glycoprotein; Pharmaceutical; Polymorphism; Signal. FT SIGNAL 1 23 FT CHAIN 24 188 Interferon alpha-2. FT /FTId=PRO_0000016360. FT CARBOHYD 129 129 O-linked (GalNAc...). FT /FTId=CAR_000049. FT DISULFID 24 121 FT DISULFID 52 161 FT VARIANT 46 46 K -> R (in alpha-2B and alpha-2C). FT /FTId=VAR_004012. FT VARIANT 57 57 H -> R (in alpha-2C). FT /FTId=VAR_013001. FT HELIX 33 44 FT TURN 49 54 FT HELIX 63 66 FT HELIX 76 91 FT HELIX 93 98 FT HELIX 101 123 FT TURN 126 127 FT TURN 133 133 FT HELIX 134 155 FT TURN 156 157 FT HELIX 160 178 FT TURN 179 182 SQ SEQUENCE 188 AA; 21550 MW; 101DD21D394CBF97 CRC64; MALTFALLVA LLVLSCKSSC SVGCDLPQTH SLGSRRTLML LAQMRKISLF SCLKDRHDFG FPQEEFGNQF QKAETIPVLH EMIQQIFNLF STKDSSAAWD ETLLDKFYTE LYQQLNDLEA CVIQGVGVTE TPLMKEDSIL AVRKYFQRIT LYLKEKKYSP CAWEVVRAEI MRSFSLSTNL QESLRSKE //