ID VTDB_HUMAN Reviewed; 474 AA. AC P02774; B4DPP2; D6RAK8; Q16309; Q16310; Q53F31; Q6GTG1; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 27-MAY-2015, entry version 174. DE RecName: Full=Vitamin D-binding protein; DE Short=DBP; DE Short=VDB; DE AltName: Full=Gc-globulin; DE AltName: Full=Group-specific component; DE Flags: Precursor; GN Name=GC; 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 1), AND VARIANTS GLU-432 AND RP THR-436. RX PubMed=2416779; DOI=10.1172/JCI112256; RA Cooke N.E., David E.V.; RT "Serum vitamin D-binding protein is a third member of the albumin and RT alpha fetoprotein gene family."; RL J. Clin. Invest. 76:2420-2424(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2415977; DOI=10.1073/pnas.82.23.7994; RA Yang F., Brune J.L., Naylor S.L., Cupples R.L., Naberhaus K.H., RA Bowman B.H.; RT "Human group-specific component (Gc) is a member of the albumin RT family."; RL Proc. Natl. Acad. Sci. U.S.A. 82:7994-7998(1985). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-432 AND THR-436. RX PubMed=7505619; DOI=10.1016/0167-4781(93)90005-X; RA Braun A., Kofler A., Morawietz S., Cleve H.; RT "Sequence and organization of the human vitamin D-binding protein RT gene."; RL Biochim. Biophys. Acta 1216:385-394(1993). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-432 AND THR-436. RX PubMed=8325650; DOI=10.1006/geno.1993.1258; RA Witke W.F., Gibbs P.E., Zielinski R., Yang F., Bowman B.H., RA Dugaiczyk A.; RT "Complete structure of the human Gc gene: differences and similarities RT between members of the albumin gene family."; RL Genomics 16:751-754(1993). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1-47 (ISOFORM 2), AND VARIANTS GLU-432; RP THR-436 AND HIS-445. RC TISSUE=Liver; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS RP GLU-432 AND THR-436. RC TISSUE=Kidney; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS THR-436 RP AND HIS-445. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS GLU-432 RP AND THR-436. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP THR-436. RC TISSUE=Liver; 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 [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19. RX PubMed=2958390; DOI=10.1016/0378-1119(87)90499-9; RA Yang F., Naberhaus K.H., Adrian G.S., Gardella J.M., Brissenden J.E., RA Bowman B.H.; RT "The vitamin D-binding protein gene contains conserved nucleotide RT sequences that respond to heavy metal, adipocyte and mitotic RT signals."; RL Gene 54:285-290(1987). RN [11] RP PROTEIN SEQUENCE OF 17-474. RX PubMed=2423133; DOI=10.1016/0167-4838(86)90173-1; RA Schoentgen F., Metz-Boutigue M.-H., Jolles J., Constans J., Jolles P.; RT "Complete amino acid sequence of human vitamin D-binding protein RT (group-specific component): evidence of a three-fold internal homology RT as in serum albumin and alpha-fetoprotein."; RL Biochim. Biophys. Acta 871:189-198(1986). RN [12] RP PROTEIN SEQUENCE OF 17-31 AND 431-441. RX PubMed=218624; DOI=10.1021/bi00575a036; RA Svasti J., Kurosky A., Bennett A., Bowman B.H.; RT "Molecular basis for the three major forms of human serum vitamin D RT binding protein (group-specific component)."; RL Biochemistry 18:1611-1617(1979). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 430-446, VARIANTS GC*1A1 THR-436 RP AND HIS-445, AND VARIANT GC*2A9 CYS-445. RX PubMed=7725672; DOI=10.1111/j.1423-0410.1995.tb02545.x; RA Kofler A., Braun A., Jenkins T., Serjeantson S.W., Cleve H.; RT "Characterization of mutants of the vitamin-D-binding protein/group RT specific component: GC aborigine (1A1) from Australian aborigines and RT South African blacks, and 2A9 from south Germany."; RL Vox Sang. 68:50-54(1995). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP VARIANTS GC*2; GC*1F AND GC*1S. RX PubMed=1352271; DOI=10.1007/BF00194311; RA Braun A., Bichlmaier R., Cleve H.; RT "Molecular analysis of the gene for the human vitamin-D-binding RT protein (group-specific component): allelic differences of the common RT genetic GC types."; RL Hum. Genet. 89:401-406(1992). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 29-473. RX PubMed=11799400; DOI=10.1038/nsb754; RA Verboven C., Rabijns A., De Maeyer M., Van Baelen H., Bouillon R., RA De Ranter C.; RT "A structural basis for the unique binding features of the human RT vitamin D-binding protein."; RL Nat. Struct. Biol. 9:131-136(2002). RN [17] RP VARIANT [LARGE SCALE ANALYSIS] THR-436, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Multifunctional protein found in plasma, ascitic fluid, CC cerebrospinal fluid, and urine and on the surface of many cell CC types. In plasma, it carries the vitamin D sterols and prevents CC polymerization of actin by binding its monomers. DBP associates CC with membrane-bound immunoglobulin on the surface of B-lymphocytes CC and with IgG Fc receptor on the membranes of T-lymphocytes. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P02774-1; Sequence=Displayed; CC Name=2; CC IsoId=P02774-2; Sequence=VSP_038427; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC Name=3; CC IsoId=P02774-3; Sequence=VSP_044523; CC Note=No experimental confirmation available.; CC -!- POLYMORPHISM: Over 80 variants of human DBP have been identified. CC The three most common alleles are called GC*1F, GC*1S, and GC*2. CC The sequence shown is that of the GC*2 allele. CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. CC {ECO:0000255|PROSITE-ProRule:PRU00769}. CC -!- SIMILARITY: Contains 3 albumin domains. {ECO:0000255|PROSITE- CC ProRule:PRU00769}. CC -!- SEQUENCE CAUTION: CC Sequence=BAG60654.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M12654; AAA52173.1; -; mRNA. DR EMBL; X03178; CAA26938.1; -; mRNA. DR EMBL; S67480; AAB29423.1; -; Genomic_DNA. DR EMBL; S67474; AAB29423.1; JOINED; Genomic_DNA. DR EMBL; S67476; AAB29423.1; JOINED; Genomic_DNA. DR EMBL; S67478; AAB29423.1; JOINED; Genomic_DNA. DR EMBL; S67479; AAB29423.1; JOINED; Genomic_DNA. DR EMBL; S67526; AAB29423.1; JOINED; Genomic_DNA. DR EMBL; L10641; AAA61704.1; -; Genomic_DNA. DR EMBL; AK290827; BAF83516.1; -; mRNA. DR EMBL; AK298433; BAG60654.1; ALT_SEQ; mRNA. DR EMBL; AK309595; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK315853; BAF98744.1; -; mRNA. DR EMBL; AK223458; BAD97178.1; -; mRNA. DR EMBL; AC024722; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471057; EAX05645.1; -; Genomic_DNA. DR EMBL; BC057228; AAH57228.1; -; mRNA. DR EMBL; M17156; AAA19662.2; -; Genomic_DNA. DR EMBL; S77129; AAD14249.1; ALT_SEQ; Genomic_DNA. DR EMBL; S77130; AAD14250.1; ALT_SEQ; Genomic_DNA. DR CCDS; CCDS3550.1; -. [P02774-1] DR CCDS; CCDS56332.1; -. [P02774-3] DR PIR; A94076; VYHUD. DR RefSeq; NP_000574.2; NM_000583.3. DR RefSeq; NP_001191235.1; NM_001204306.1. DR RefSeq; NP_001191236.1; NM_001204307.1. DR UniGene; Hs.418497; -. DR PDB; 1J78; X-ray; 2.31 A; A/B=17-474. DR PDB; 1J7E; X-ray; 2.55 A; A/B=17-474. DR PDB; 1KW2; X-ray; 2.15 A; A/B=17-474. DR PDB; 1KXP; X-ray; 2.10 A; D=17-474. DR PDB; 1LOT; X-ray; 2.50 A; A=17-474. DR PDB; 1MA9; X-ray; 2.40 A; A=17-474. DR PDBsum; 1J78; -. DR PDBsum; 1J7E; -. DR PDBsum; 1KW2; -. DR PDBsum; 1KXP; -. DR PDBsum; 1LOT; -. DR PDBsum; 1MA9; -. DR ProteinModelPortal; P02774; -. DR SMR; P02774; 20-474. DR BioGrid; 108908; 20. DR DIP; DIP-17038N; -. DR IntAct; P02774; 7. DR MINT; MINT-239255; -. DR STRING; 9606.ENSP00000273951; -. DR BindingDB; P02774; -. DR ChEMBL; CHEMBL2259; -. DR DrugBank; DB01436; Alfacalcidol. DR DrugBank; DB00169; Cholecalciferol. DR PhosphoSite; P02774; -. DR UniCarbKB; P02774; -. DR BioMuta; GC; -. DR DMDM; 139641; -. DR DOSAC-COBS-2DPAGE; P02774; -. DR REPRODUCTION-2DPAGE; IPI00555812; -. DR REPRODUCTION-2DPAGE; P02774; -. DR SWISS-2DPAGE; P02774; -. DR PaxDb; P02774; -. DR PeptideAtlas; P02774; -. DR PRIDE; P02774; -. DR Ensembl; ENST00000273951; ENSP00000273951; ENSG00000145321. DR Ensembl; ENST00000504199; ENSP00000421725; ENSG00000145321. DR GeneID; 2638; -. DR KEGG; hsa:2638; -. DR CTD; 2638; -. DR GeneCards; GC04M072596; -. DR HGNC; HGNC:4187; GC. DR HPA; CAB008596; -. DR HPA; HPA001526; -. DR HPA; HPA019855; -. DR MIM; 139200; gene. DR neXtProt; NX_P02774; -. DR PharmGKB; PA28601; -. DR eggNOG; NOG40465; -. DR HOGENOM; HOG000140946; -. DR HOVERGEN; HBG009729; -. DR InParanoid; P02774; -. DR KO; K12258; -. DR OrthoDB; EOG7B05CR; -. DR PhylomeDB; P02774; -. DR TreeFam; TF335561; -. DR Reactome; REACT_13523; Vitamin D (calciferol) metabolism. DR ChiTaRS; GC; human. DR EvolutionaryTrace; P02774; -. DR GeneWiki; Vitamin_D-binding_protein; -. DR GenomeRNAi; 2638; -. DR NextBio; 10400; -. DR PRO; PR:P02774; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; P02774; -. DR CleanEx; HS_GC; -. DR ExpressionAtlas; P02774; baseline and differential. DR Genevestigator; P02774; -. DR GO; GO:0072562; C:blood microparticle; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome. DR GO; GO:0003779; F:actin binding; IPI:UniProtKB. DR GO; GO:1902118; F:calcidiol binding; IDA:UniProtKB. DR GO; GO:0005499; F:vitamin D binding; TAS:ProtInc. DR GO; GO:0051183; F:vitamin transporter activity; IEA:InterPro. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0008202; P:steroid metabolic process; TAS:Reactome. DR GO; GO:0042359; P:vitamin D metabolic process; TAS:Reactome. DR GO; GO:0051180; P:vitamin transport; TAS:ProtInc. DR InterPro; IPR000264; ALB/AFP/VDB. DR InterPro; IPR020858; Serum_albumin-like. DR InterPro; IPR020857; Serum_albumin_CS. DR InterPro; IPR014760; Serum_albumin_N. DR InterPro; IPR000213; VitD-bd. DR InterPro; IPR015247; VitD-bind_III. DR Pfam; PF00273; Serum_albumin; 2. DR Pfam; PF09164; VitD-bind_III; 1. DR PRINTS; PR00802; SERUMALBUMIN. DR PRINTS; PR00804; VITAMNDBNDNG. DR SMART; SM00103; ALBUMIN; 2. DR SUPFAM; SSF48552; SSF48552; 3. DR PROSITE; PS00212; ALBUMIN_1; 1. DR PROSITE; PS51438; ALBUMIN_2; 2. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Alternative splicing; Complete proteome; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Polymorphism; KW Reference proteome; Repeat; Secreted; Signal; Transport; Vitamin D. FT SIGNAL 1 16 {ECO:0000269|PubMed:218624, FT ECO:0000269|PubMed:2423133}. FT CHAIN 17 474 Vitamin D-binding protein. FT /FTId=PRO_0000001102. FT DOMAIN 17 208 Albumin 1. {ECO:0000255|PROSITE- FT ProRule:PRU00769}. FT DOMAIN 209 394 Albumin 2. {ECO:0000255|PROSITE- FT ProRule:PRU00769}. FT DOMAIN 395 474 Albumin 3. {ECO:0000255|PROSITE- FT ProRule:PRU00769}. FT CARBOHYD 288 288 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 29 75 FT DISULFID 74 83 {ECO:0000255|PROSITE-ProRule:PRU00769}. FT DISULFID 96 112 FT DISULFID 111 122 FT DISULFID 145 190 FT DISULFID 189 198 FT DISULFID 220 266 FT DISULFID 265 273 FT DISULFID 286 300 FT DISULFID 299 311 FT DISULFID 335 376 FT DISULFID 375 384 FT DISULFID 407 453 FT DISULFID 452 462 FT VAR_SEQ 1 122 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_038427. FT VAR_SEQ 1 1 M -> MLWSWSEERGGAARLSGRKM (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_044523. FT VARIANT 432 432 D -> E (in allele GC*1S; dbSNP:rs7041). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:2416779, FT ECO:0000269|PubMed:7505619, FT ECO:0000269|PubMed:8325650, FT ECO:0000269|Ref.6, ECO:0000269|Ref.8}. FT /FTId=VAR_000548. FT VARIANT 436 436 K -> T (in allele GC*1F, allele GC*1A1 FT and allele GC*1S; dbSNP:rs4588). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:15815621, FT ECO:0000269|PubMed:2416779, FT ECO:0000269|PubMed:24275569, FT ECO:0000269|PubMed:7505619, FT ECO:0000269|PubMed:7725672, FT ECO:0000269|PubMed:8325650, FT ECO:0000269|Ref.6, ECO:0000269|Ref.8}. FT /FTId=VAR_000549. FT VARIANT 445 445 R -> C (in allele GC*2A9). FT {ECO:0000269|PubMed:7725672}. FT /FTId=VAR_014120. FT VARIANT 445 445 R -> H (in allele GC*1A1; dbSNP:rs9016). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15815621, FT ECO:0000269|PubMed:7725672}. FT /FTId=VAR_014121. FT CONFLICT 168 168 G -> E (in Ref. 1; AAA52173). FT {ECO:0000305}. FT CONFLICT 183 183 L -> P (in Ref. 5; AK309595). FT {ECO:0000305}. FT CONFLICT 327 327 E -> R (in Ref. 1; AAA52173). FT {ECO:0000305}. FT HELIX 23 35 {ECO:0000244|PDB:1KXP}. FT HELIX 37 51 {ECO:0000244|PDB:1KXP}. FT HELIX 57 74 {ECO:0000244|PDB:1KXP}. FT STRAND 76 79 {ECO:0000244|PDB:1KW2}. FT HELIX 83 94 {ECO:0000244|PDB:1KXP}. FT STRAND 97 99 {ECO:0000244|PDB:1J78}. FT HELIX 108 111 {ECO:0000244|PDB:1KW2}. FT HELIX 116 125 {ECO:0000244|PDB:1KW2}. FT HELIX 141 150 {ECO:0000244|PDB:1KXP}. FT HELIX 152 166 {ECO:0000244|PDB:1KXP}. FT HELIX 172 190 {ECO:0000244|PDB:1KXP}. FT STRAND 192 194 {ECO:0000244|PDB:1KXP}. FT HELIX 195 226 {ECO:0000244|PDB:1KXP}. FT HELIX 228 242 {ECO:0000244|PDB:1KXP}. FT HELIX 248 265 {ECO:0000244|PDB:1KXP}. FT HELIX 273 289 {ECO:0000244|PDB:1KXP}. FT TURN 290 292 {ECO:0000244|PDB:1KXP}. FT HELIX 294 299 {ECO:0000244|PDB:1KXP}. FT STRAND 302 304 {ECO:0000244|PDB:1KXP}. FT HELIX 305 314 {ECO:0000244|PDB:1KXP}. FT HELIX 331 335 {ECO:0000244|PDB:1KXP}. FT STRAND 336 338 {ECO:0000244|PDB:1LOT}. FT HELIX 340 351 {ECO:0000244|PDB:1KXP}. FT HELIX 358 373 {ECO:0000244|PDB:1KXP}. FT TURN 374 377 {ECO:0000244|PDB:1KXP}. FT HELIX 381 406 {ECO:0000244|PDB:1KXP}. FT TURN 407 412 {ECO:0000244|PDB:1KXP}. FT HELIX 415 429 {ECO:0000244|PDB:1KXP}. FT HELIX 435 452 {ECO:0000244|PDB:1KXP}. FT HELIX 459 470 {ECO:0000244|PDB:1KXP}. SQ SEQUENCE 474 AA; 52964 MW; 6AD8F163B551F1E4 CRC64; MKRVLVLLLA VAFGHALERG RDYEKNKVCK EFSHLGKEDF TSLSLVLYSR KFPSGTFEQV SQLVKEVVSL TEACCAEGAD PDCYDTRTSA LSAKSCESNS PFPVHPGTAE CCTKEGLERK LCMAALKHQP QEFPTYVEPT NDEICEAFRK DPKEYANQFM WEYSTNYGQA PLSLLVSYTK SYLSMVGSCC TSASPTVCFL KERLQLKHLS LLTTLSNRVC SQYAAYGEKK SRLSNLIKLA QKVPTADLED VLPLAEDITN ILSKCCESAS EDCMAKELPE HTVKLCDNLS TKNSKFEDCC QEKTAMDVFV CTYFMPAAQL PELPDVELPT NKDVCDPGNT KVMDKYTFEL SRRTHLPEVF LSKVLEPTLK SLGECCDVED STTCFNAKGP LLKKELSSFI DKGQELCADY SENTFTEYKK KLAERLKAKL PDATPKELAK LVNKRSDFAS NCCSINSPPL YCDSEIDAEL KNIL //