ID VTDB_HUMAN Reviewed; 474 AA. AC P02774; B4DPP2; D6RAK8; Q16309; Q16310; Q53F31; Q6GTG1; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 12-SEP-2018, sequence version 2. DT 28-JUN-2023, entry version 233. DE RecName: Full=Vitamin D-binding protein; DE Short=DBP; DE Short=VDB; DE AltName: Full=Gc protein-derived macrophage activating factor {ECO:0000303|PubMed:16302727}; DE Short=Gc-MAF; DE Short=GcMAF {ECO:0000303|PubMed:16302727}; DE AltName: Full=Gc-globulin; DE AltName: Full=Group-specific component; DE Short=Gc {ECO:0000303|PubMed:16302727}; DE AltName: Full=Vitamin D-binding protein-macrophage activating factor; DE Short=DBP-maf; DE Flags: Precursor; GN Name=GC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS RP GLU-432 AND ARG-445. 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 alpha RT fetoprotein gene family."; RL J. Clin. Invest. 76:2420-2424(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS LYS-436 AND ARG-445. 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 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 ARG-445. 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 gene."; RL Biochim. Biophys. Acta 1216:385-394(1993). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-432 AND ARG-445. RX PubMed=8325650; DOI=10.1006/geno.1993.1258; RA Witke W.F., Gibbs P.E., Zielinski R., Yang F., Bowman B.H., 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 LYS-436 AND ARG-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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 GLU-432 RP AND ARG-445. 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]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., 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., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., 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., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS GLU-432 AND RP ARG-445. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., 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 ARG-445. 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 project: RT 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 sequences RT that respond to heavy metal, adipocyte and mitotic signals."; RL Gene 54:285-290(1987). RN [11] RP PROTEIN SEQUENCE OF 17-474, AND SUBCELLULAR LOCATION. 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 (group- RT specific component): evidence of a three-fold internal homology as in serum RT 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 binding RT protein (group-specific component)."; RL Biochemistry 18:1611-1617(1979). RN [13] RP PROTEIN SEQUENCE OF 409-446 (ALLELE GC*1S), VARIANTS GLU-432 AND ARG-445, RP TISSUE SPECIFICITY, AND GLYCOSYLATION (ALLELE GC*1S). RX PubMed=20079467; DOI=10.1016/j.bbapap.2009.12.022; RA Ravnsborg T., Olsen D.T., Thysen A.H., Christiansen M., Houen G., RA Hoejrup P.; RT "The glycosylation and characterization of the candidate Gc macrophage RT activating factor."; RL Biochim. Biophys. Acta 1804:909-917(2010). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 430-446, AND VARIANT 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 South RT African blacks, and 2A9 from south Germany."; RL Vox Sang. 68:50-54(1995). RN [15] RP REVIEW. RX PubMed=16302727; RA Nagasawa H., Uto Y., Sasaki H., Okamura N., Murakami A., Kubo S., RA Kirk K.L., Hori H.; RT "Gc protein (vitamin D-binding protein): Gc genotyping and GcMAF precursor RT activity."; RL Anticancer Res. 25:3689-3695(2005). RN [16] RP GLYCOSYLATION. RX PubMed=17360250; DOI=10.1016/j.bbapap.2007.01.005; RA Christiansen M., Joergensen C.S., Laursen I., Hirschberg D., Hoejrup P., RA Houen G.; RT "Protein chemical characterization of Gc globulin (vitamin D-binding RT protein) isoforms; Gc-1f, Gc-1s and Gc-2."; RL Biochim. Biophys. Acta 1774:481-492(2007). RN [17] 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., Buerckstuemmer T., RA 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 [18] RP VARIANTS GLU-432; LYS-436 AND ARG-445. 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 protein RT (group-specific component): allelic differences of the common genetic GC RT types."; RL Hum. Genet. 89:401-406(1992). RN [19] 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 vitamin D- RT binding protein."; RL Nat. Struct. Biol. 9:131-136(2002). RN [20] RP IDENTIFICATION BY MASS 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Involved in vitamin D transport and storage, scavenging of CC extracellular G-actin, enhancement of the chemotactic activity of C5 CC alpha for neutrophils in inflammation and macrophage activation. CC {ECO:0000305|PubMed:16302727}. CC -!- SUBUNIT: Associates with membrane-bound immunoglobulin on the surface CC of B-lymphocytes and with IgG Fc receptor on the membranes of T- CC lymphocytes. Interacts with LRP2; the interaction is required for renal CC uptake of GC in complex with 25-hydroxyvitamin D3 (By similarity). CC {ECO:0000250|UniProtKB:P21614}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2423133}. 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 Name=3; CC IsoId=P02774-3; Sequence=VSP_044523; CC -!- TISSUE SPECIFICITY: Expressed in the liver. Found in plasma, ascites, CC cerebrospinal fluid and urine. {ECO:0000269|PubMed:20079467, CC ECO:0000269|PubMed:2416779, ECO:0000305|PubMed:16302727}. CC -!- PTM: Allele GC*1S is O-glycosylated at Thr-436 (PubMed:20079467). The CC trisaccharide sugar moiety can be modified by the successive removal of CC neuraminic acid and galactose leaving an O-mceeN-acetyl-galactosamine. CC This conversion is thought to produce a macrophage-activating factor CC (Gc-MAF). Only a minor proportion of plasma GC is O-glycosylated CC (PubMed:17360250). The potential N-glycosylation site predicted at Asn- CC 288 is thought to be nonglycosylated. {ECO:0000269|PubMed:17360250, CC ECO:0000269|PubMed:20079467, ECO:0000305|PubMed:16302727}. CC -!- POLYMORPHISM: Over 80 variants of human DBP have been identified. The CC three most common alleles are called GC*1F, GC*1S, and GC*2. The CC sequence shown is that of the GC*1A1 allele. CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {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. [P02774-1] DR RefSeq; NP_001191235.1; NM_001204306.1. [P02774-1] DR RefSeq; NP_001191236.1; NM_001204307.1. [P02774-3] 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 AlphaFoldDB; P02774; -. DR SMR; P02774; -. DR BioGRID; 108908; 62. DR DIP; DIP-17038N; -. DR IntAct; P02774; 23. DR MINT; P02774; -. DR STRING; 9606.ENSP00000421725; -. DR ChEMBL; CHEMBL2259; -. DR DrugBank; DB01436; Alfacalcidol. DR DrugBank; DB00136; Calcitriol. DR DrugBank; DB00169; Cholecalciferol. DR DrugBank; DB00153; Ergocalciferol. DR DrugBank; DB04224; Oleic Acid. DR DrugBank; DB11094; Vitamin D. DR DrugCentral; P02774; -. DR CarbonylDB; P02774; -. DR GlyConnect; 619; 1 N-Linked glycan (1 site), 1 O-Linked glycan. DR GlyCosmos; P02774; 1 site, 4 glycans. DR GlyGen; P02774; 3 sites, 2 N-linked glycans (1 site), 2 O-linked glycans (1 site). DR iPTMnet; P02774; -. DR PhosphoSitePlus; 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 EPD; P02774; -. DR jPOST; P02774; -. DR MassIVE; P02774; -. DR PaxDb; P02774; -. DR PeptideAtlas; P02774; -. DR PRIDE; P02774; -. DR ProteomicsDB; 13358; -. DR ProteomicsDB; 51590; -. [P02774-1] DR ProteomicsDB; 51591; -. [P02774-2] DR Antibodypedia; 871; 836 antibodies from 40 providers. DR DNASU; 2638; -. DR Ensembl; ENST00000273951.13; ENSP00000273951.8; ENSG00000145321.13. [P02774-1] DR Ensembl; ENST00000504199.5; ENSP00000421725.1; ENSG00000145321.13. [P02774-3] DR GeneID; 2638; -. DR KEGG; hsa:2638; -. DR MANE-Select; ENST00000273951.13; ENSP00000273951.8; NM_000583.4; NP_000574.2. DR UCSC; uc003hge.4; human. [P02774-1] DR AGR; HGNC:4187; -. DR CTD; 2638; -. DR DisGeNET; 2638; -. DR GeneCards; GC; -. DR HGNC; HGNC:4187; GC. DR HPA; ENSG00000145321; Tissue enriched (liver). DR MIM; 139200; gene. DR neXtProt; NX_P02774; -. DR OpenTargets; ENSG00000145321; -. DR PharmGKB; PA28601; -. DR VEuPathDB; HostDB:ENSG00000145321; -. DR eggNOG; ENOG502QTPW; Eukaryota. DR GeneTree; ENSGT00390000000113; -. DR HOGENOM; CLU_045992_0_0_1; -. DR InParanoid; P02774; -. DR OrthoDB; 5311143at2759; -. DR PhylomeDB; P02774; -. DR TreeFam; TF335561; -. DR PathwayCommons; P02774; -. DR Reactome; R-HSA-196791; Vitamin D (calciferol) metabolism. DR SignaLink; P02774; -. DR SIGNOR; P02774; -. DR BioGRID-ORCS; 2638; 16 hits in 1147 CRISPR screens. DR ChiTaRS; GC; human. DR EvolutionaryTrace; P02774; -. DR GeneWiki; Vitamin_D-binding_protein; -. DR GenomeRNAi; 2638; -. DR Pharos; P02774; Tchem. DR PRO; PR:P02774; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P02774; protein. DR Bgee; ENSG00000145321; Expressed in liver and 112 other tissues. DR ExpressionAtlas; P02774; baseline and differential. DR Genevisible; P02774; HS. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; HDA: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; IBA:GO_Central. DR GO; GO:0090482; F:vitamin transmembrane transporter activity; IEA:InterPro. DR GO; GO:0042359; P:vitamin D metabolic process; IEA:Ensembl. DR GO; GO:0051180; P:vitamin transport; TAS:ProtInc. DR CDD; cd00015; ALBUMIN; 1. DR Gene3D; 1.10.246.10; -; 5. DR IDEAL; IID00264; -. 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 PANTHER; PTHR11385; SERUM ALBUMIN-RELATED; 1. DR PANTHER; PTHR11385:SF11; VITAMIN D-BINDING PROTEIN; 1. 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; Serum albumin-like; 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; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Reference proteome; Repeat; Secreted; Signal; Transport; Vitamin D. FT SIGNAL 1..16 FT /evidence="ECO:0000269|PubMed:218624, FT ECO:0000269|PubMed:2423133" FT CHAIN 17..474 FT /note="Vitamin D-binding protein" FT /id="PRO_0000001102" FT DOMAIN 17..208 FT /note="Albumin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769" FT DOMAIN 209..394 FT /note="Albumin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769" FT DOMAIN 395..474 FT /note="Albumin 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769" FT DISULFID 29..75 FT DISULFID 74..83 FT /evidence="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 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_038427" FT VAR_SEQ 1 FT /note="M -> MLWSWSEERGGAARLSGRKM (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044523" FT VARIANT 432 FT /note="D -> E (in allele GC*1S; dbSNP:rs7041)" FT /evidence="ECO:0000269|PubMed:1352271, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:20079467, FT ECO:0000269|PubMed:2416779, ECO:0000269|PubMed:7505619, FT ECO:0000269|PubMed:8325650, ECO:0000269|Ref.6, FT ECO:0000269|Ref.8" FT /id="VAR_000548" FT VARIANT 436 FT /note="T -> K (in allele GC*2, allele GC*2A9; FT dbSNP:rs4588)" FT /evidence="ECO:0000269|PubMed:1352271, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:2415977, FT ECO:0000269|PubMed:7725672" FT /id="VAR_000549" FT VARIANT 445 FT /note="H -> C (in allele GC*2A9; requires 2 nucleotide FT substitutions)" FT /evidence="ECO:0000269|PubMed:7725672" FT /id="VAR_014120" FT VARIANT 445 FT /note="H -> R (in allele GC*1F, allele GC*2 and allele FT GC*1S; dbSNP:rs9016)" FT /evidence="ECO:0000269|PubMed:1352271, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:20079467, ECO:0000269|PubMed:2415977, FT ECO:0000269|PubMed:2416779, ECO:0000269|PubMed:7505619, FT ECO:0000269|PubMed:7725672, ECO:0000269|PubMed:8325650, FT ECO:0000269|Ref.6, ECO:0000269|Ref.8" FT /id="VAR_014121" FT CONFLICT 168 FT /note="G -> E (in Ref. 1; AAA52173)" FT /evidence="ECO:0000305" FT CONFLICT 183 FT /note="L -> P (in Ref. 5; AK309595)" FT /evidence="ECO:0000305" FT CONFLICT 327 FT /note="E -> R (in Ref. 1; AAA52173)" FT /evidence="ECO:0000305" FT HELIX 23..35 FT /evidence="ECO:0007829|PDB:1KXP" FT HELIX 37..51 FT /evidence="ECO:0007829|PDB:1KXP" FT HELIX 57..74 FT /evidence="ECO:0007829|PDB:1KXP" FT STRAND 76..79 FT /evidence="ECO:0007829|PDB:1KW2" FT TURN 80..82 FT /evidence="ECO:0007829|PDB:1J78" FT HELIX 83..94 FT /evidence="ECO:0007829|PDB:1KXP" FT STRAND 97..99 FT /evidence="ECO:0007829|PDB:1J78" FT HELIX 108..111 FT /evidence="ECO:0007829|PDB:1KW2" FT HELIX 116..125 FT /evidence="ECO:0007829|PDB:1KW2" FT HELIX 141..150 FT /evidence="ECO:0007829|PDB:1KXP" FT HELIX 152..166 FT /evidence="ECO:0007829|PDB:1KXP" FT HELIX 172..190 FT /evidence="ECO:0007829|PDB:1KXP" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:1KXP" FT HELIX 195..226 FT /evidence="ECO:0007829|PDB:1KXP" FT HELIX 228..242 FT /evidence="ECO:0007829|PDB:1KXP" FT HELIX 248..265 FT /evidence="ECO:0007829|PDB:1KXP" FT HELIX 273..289 FT /evidence="ECO:0007829|PDB:1KXP" FT TURN 290..292 FT /evidence="ECO:0007829|PDB:1KXP" FT HELIX 294..299 FT /evidence="ECO:0007829|PDB:1KXP" FT STRAND 302..304 FT /evidence="ECO:0007829|PDB:1KXP" FT HELIX 305..314 FT /evidence="ECO:0007829|PDB:1KXP" FT HELIX 331..335 FT /evidence="ECO:0007829|PDB:1KXP" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:1LOT" FT HELIX 340..351 FT /evidence="ECO:0007829|PDB:1KXP" FT HELIX 358..373 FT /evidence="ECO:0007829|PDB:1KXP" FT TURN 374..377 FT /evidence="ECO:0007829|PDB:1KXP" FT HELIX 381..406 FT /evidence="ECO:0007829|PDB:1KXP" FT TURN 407..412 FT /evidence="ECO:0007829|PDB:1KXP" FT HELIX 415..429 FT /evidence="ECO:0007829|PDB:1KXP" FT HELIX 435..452 FT /evidence="ECO:0007829|PDB:1KXP" FT HELIX 459..470 FT /evidence="ECO:0007829|PDB:1KXP" SQ SEQUENCE 474 AA; 52918 MW; 484BF163B54A43E6 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 PDATPTELAK LVNKHSDFAS NCCSINSPPL YCDSEIDAEL KNIL //