VTDB_HUMAN
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 03-AUG-2022, entry version 228.
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};
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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; 58.
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 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; 797 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 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; 514529at2759; -.
DR PhylomeDB; P02774; -.
DR TreeFam; TF335561; -.
DR PathwayCommons; P02774; -.
DR Reactome; R-HSA-196791; Vitamin D (calciferol) metabolism.
DR SignaLink; P02774; -.
DR BioGRID-ORCS; 2638; 13 hits in 1069 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 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; PTHR11385; 1.
DR PANTHER; PTHR11385:SF11; PTHR11385:SF11; 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; 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;
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
