ID VTDB_HUMAN STANDARD; PRT; 474 AA. AC P02774; Q16309; Q16310; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 15-SEP-2003 (Rel. 42, Last annotation update) DE Vitamin D-binding protein precursor (DBP) (Group-specific component) DE (GC-globulin) (VDB). GN GC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86068030; PubMed=2415977; 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 [2] RP SEQUENCE FROM N.A. RX MEDLINE=86086396; PubMed=2416779; 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 [3] RP SEQUENCE FROM N.A. RX MEDLINE=94092730; PubMed=7505619; 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 SEQUENCE OF 17-474. RX MEDLINE=86216223; PubMed=2423133; RA Schoentgen F., Metz-Boutigue M.-H., Jolles J., Constans J., RA Jolles P.; RT "Complete amino acid sequence of human vitamin D-binding protein RT (group-specific component): evidence of a three-fold internal RT homology as in serum albumin and alpha-fetoprotein."; RL Biochim. Biophys. Acta 871:189-198(1986). RN [5] RP SEQUENCE OF 17-31 AND 431-441. RX MEDLINE=79145448; PubMed=218624; 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 [6] RP SEQUENCE OF 1-19 FROM N.A. RX MEDLINE=88005794; PubMed=2958390; 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 [7] RP VARIANTS GC*2; GC*1F AND GC*1S. RX MEDLINE=92316509; PubMed=1352271; 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 [8] RP SEQUENCE OF 430-446 FROM N.A., AND VARIANTS GC*2A9 CYS-445 AND GC*1A1 RP HIS-445. RX MEDLINE=95242701; PubMed=7725672; 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). 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 -!- POLYMORPHISM: OVER 80 VARIANTS OF HUMAN DBP HAVE BEEN IDENTIFIED. CC THE THREE MOST COMMON ALLELES ARE CALLED GC1F, GC1S, AND GC2. THE CC SEQUENCE SHOWN IS THAT OF THE GC2 ALLELE. CC -!- SIMILARITY: BELONGS TO THE ALB/AFP/VDB FAMILY. CC -!- SIMILARITY: Contains 3 albumin domains. 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; L10641; AAA61704.1; -. DR EMBL; X03178; CAA26938.1; -. DR EMBL; M12654; AAA52173.1; -. DR EMBL; S67480; AAB29423.1; -. DR EMBL; S67474; AAB29423.1; JOINED. DR EMBL; S67476; AAB29423.1; JOINED. DR EMBL; S67478; AAB29423.1; JOINED. DR EMBL; S67479; AAB29423.1; JOINED. DR EMBL; S67526; AAB29423.1; JOINED. DR EMBL; M17156; AAA19662.2; -. DR EMBL; S77129; AAD14249.1; ALT_SEQ. DR EMBL; S77130; AAD14250.1; ALT_SEQ. DR PIR; A94076; VYHUD. DR PDB; 1J78; 06-FEB-02. DR PDB; 1J7E; 06-FEB-02. DR PDB; 1KW2; 19-JUN-02. DR PDB; 1KXP; 19-JUN-02. DR PDB; 1LOT; 31-JUL-02. DR PDB; 1MA9; 11-FEB-03. DR GlycoSuiteDB; P02774; -. DR SWISS-2DPAGE; P02774; HUMAN. DR Siena-2DPAGE; P02774; -. DR Genew; HGNC:4187; GC. DR MIM; 139200; -. DR GO; GO:0005386; F:carrier activity; TAS. DR GO; GO:0005209; F:plasma protein; TAS. DR GO; GO:0005499; F:vitamin D binding activity; TAS. DR GO; GO:0015875; P:vitamin/cofactor transport; TAS. DR InterPro; IPR000264; Serum_albumin. DR Pfam; PF00273; transport_prot; 2. DR PRINTS; PR00802; SERUMALBUMIN. DR ProDom; PD002486; Serum_albumin; 1. DR SMART; SM00103; ALBUMIN; 2. DR PROSITE; PS00212; ALBUMIN; 1. KW Glycoprotein; Vitamin D; Transport; Actin-binding; Repeat; KW Polymorphism; Signal; 3D-structure. FT SIGNAL 1 16 FT CHAIN 17 474 VITAMIN D-BINDING PROTEIN. FT DOMAIN 20 202 ALBUMIN 1. FT DOMAIN 208 388 ALBUMIN 2. FT DOMAIN 395 474 ALBUMIN 3. FT DISULFID 29 75 BY SIMILARITY. FT DISULFID 74 83 BY SIMILARITY. FT DISULFID 96 112 BY SIMILARITY. FT DISULFID 111 122 BY SIMILARITY. FT DISULFID 145 190 BY SIMILARITY. FT DISULFID 189 198 BY SIMILARITY. FT DISULFID 220 266 BY SIMILARITY. FT DISULFID 265 273 BY SIMILARITY. FT DISULFID 286 300 BY SIMILARITY. FT DISULFID 299 311 BY SIMILARITY. FT DISULFID 335 376 BY SIMILARITY. FT DISULFID 375 384 BY SIMILARITY. FT DISULFID 407 453 BY SIMILARITY. FT DISULFID 452 462 BY SIMILARITY. FT CARBOHYD 288 288 N-LINKED (GLCNAC...) (POTENTIAL). FT VARIANT 432 432 D -> E (IN ALLELE GC*1S; dbSNP:7041). FT /FTId=VAR_000548. FT VARIANT 436 436 K -> T (in allele GC*1F and allele GC*1S; FT dbSNP:1047220). FT /FTId=VAR_000549. FT VARIANT 445 445 R -> C (IN ALLELE GC*2A9). FT /FTId=VAR_014120. FT VARIANT 445 445 R -> H (IN ALLELE GC*1A1; dbSNP:222038). FT /FTId=VAR_014121. FT CONFLICT 168 168 G -> E (IN REF. 2). FT CONFLICT 327 327 E -> R (IN REF. 2). SQ SEQUENCE 474 AA; 52963 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 //