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-MAR-2004 (Rel. 43, 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 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 -!- 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:0005499; F:vitamin D binding; 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). FT HELIX 23 35 FT HELIX 37 51 FT TURN 53 54 FT HELIX 57 75 FT TURN 81 82 FT HELIX 83 94 FT TURN 95 96 FT TURN 98 99 FT TURN 106 107 FT HELIX 108 111 FT TURN 112 113 FT HELIX 116 125 FT HELIX 141 150 FT HELIX 152 166 FT TURN 168 169 FT HELIX 172 189 FT TURN 190 191 FT HELIX 195 242 FT TURN 244 245 FT HELIX 248 265 FT TURN 266 267 FT TURN 271 272 FT HELIX 273 289 FT TURN 290 292 FT HELIX 294 299 FT TURN 300 301 FT HELIX 305 314 FT HELIX 332 334 FT TURN 337 338 FT HELIX 341 353 FT HELIX 358 371 FT TURN 372 372 FT HELIX 373 375 FT TURN 376 376 FT HELIX 381 406 FT TURN 407 412 FT HELIX 415 429 FT TURN 431 432 FT HELIX 435 452 FT TURN 455 456 FT HELIX 459 470 FT TURN 471 471 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 //