ID VTDB$HUMAN STANDARD; PRT; 474 AA. AC P02774; DT 21-JUL-1986 (REL. 01, CREATED) DT 21-JUL-1986 (REL. 01, LAST SEQUENCE UPDATE) DT 01-NOV-1990 (REL. 16, LAST ANNOTATION UPDATE) DE VITAMIN D-BINDING PROTEIN PRECURSOR (DBP) (GROUP-SPECIFIC COMPONENT) DE (GC-GLOBULIN) (GENE NAME: GC). OS HUMAN (HOMO SAPIENS). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] (SEQUENCE FROM N.A.) RA YANG F., BRUNE J.L., NAYLOR S.L., CUPPLES R.L., NABERHAUS K.H., RA BOWMAN B.H.; RL PROC. NATL. ACAD. SCI. U.S.A. 82:7994-7998(1985). RN [2] (SEQUENCE FROM N.A.) RA COOKE N.E., DAVID E.V.; RL J. CLIN. INVEST. 76:2420-2424(1985). RN [3] (SEQUENCE OF 17-474) RA SCHOENTGEN F., METZ-BOUTIGUE M.-H., JOLLES J., CONSTANS J., RA JOLLES P.; RL BIOCHIM. BIOPHYS. ACTA 871:189-198(1986). RN [4] (SEQUENCE OF 17-31 AND 431-441) RA SVASTI J., KUROSKY A., BENNETT A., BOWMAN B.H.; RL BIOCHEMISTRY 18:1611-1617(1979). RN [5] (SEQUENCE OF 1-19 FROM N.A.) RA YANG F., NABERHAUS K.H., ADRIAN G.S., GARDELLA J.M., BRISSENDEN J.E., RA BOWMAN B.H.; RL GENE 54:285-290(1987). CC -!- FUNCTION: DBP IS A MULTIFUNCTIONAL PROTEIN FOUND IN PLASMA, CC ASCITIC FLUID, CEREBROSPINAL FLUID, AND URINE AND ON THE SURFACE CC OF MANY CELL TYPES. IN PLASMA, IT CARRIES THE VITAMIN D STEROLS CC AND PREVENTS POLYMERIZATION OF ACTIN BY BINDING ITS MONOMERS. DBP CC ASSOCIATES WITH MEMBRANE-BOUND IMMUNOGLOBULIN ON THE SURFACE OF CC B-LYMPHOCYTES AND WITH IGG FC RECEPTOR ON THE MEMBRANES OF CC T-LYMPHOCYTES. CC -!- SIMILARITY: THE PROTEIN CAN BE SUBDIVIDED INTO THREE HOMOLOGOUS CC DOMAINS. CC -!- SIMILARITY: ALBUMIN, ALPHA-FETOPROTEIN, AND VITAMIN D-BINDING CC PROTEIN CONSTITUTE A FAMILY OF RELATED SERUM PROTEINS. CC -!- OVER 80 VARIANTS OF HUMAN DBP HAVE BEEN IDENTIFIED. THE THREE CC MOST COMMON ALLELES ARE CALLED GC1F, GC1S, AND GC2. CC -!- THIS SEQUENCE HAS ALL THREE RESIDUES CHARACTERISTIC OF THE GC2 CC ALLELE. 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; X03178; HSGCR. DR EMBL; M12654; HSDBP. DR EMBL; M17156; HSDBPG. DR PIR; A03237; VYHUD. DR PIR; A24066; A24066. DR PIR; A29096; A29096. DR MIM; 139200; NINTH EDITION. DR PROSITE; PS00212; ALBUMIN. KW ALBUMIN; GLYCOPROTEIN; VITAMIN D; TRANSPORT; PLASMA; ACTIN-BINDING; KW DUPLICATION; POLYMORPHISM; SIGNAL. FT SIGNAL 1 16 FT CHAIN 17 474 VITAMIN D-BINDING PROTEIN. FT REPEAT 22 199 FT REPEAT 218 385 FT REPEAT 404 474 FT DISULFID 29 75 BY HOMOLOGY. FT DISULFID 74 83 BY HOMOLOGY. FT DISULFID 96 112 BY HOMOLOGY. FT DISULFID 111 122 BY HOMOLOGY. FT DISULFID 145 190 BY HOMOLOGY. FT DISULFID 189 198 BY HOMOLOGY. FT DISULFID 220 266 BY HOMOLOGY. FT DISULFID 265 273 BY HOMOLOGY. FT DISULFID 286 300 BY HOMOLOGY. FT DISULFID 299 311 BY HOMOLOGY. FT DISULFID 335 376 BY HOMOLOGY. FT DISULFID 375 384 BY HOMOLOGY. FT DISULFID 407 453 BY HOMOLOGY. FT DISULFID 452 462 BY HOMOLOGY. FT CARBOHYD 288 288 POTENTIAL. FT VARIANT 432 432 D -> E (IN GC1 ALLELE). FT VARIANT 434 434 T -> K (IN GC1 ALLELE). FT VARIANT 440 440 K -> T (IN GC1 ALLELE). FT CONFLICT 168 168 G -> E (IN REF. 2). FT CONFLICT 327 327 E -> R (IN REF. 2). FT CONFLICT 436 436 K -> T (IN REF. 2). SQ SEQUENCE 474 AA; 52963 MW; 1164403 CN; 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 //