VTDB_RAT
ID VTDB_RAT Reviewed; 476 AA.
AC P04276;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 3.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=Vitamin D-binding protein;
DE Short=DBP;
DE Short=VDB;
DE AltName: Full=Gc-globulin;
DE AltName: Full=Group-specific component;
DE Flags: Precursor;
GN Name=Gc; Synonyms=Dbp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2419332; DOI=10.1016/s0021-9258(17)35803-9;
RA Cooke N.E.;
RT "Rat vitamin D binding protein. Determination of the full-length primary
RT structure from cloned cDNA.";
RL J. Biol. Chem. 261:3441-3450(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2480956; DOI=10.1016/s0021-9258(20)88249-0;
RA McLeod J.F., Cooke N.E.;
RT "The vitamin D-binding protein, alpha-fetoprotein, albumin multigene
RT family: detection of transcripts in multiple tissues.";
RL J. Biol. Chem. 264:21760-21769(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2007578; DOI=10.1016/s0021-9258(18)38107-9;
RA Ray K., Wang X., Zhao M., Cooke N.E.;
RT "The rat vitamin D binding protein (Gc-globulin) gene. Structural analysis,
RT functional and evolutionary correlations.";
RL J. Biol. Chem. 266:6221-6229(1991).
RN [4]
RP PROTEIN SEQUENCE OF 17-40, AND SUBCELLULAR LOCATION.
RX PubMed=3713442; DOI=10.1016/0024-3205(86)90569-2;
RA Litwiller R.D., Fass D.N., Kumar R.;
RT "The amino acid sequence of the NH2-terminal portion of rat and human
RT vitamin D binding protein: evidence for a high degree of homology between
RT rat and human vitamin D binding protein.";
RL Life Sci. 38:2179-2184(1986).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:0000250|UniProtKB:P02774}.
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.
CC {ECO:0000250|UniProtKB:P02774, ECO:0000250|UniProtKB:P21614}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3713442}.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
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DR EMBL; M12450; AAA41080.1; -; mRNA.
DR EMBL; J05148; AAA41082.1; -; mRNA.
DR EMBL; M60205; AAA41081.1; -; Genomic_DNA.
DR EMBL; M60197; AAA41081.1; JOINED; Genomic_DNA.
DR EMBL; M60198; AAA41081.1; JOINED; Genomic_DNA.
DR EMBL; M60199; AAA41081.1; JOINED; Genomic_DNA.
DR EMBL; M60200; AAA41081.1; JOINED; Genomic_DNA.
DR EMBL; M60201; AAA41081.1; JOINED; Genomic_DNA.
DR EMBL; M60202; AAA41081.1; JOINED; Genomic_DNA.
DR EMBL; M60203; AAA41081.1; JOINED; Genomic_DNA.
DR EMBL; M60204; AAA41081.1; JOINED; Genomic_DNA.
DR PIR; A38726; VYRTD.
DR AlphaFoldDB; P04276; -.
DR SMR; P04276; -.
DR STRING; 10116.ENSRNOP00000004174; -.
DR BindingDB; P04276; -.
DR ChEMBL; CHEMBL2163; -.
DR GlyGen; P04276; 1 site.
DR iPTMnet; P04276; -.
DR PaxDb; P04276; -.
DR PRIDE; P04276; -.
DR UCSC; RGD:2667; rat.
DR RGD; 2667; Gc.
DR eggNOG; ENOG502QTPW; Eukaryota.
DR InParanoid; P04276; -.
DR PhylomeDB; P04276; -.
DR Reactome; R-RNO-196791; Vitamin D (calciferol) metabolism.
DR PRO; PR:P04276; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:1902118; F:calcidiol binding; ISO:RGD.
DR GO; GO:0005499; F:vitamin D binding; IDA:RGD.
DR GO; GO:0090482; F:vitamin transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0007595; P:lactation; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR GO; GO:0042359; P:vitamin D metabolic process; ISO:RGD.
DR CDD; cd00015; ALBUMIN; 1.
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 Actin-binding; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal; Transport;
KW Vitamin D.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:3713442"
FT CHAIN 17..476
FT /note="Vitamin D-binding protein"
FT /evidence="ECO:0000269|PubMed:2419332"
FT /id="PRO_0000001105"
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..476
FT /note="Albumin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 74..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 96..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 111..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 145..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 189..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 220..266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 265..273
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 286..300
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 299..311
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 335..376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 375..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 407..453
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 452..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT CONFLICT 132
FT /note="E -> Q (in Ref. 2; AAA41082)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="L -> P (in Ref. 1; AAA41080)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="L -> S (in Ref. 2; AAA41082)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 53544 MW; D3C7729BC44E221E CRC64;
MKRVLVLLLA LAFGHALERG RDYEKDKVCQ ELSTLGKDDF RSLSLILYSR KFPSSTFEQV
SQLVKEVVSL TEECCAEGAD PNCYDTRTSE LSIKSCESDA PFPVHPGTSE CCTKEGLERK
LCMAALSHQP QEFPAYVEPT NDEICEAFRK DPKGFADQFL FEYSSNYGQA PLPLLVGYTK
SYLSMVGSCC TSAKPTVCFL KERLQMKQLL LLTTMSNRVC SQYAAYGKEK SRMSHLIKLA
QKVPTANLED VLPLAEDLTE ILSRCCKSTS EDCMARELPE HTLKICGNLS KKNSKFEECC
YETTPMGIFM CSYFMPTAEP LQLPAIKLPT SKDLCGQSAT QAMDQYTFEL SRRTQVPEVF
LSKVLDTTLK TLRECCDTQD SVSCFSTQSP LMKRQLTSFI EKGQEMCADY SENTFTEYKK
KLAERLRTKM PNASPEELAD MVAKHSDFAS KCCSINSPPR YCSSQIDAEM RDILQS
