VTDB_BOVIN
ID VTDB_BOVIN Reviewed; 474 AA.
AC Q3MHN5;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 78.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P21614}.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
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DR EMBL; BC105171; AAI05172.1; -; mRNA.
DR RefSeq; NP_001030457.1; NM_001035380.2.
DR AlphaFoldDB; Q3MHN5; -.
DR SMR; Q3MHN5; -.
DR STRING; 9913.ENSBTAP00000033386; -.
DR PaxDb; Q3MHN5; -.
DR PeptideAtlas; Q3MHN5; -.
DR PRIDE; Q3MHN5; -.
DR GeneID; 530076; -.
DR KEGG; bta:530076; -.
DR CTD; 2638; -.
DR eggNOG; ENOG502QTPW; Eukaryota.
DR InParanoid; Q3MHN5; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005499; F:vitamin D binding; IBA:GO_Central.
DR GO; GO:0090482; F:vitamin transmembrane transporter activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Actin-binding; Disulfide bond; Glycoprotein; Reference proteome; Repeat;
KW Secreted; Signal; Transport; Vitamin D.
FT SIGNAL 1..16
FT /evidence="ECO:0000250|UniProtKB:P21614"
FT CHAIN 17..474
FT /note="Vitamin D-binding protein"
FT /id="PRO_0000045781"
FT DOMAIN 17..208
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 209..393
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 394..474
FT /note="Albumin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
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 285..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 298..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 334..375
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 374..383
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 406..452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DISULFID 451..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
SQ SEQUENCE 474 AA; 53342 MW; 22C6CC2B324E4CFB CRC64;
MKRILVFLLA VAFVHALERG RDYEKDKVCK DLASLGREDF TSLSMVLYSR KFPSGTFEQI
SHLVNEVVSL TVTCCAEGAD PDCYDNRTSA LSDKSCESNS PFPVHPGTPE CCTHEGLEKK
LCMAALKHQP QEFPTYVEPT NDEICEAFRK DPKDFADRFM YEYSINYGQA PLTLLVGYTK
SYLSMVGSCC TSPNPTVCFL KERLQLKHFS LLTIMTNRIC SQYAAYGKEK SRLSHLIKFA
QKVPTAHLED VLPLAEDITT ILSKCCDSVS EDCIKELPEY AVKLCDNLST KNSKFKDCCQ
EKTPMEIFVC AYFMPASPNP ELPDVKLPMN KDVCDEGNTK VLDQYIFELS RKTQIPEVFL
TKILESTLKS LDECCHSESS TACLNAKGPQ LTRELSSFIQ KGQELCADYS ENTFTEYKKK
LAERLRGKFP DATETDLQEL VAKRSDFASK CCSVNSPPLY CNSEIDAEIN TLQS
