VTDB_RABIT
ID VTDB_RABIT Reviewed; 476 AA.
AC P53789;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 101.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Liver;
RX PubMed=7703896;
RA Osawa M., Tsuji T., Yukawa N., Saito T., Takeichi S.;
RT "Cloning and sequence analysis of cDNA encoding rabbit vitamin D-binding
RT protein (Gc globulin).";
RL Biochem. Mol. Biol. Int. 34:1003-1009(1994).
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; D29666; BAA06137.1; -; mRNA.
DR RefSeq; NP_001075673.1; NM_001082204.1.
DR AlphaFoldDB; P53789; -.
DR SMR; P53789; -.
DR STRING; 9986.ENSOCUP00000006902; -.
DR PRIDE; P53789; -.
DR GeneID; 100008994; -.
DR KEGG; ocu:100008994; -.
DR CTD; 2638; -.
DR eggNOG; ENOG502QTPW; Eukaryota.
DR InParanoid; P53789; -.
DR OrthoDB; 514529at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0005499; F:vitamin D binding; IEA:UniProtKB-KW.
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..476
FT /note="Vitamin D-binding protein"
FT /id="PRO_0000001104"
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 CARBOHYD 86
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"
SQ SEQUENCE 476 AA; 52912 MW; 276A530196B014A5 CRC64;
MKRVLLLLLA VVCGHALERG RDYEKDKVCK ELSTLGKDDF RTLSLVLYSR KFPSGTFDQV
MKLVKEVVSL TEDCCTEDAD PGCYDNRTSA LSATSCESDS PFPVHPGTAE CCTKEGLGRK
LCMAALKHPP QEFPTYVEPA NDEICEAFRQ DPMEFADKFL YEYSSNYGQA PLPILVSYTK
SYLSMVGTCC TSASPTVCFL KERLQIKHLS LLTTLSNRVC SQYAAYGKEK SRRSHLIKLA
QKAPTAALKE VLPLAEDITN ILSKCCESTS EDCMAKELPE HTVKICDTLS TKNPKFEECC
QEKTPMDIFV CTYFMPAAQP PEPANVELPT SKDVCDSKNI NVMDQYTFEL SRKTHIPEVF
LSKVLEPTLK SLSECCHSAD STACLNAKGP VLKKEVSSFI DKGQELCAGY SENTFTEYKK
KLSQQLRAKL PEATSAELAE LVEKHSDFAS KCCSINSPPN YCDSEIDAEI KNLPEP
