| Tag | Content |
|---|
| CPLM ID | CPLM-004990 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Vitamin D-binding protein |
Protein Synonyms/Alias | DBP; VDB; Gc-globulin; Group-specific component |
Gene Name | Gc |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 363 | VPEVFLSKVLEPTLK | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Multifunctional protein found in plasma, ascitic fluid, cerebrospinal fluid, and urine and on the surface of many cell types. In plasma, it carries the vitamin D sterols and prevents polymerization of actin by binding its monomers. DBP associates with membrane-bound immunoglobulin on the surface of B-lymphocytes and with IgG Fc receptor on the membranes of T-lymphocytes. |
Sequence Annotation | DOMAIN 17 208 Albumin 1.
DOMAIN 209 394 Albumin 2.
DOMAIN 395 476 Albumin 3.
CARBOHYD 288 288 N-linked (GlcNAc...).
DISULFID 29 75 By similarity.
DISULFID 74 83 By similarity.
DISULFID 96 112 By similarity.
DISULFID 111 122 By similarity.
DISULFID 145 190 By similarity.
DISULFID 189 198 By similarity.
DISULFID 220 266 By similarity.
DISULFID 265 273 By similarity.
DISULFID 286 300 By similarity.
DISULFID 299 311 By similarity.
DISULFID 335 376 By similarity.
DISULFID 375 384 By similarity.
DISULFID 407 453 By similarity.
DISULFID 452 462 By similarity. |
Keyword | Actin-binding; Complete proteome; Direct protein sequencing; Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted; Signal; Transport; Vitamin D. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 476 AA |
Protein Sequence | MKRVLVLLLA LAFGHALERG RDYEKDKVCN ELAMLGKEDF RSLSLILYSR KFSSSTFEQV 60
NQLVKEVVSL TEECCAEGAD PTCYDTRTSE LSVKSCESDA PFPVHPGTPE CCTKEGLERK 120
LCMAALSHQP QEFPTYVEPT NDEICEAFRR DPKGFADQFL YEYSSNYGQA PLPLLVAYTK 180
NYLSMVGSCC TSANPTVCFV KERLQMKHLS LLTTMSNRVC SQYAAYGKEK SRLSHLIKLA 240
QKVPTANLEN VLPLAEDFTE ILSRCCESTS EDCMASELPE HTIKICQNLS KKNSKFEECC 300
QENTPMNIFM CTYFMPAAEP LQLPAIKLPT GKDLCGQSTT QAMDQYTFEL SRRTQVPEVF 360
LSKVLEPTLK TLRECCDTQD SVACFSTQSP LLKRQLTSFI EKGQEMCADY SENTFTEYKK 420
KLAERLRTKT PNTSPAELKD MVEKHSDFAS KCCSINSPPL YCSSQIDAEM IDTLQS 476 |
Gene Ontology | GO:0005615; C:extracellular space; IEA:InterPro. GO:0003779; F:actin binding; ISS:UniProtKB. GO:0005499; F:vitamin D binding; IEA:UniProtKB-KW. GO:0051183; F:vitamin transporter activity; IEA:InterPro. GO:0042359; P:vitamin D metabolic process; IDA:MGI. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |