CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002116
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
 Dbp 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
238SRMSHLIKLAQKVPTacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
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...) (Potential).
 CARBOHYD 432 432 N-linked (GlcNAc...) (Potential).
 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 RDYEKDKVCQ ELSTLGKDDF RSLSLILYSR KFPSSTFEQV 60
SQLVKEVVSL TEECCAEGAD PNCYDTRTSE LSIKSCESDA PFPVHPGTSE CCTKEGLERK 120
LCMAALSHQP QEFPAYVEPT NDEICEAFRK DPKGFADQFL FEYSSNYGQA PLPLLVGYTK 180
SYLSMVGSCC TSAKPTVCFL KERLQMKQLL LLTTMSNRVC SQYAAYGKEK SRMSHLIKLA 240
QKVPTANLED VLPLAEDLTE ILSRCCKSTS EDCMARELPE HTLKICGNLS KKNSKFEECC 300
YETTPMGIFM CSYFMPTAEP LQLPAIKLPT SKDLCGQSAT QAMDQYTFEL SRRTQVPEVF 360
LSKVLDTTLK TLRECCDTQD SVSCFSTQSP LMKRQLTSFI EKGQEMCADY SENTFTEYKK 420
KLAERLRTKM PNASPEELAD MVAKHSDFAS KCCSINSPPR YCSSQIDAEM RDILQS 476 
Gene Ontology
 GO:0030424; C:axon; IDA:RGD.
 GO:0005829; C:cytosol; IDA:RGD.
 GO:0005615; C:extracellular space; IDA:RGD.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
 GO:0003779; F:actin binding; ISS:UniProtKB.
 GO:0005499; F:vitamin D binding; IDA:RGD.
 GO:0051183; F:vitamin transporter activity; IEA:InterPro.
 GO:0007565; P:female pregnancy; IEP:RGD.
 GO:0007595; P:lactation; IEP:RGD.
 GO:0032355; P:response to estradiol stimulus; IEP:RGD.
 GO:0031667; P:response to nutrient levels; IEP:RGD. 
Interpro
 IPR000264; ALB/AFP/VDB.
 IPR020858; Serum_albumin-like.
 IPR020857; Serum_albumin_CS.
 IPR014760; Serum_albumin_N.
 IPR000213; VitD-bd.
 IPR015247; VitD-bind_III. 
Pfam
 PF00273; Serum_albumin
 PF09164; VitD-bind_III 
SMART
 SM00103; ALBUMIN 
PROSITE
 PS00212; ALBUMIN_1
 PS51438; ALBUMIN_2 
PRINTS
 PR00802; SERUMALBUMIN.
 PR00804; VITAMNDBNDNG.