CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011064
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Regucalcin 
Protein Synonyms/Alias
 RC; Gluconolactonase; GNL; Senescence marker protein 30; SMP-30 
Gene Name
 Rgn 
Gene Synonyms/Alias
 Smp30 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
144LFPDHSVKKYFDQVDacetylation[1]
145FPDHSVKKYFDQVDIacetylation[1]
195SNRRTVYKMEKDEQIacetylation[1]
233RLDPETGKRLQTVKLacetylation[1]
239GKRLQTVKLPVDKTTacetylation[1]
283PDAGNIFKITGLGVKacetylation[1]
290KITGLGVKGIAPYSYacetylation[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
 Gluconolactonase with low activity towards other sugar lactones, including gulonolactone and galactonolactone. Catalyzes a key step in ascorbic acid (vitamin C) biosynthesis. Can also hydrolyze diisopropyl phosphorofluoridate and phenylacetate (in vitro). Calcium-binding protein. Modulates Ca(2+) signaling, and Ca(2+)-dependent cellular processes and enzyme activities. 
Sequence Annotation
 ACT_SITE 204 204 Proton donor/acceptor (By similarity).
 METAL 18 18 Divalent metal cation (By similarity).
 METAL 154 154 Divalent metal cation (By similarity).
 METAL 204 204 Divalent metal cation (By similarity).
 BINDING 101 101 Substrate (By similarity).
 BINDING 103 103 Substrate (By similarity).
 BINDING 121 121 Substrate (By similarity).
 MOD_RES 3 3 Phosphoserine (By similarity).  
Keyword
 Ascorbate biosynthesis; Calcium; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 299 AA 
Protein Sequence
MSSIKIECVL RENYRCGESP VWEEASKCLL FVDIPSKTVC RWDSISNRVQ RVGVDAPVSS 60
VALRQSGGYV ATIGTKFCAL NWEDQSVFIL AMVDEDKKNN RFNDGKVDPA GRYFAGTMAE 120
ETAPAVLERH QGSLYSLFPD HSVKKYFDQV DISNGLDWSL DHKIFYYIDS LSYTVDAFDY 180
DLPTGQISNR RTVYKMEKDE QIPDGMCIDV EGKLWVACYN GGRVIRLDPE TGKRLQTVKL 240
PVDKTTSCCF GGKDYSEMYV TCARDGMSAE GLLRQPDAGN IFKITGLGVK GIAPYSYAG 299 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0005509; F:calcium ion binding; IDA:UniProtKB.
 GO:0030234; F:enzyme regulator activity; IEA:InterPro.
 GO:0004341; F:gluconolactonase activity; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; ISS:UniProtKB.
 GO:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB.
 GO:0019853; P:L-ascorbic acid biosynthetic process; ISS:UniProtKB.
 GO:0032781; P:positive regulation of ATPase activity; IDA:UniProtKB.
 GO:0050848; P:regulation of calcium-mediated signaling; IDA:UniProtKB. 
Interpro
 IPR011042; 6-blade_b-propeller_TolB-like.
 IPR008367; Regucalcin.
 IPR013658; SGL.
 IPR005511; SMP-30. 
Pfam
 PF08450; SGL 
SMART
  
PROSITE
  
PRINTS
 PR01791; REGUCALCIN.
 PR01790; SMP30FAMILY.