Tag | Content |
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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 |
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144 | LFPDHSVKKYFDQVD | acetylation | [1] | 145 | FPDHSVKKYFDQVDI | acetylation | [1] | 195 | SNRRTVYKMEKDEQI | acetylation | [1] | 233 | RLDPETGKRLQTVKL | acetylation | [1] | 239 | GKRLQTVKLPVDKTT | acetylation | [1] | 283 | PDAGNIFKITGLGVK | acetylation | [1] | 290 | KITGLGVKGIAPYSY | acetylation | [1] |
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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. |
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