Tag | Content |
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CPLM ID | CPLM-015345 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Cytosolic non-specific dipeptidase |
Protein Synonyms/Alias | CNDP dipeptidase 2 |
Gene Name | Cndp2 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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68 | LVDIGKQKLPDGSEI | acetylation | [1] | 339 | IPRKVVGKFSIRLVP | acetylation | [1] | 363 | QVSSYLSKKFAELQS | acetylation | [1] | 364 | VSSYLSKKFAELQSP | acetylation | [1] | 375 | LQSPNKFKVYMGHGG | acetylation | [1] | 383 | VYMGHGGKPWVSDFN | 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 | Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly (By similarity). |
Sequence Annotation | REGION 166 167 Substrate binding (By similarity). ACT_SITE 101 101 By similarity. ACT_SITE 166 166 Proton acceptor (By similarity). METAL 99 99 Manganese 2 (By similarity). METAL 132 132 Manganese 1 (By similarity). METAL 132 132 Manganese 2 (By similarity). METAL 167 167 Manganese 1 (By similarity). METAL 195 195 Manganese 2 (By similarity). METAL 445 445 Manganese 1 (By similarity). BINDING 195 195 Substrate; via carbonyl oxygen (By BINDING 228 228 Substrate; shared with homodimeric BINDING 330 330 Substrate; shared with homodimeric BINDING 343 343 Substrate (By similarity). BINDING 417 417 Substrate; via amide nitrogen and BINDING 445 445 Substrate (By similarity). |
Keyword | Carboxypeptidase; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Manganese; Metal-binding; Metalloprotease; Protease; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 475 AA |
Protein Sequence | MSALKAVFQY IDENQDRFVK KLAEWVAIQS VSAWPEKRGE IRRMTEAAAA DVQRLGGSVE 60 LVDIGKQKLP DGSEIPLPPI LLGKLGSDPQ KKTVCIYGHL DVQPAALEDG WDSEPFTLVE 120 REGKLYGRGS TDDKGPVAGW MNALEAYQKT GQEIPVNLRF CLEGMEESGS EGLDELIFAQ 180 KDKFFKDVDY VCISDNYWLG KNKPCITYGL RGICYFFIEV ECSDKDLHSG VYGGSVHEAM 240 TDLISLMGCL IDKKGKILIP GINDAVAPVT DEEHELYDHI DFDMEEFAKD VGAGTLLHSC 300 KKDILMHRWR YPSLSLHGIE GAFSGSGAKT VIPRKVVGKF SIRLVPDMIP EVVSEQVSSY 360 LSKKFAELQS PNKFKVYMGH GGKPWVSDFN HPHYQAGRRA LKTVFGVEPD LTREGGSIPV 420 TLTFQEATGK NVMLLPVGSA DDGAHSQNEK LNRLNYIEGT KMLAAYLYEV SQLKN 475 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW. GO:0016805; F:dipeptidase activity; IEA:InterPro. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. GO:0034701; F:tripeptidase activity; IEA:InterPro. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. |
Interpro | |
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