Tag | Content |
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CPLM ID | CPLM-014777 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | NAD-dependent protein deacylase sirtuin-5, mitochondrial |
Protein Synonyms/Alias | Regulatory protein SIR2 homolog 5; SIR2-like protein 5 |
Gene Name | Sirt5 |
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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203 | ESRIPVHKLPRCEEA | 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 | NAD-dependent lysine demalonylase and desuccinylase that specifically removes malonyl and succinyl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Has weak NAD- dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro (By similarity). |
Sequence Annotation | DOMAIN 41 310 Deacetylase sirtuin-type. NP_BIND 58 77 NAD (By similarity). NP_BIND 140 143 NAD (By similarity). NP_BIND 249 251 NAD (By similarity). NP_BIND 275 277 NAD (By similarity). ACT_SITE 158 158 Proton acceptor (By similarity). METAL 166 166 Zinc (By similarity). METAL 169 169 Zinc (By similarity). METAL 207 207 Zinc (By similarity). METAL 212 212 Zinc (By similarity). BINDING 102 102 Substrate (By similarity). BINDING 105 105 Substrate (By similarity). BINDING 293 293 NAD; via amide nitrogen (By similarity). |
Keyword | Complete proteome; Hydrolase; Metal-binding; Mitochondrion; NAD; Reference proteome; Transit peptide; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 310 AA |
Protein Sequence | MRPLPVAPGR LFSQLCCGPK PSASPQSKIC LTMARPSSNM ADFRKCFANA KHIVIISGAG 60 VSAESGVPTF RGTGGYWRKW QAQHLATPLA FAHNPSQVWE FYHYRREVMR NKEPNPGHLA 120 IAQCEARLRD QGRRVVVITQ NIDELHRKAG TKNLLEIHGT LFKTRCTSCG NVAENYKSPI 180 CPALLGKGAP EPDTQESRIP VHKLPRCEEA GCGGLLRPHV VWFGENLDPA ILKEVDRELA 240 RCDLCLVVGT SSVVYPAAMF APQVASRGVP VAEFNMETTP ATNRFRFHFP GPCGVTLPEA 300 LAPHETERIS 310 |
Gene Ontology | GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB. GO:0005759; C:mitochondrial matrix; ISS:UniProtKB. GO:0070403; F:NAD+ binding; ISS:UniProtKB. GO:0036054; F:protein-malonyllysine demalonylase activity; ISS:UniProtKB. GO:0036055; F:protein-succinyllysine desuccinylase activity; ISS:UniProtKB. GO:0008270; F:zinc ion binding; ISS:UniProtKB. GO:0006476; P:protein deacetylation; ISS:UniProtKB. |
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