Sirt4
entrez
75387
canonical
uniprot
Q8R216
canonical
ensembl
ENSMUSG00000029524
resolver
ensp
ENSMUSP00000107697
resolver
ensp
ENSMUSP00000107698
resolver
ensp
ENSMUSP00000170467
resolver
ensp
ENSMUSP00000170470
resolver
ensp
ENSMUSP00000359034
resolver
enst
ENSMUST00000112066
resolver
enst
ENSMUST00000112067
resolver
genesymbol
Sirt4
resolver
genesymbol_syn
Sir2l4
resolver
uniprot
D3Z1D9
resolver
uniprot_entry
SIR4_MOUSE
resolver
uniprot_sec
D3Z1D9
resolver
amino_acid_sequence
MSGLTFRPTKGRWITHLSRPRSCGPSGLFVPPSPPLDPEKIKELQRFISLSKKLLVMTGAGISTESGIPDYRSEKVGLYARTDRRPIQHIDFVRSAPVRQRYWARNFVGWPQFSSHQPNPAHWALSNWERLGKLHWLVTQNVDALHSKAGSQRLTELHGCMHRVLCLNCGEQTARRVLQERFQALNPSWSAEAQGVAPDGDVFLTEEQVRSFQVPCCDRCGGPLKPDVVFFGDTVNPDKVDFVHRRVKEADSLLVVGSSLQVYSGYRFILTAREQKLPIAILNIGPTRSDDLACLKLDSRCGELLPLIDPRRQHSDVQRLEMNFPLSSAAQDP
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
2.3.1.286
uniprot
proteins
ec_number
2.3.1.313
uniprot
proteins
ec_number
2.4.2.-
uniprot
proteins
function
FUNCTION: Acts as a NAD-dependent protein lipoamidase, biotinylase, deacetylase and ADP-ribosyl transferase (PubMed:19220062). Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications. Inhibits the pyruvate dehydrogenase complex (PDH) activity via the enzymatic hydrolysis of the lipoamide cofactor from the E2 component, DLAT, in a phosphorylation-independent manner (PubMed:25525879). Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity. Acts as a negative regulator of mitochondrial glutamine metabolism by mediating mono ADP-ribosylation of GLUD1: expressed in response to DNA damage and negatively regulates anaplerosis by inhibiting GLUD1, leading to block metabolism of glutamine into tricarboxylic acid cycle and promoting cell cycle arrest (PubMed:16959573). In response to mTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis and cell proliferation (PubMed:23663782). Acts as a tumor suppressor (PubMed:23562301, PubMed:23663782). Also acts as a NAD-dependent protein deacetylase: mediates deacetylation of 'Lys-471' of MLYCD, inhibiting its activity, thereby acting as a regulator of lipid homeostasis (PubMed:23746352). Does not seem to deacetylate PC (PubMed:23438705). Controls fatty acid oxidation by inhibiting PPARA transcriptional activation. Impairs SIRT1-PPARA interaction probably through the regulation of NAD(+) levels (PubMed:20685656, PubMed:24043310). Down-regulates insulin secretion (By similarity). {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000269|PubMed:19220062, ECO:0000269|PubMed:20685656, ECO:0000269|PubMed:23438705, ECO:0000269|PubMed:23562301, ECO:0000269|PubMed:23663782, ECO:0000269|PubMed:23746352, ECO:0000269|PubMed:24043310, ECO:0000269|PubMed:25525879}.
uniprot
proteins
mass_dalton
37525
uniprot
proteins
protein_family
Class II subfamily
uniprot
proteins
protein_family
Sirtuin family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16959573
uniprot
proteins
pubmed
19220062
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20685656
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23438705
uniprot
proteins
pubmed
23562301
uniprot
proteins
pubmed
23663782
uniprot
proteins
pubmed
23746352
uniprot
proteins
pubmed
24043310
uniprot
proteins
pubmed
25525879
uniprot
proteins
sequence_length
333
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03161, ECO:0000269|PubMed:16959573, ECO:0000269|PubMed:23746352}.
uniprot
proteins