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NAD-dependent protein lipoamidase sirtuin-4, mitochondrial (EC 3.5.1.-) (NAD-dependent ADP-ribosyltransferase sirtuin-4) (EC 2.4.2.-) (NAD-dependent protein deacetylase sirtuin-4) (EC 3.5.1.-) (Regulatory protein SIR2 homolog 4) (SIR2-like protein 4)

 G3SBZ3_GORGO            Unreviewed;       314 AA.
G3SBZ3;
16-NOV-2011, integrated into UniProtKB/TrEMBL.
16-NOV-2011, sequence version 1.
28-MAR-2018, entry version 51.
RecName: Full=NAD-dependent protein lipoamidase sirtuin-4, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03161};
EC=3.5.1.- {ECO:0000256|HAMAP-Rule:MF_03161};
AltName: Full=NAD-dependent ADP-ribosyltransferase sirtuin-4 {ECO:0000256|HAMAP-Rule:MF_03161};
EC=2.4.2.- {ECO:0000256|HAMAP-Rule:MF_03161};
AltName: Full=NAD-dependent protein deacetylase sirtuin-4 {ECO:0000256|HAMAP-Rule:MF_03161};
EC=3.5.1.- {ECO:0000256|HAMAP-Rule:MF_03161};
AltName: Full=Regulatory protein SIR2 homolog 4 {ECO:0000256|HAMAP-Rule:MF_03161};
AltName: Full=SIR2-like protein 4 {ECO:0000256|HAMAP-Rule:MF_03161};
Name=SIRT4 {ECO:0000256|HAMAP-Rule:MF_03161,
ECO:0000313|Ensembl:ENSGGOP00000025620};
Gorilla gorilla gorilla (Western lowland gorilla).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Gorilla.
NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000025620, ECO:0000313|Proteomes:UP000001519};
[1] {ECO:0000313|Ensembl:ENSGGOP00000025620, ECO:0000313|Proteomes:UP000001519}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Scally A.;
"Insights into the evolution of the great apes provided by the gorilla
genome.";
Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|Ensembl:ENSGGOP00000025620}
IDENTIFICATION.
Ensembl;
Submitted (SEP-2011) to UniProtKB.
-!- FUNCTION: Acts as NAD-dependent protein lipoamidase, ADP-ribosyl
transferase and deacetylase. 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.
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. In response to mTORC1
signal, SIRT4 expression is repressed, promoting anaplerosis and
cell proliferation. Acts as a tumor suppressor. 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. Controls fatty acid oxidation by
inhibiting PPARA transcriptional activation. Impairs SIRT1:PPARA
interaction probably through the regulation of NAD(+) levels.
Down-regulates insulin secretion. {ECO:0000256|HAMAP-
Rule:MF_03161}.
-!- CATALYTIC ACTIVITY: NAD(+) + a protein = nicotinamide + an N-(ADP-
D-ribosyl)-protein. {ECO:0000256|HAMAP-Rule:MF_03161}.
-!- CATALYTIC ACTIVITY: NAD(+) + an acetylprotein = nicotinamide + O-
acetyl-ADP-ribose + a protein. {ECO:0000256|HAMAP-Rule:MF_03161}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|HAMAP-Rule:MF_03161};
Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_03161};
-!- SUBUNIT: Interacts with GLUD1, IDE and SLC25A5. Interacts with
DLAT and PDHX. {ECO:0000256|HAMAP-Rule:MF_03161}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000256|HAMAP-
Rule:MF_03161}.
-!- MISCELLANEOUS: According to some authors, ADP-ribosyltransferase
activity of sirtuins may be an inefficient side reaction of the
deacetylase activity and may not be physiologically relevant.
{ECO:0000256|HAMAP-Rule:MF_03161}.
-!- SIMILARITY: Belongs to the sirtuin family. Class II subfamily.
{ECO:0000256|HAMAP-Rule:MF_03161}.
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EMBL; CABD030087057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CABD030087058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CABD030087059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CABD030087060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; XP_004054043.1; XM_004053995.2.
STRING; 9593.ENSGGOP00000025620; -.
Ensembl; ENSGGOT00000032929; ENSGGOP00000025620; ENSGGOG00000024753.
GeneID; 101130710; -.
KEGG; ggo:101130710; -.
CTD; 23409; -.
GeneTree; ENSGT00870000136443; -.
InParanoid; G3SBZ3; -.
KO; K11414; -.
OMA; ARQRYWA; -.
OrthoDB; EOG091G0DTB; -.
TreeFam; TF106182; -.
Proteomes; UP000001519; Chromosome 12.
Bgee; ENSGGOG00000024753; -.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0047708; F:biotinidase activity; IEA:Ensembl.
GO; GO:0061690; F:lipoamidase activity; IEA:Ensembl.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-UniRule.
GO; GO:0034979; F:NAD-dependent protein deacetylase activity; IEA:UniProtKB-UniRule.
GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
GO; GO:0006541; P:glutamine metabolic process; IEA:Ensembl.
GO; GO:0046322; P:negative regulation of fatty acid oxidation; IEA:Ensembl.
GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
GO; GO:0034983; P:peptidyl-lysine deacetylation; IEA:Ensembl.
GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IEA:Ensembl.
GO; GO:0006471; P:protein ADP-ribosylation; IEA:UniProtKB-UniRule.
GO; GO:0000820; P:regulation of glutamine family amino acid metabolic process; IEA:Ensembl.
GO; GO:1904182; P:regulation of pyruvate dehydrogenase activity; IEA:Ensembl.
GO; GO:0072350; P:tricarboxylic acid metabolic process; IEA:Ensembl.
Gene3D; 3.30.1600.10; -; 2.
HAMAP; MF_01967; Sirtuin_ClassII; 1.
InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
InterPro; IPR003000; Sirtuin.
InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
InterPro; IPR026587; Sirtuin_class_II.
InterPro; IPR026590; Ssirtuin_cat_dom.
Pfam; PF02146; SIR2; 1.
SUPFAM; SSF52467; SSF52467; 1.
PROSITE; PS50305; SIRTUIN; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000001519};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_03161};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03161};
Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03161};
NAD {ECO:0000256|HAMAP-Rule:MF_03161};
Reference proteome {ECO:0000313|Proteomes:UP000001519};
Transferase {ECO:0000256|HAMAP-Rule:MF_03161};
Transit peptide {ECO:0000256|HAMAP-Rule:MF_03161};
Zinc {ECO:0000256|HAMAP-Rule:MF_03161}.
DOMAIN 45 314 Deacetylase sirtuin-type.
{ECO:0000259|PROSITE:PS50305}.
NP_BIND 62 82 NAD. {ECO:0000256|HAMAP-Rule:MF_03161}.
NP_BIND 143 146 NAD. {ECO:0000256|HAMAP-Rule:MF_03161}.
NP_BIND 260 262 NAD. {ECO:0000256|HAMAP-Rule:MF_03161}.
NP_BIND 286 288 NAD. {ECO:0000256|HAMAP-Rule:MF_03161}.
ACT_SITE 161 161 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_03161}.
METAL 169 169 Zinc. {ECO:0000256|HAMAP-Rule:MF_03161}.
METAL 172 172 Zinc. {ECO:0000256|HAMAP-Rule:MF_03161}.
METAL 220 220 Zinc. {ECO:0000256|HAMAP-Rule:MF_03161}.
METAL 223 223 Zinc. {ECO:0000256|HAMAP-Rule:MF_03161}.
BINDING 304 304 NAD; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_03161}.
SEQUENCE 314 AA; 35207 MW; D590A16349F8505B CRC64;
MKMSFVLTFR SAKGRWIANP SQPCSKASIG LFVPASPPLD PEKVKELQRF ITLSKRLLVM
TGAGISTESG IPDYRSEKVG LYARTDRRPI QHGDFVRSAP IRQRYWARNF VGWPQFSSHQ
PNPAHWALST WEKLGKLYWL VTQNVDALHT KAGSRRLTEL HGCMDRVLCL DCGEQTPRGV
LQERFQVLNP TWSAEAHGLA PDGDVFLSEE QVQSFQVPTC VQCGGRLKPD VVFFGDTVNP
DKVDFVHKRV KEADSLLVVG SSLQVYSGYR FILTAWEKKL PIAILNIGPT RSDDLACLKL
NSRCGELLPL IDPC


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