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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)

 M3X2J8_FELCA            Unreviewed;       313 AA.
M3X2J8;
01-MAY-2013, integrated into UniProtKB/TrEMBL.
10-OCT-2018, sequence version 2.
13-FEB-2019, entry version 48.
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:ENSFCAP00000020847};
Felis catus (Cat) (Felis silvestris catus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
Felinae; Felis.
NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000020847, ECO:0000313|Proteomes:UP000011712};
[1] {ECO:0000313|Ensembl:ENSFCAP00000020847, ECO:0000313|Proteomes:UP000011712}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000020847,
ECO:0000313|Proteomes:UP000011712};
PubMed=17975172; DOI=10.1101/gr.6380007;
Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N.,
Schaffer A.A., Agarwala R., Narfstrom K., Murphy W.J., Giger U.,
Roca A.L., Antunes A., Menotti-Raymond M., Yuhki N.,
Pecon-Slattery J., Johnson W.E., Bourque G., Tesler G., O'Brien S.J.;
"Initial sequence and comparative analysis of the cat genome.";
Genome Res. 17:1675-1689(2007).
[2] {ECO:0000313|Ensembl:ENSFCAP00000020847}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000020847};
Hillier L.W., Warren W., Obrien S., Wilson R.K.;
"Sequence assembly of the Felis catus genome version 6.2.";
Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|Ensembl:ENSFCAP00000020847}
IDENTIFICATION.
STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000020847};
Ensembl;
Submitted (MAR-2013) 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:
Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-
acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731,
ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767;
Evidence={ECO:0000256|HAMAP-Rule:MF_03161};
-!- CATALYTIC ACTIVITY:
Reaction=L-cysteinyl-[protein] + NAD(+) = H(+) + nicotinamide + S-
(ADP-D-ribosyl)-L-cysteinyl-[protein]; Xref=Rhea:RHEA:56612,
Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14624, ChEBI:CHEBI:15378,
ChEBI:CHEBI:17154, ChEBI:CHEBI:29950, ChEBI:CHEBI:57540,
ChEBI:CHEBI:140607; Evidence={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; AANG04002472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
STRING; 9685.ENSFCAP00000020847; -.
Ensembl; ENSFCAT00000027416; ENSFCAP00000020847; ENSFCAG00000025934.
eggNOG; KOG2683; Eukaryota.
eggNOG; COG0846; LUCA.
GeneTree; ENSGT00940000158891; -.
InParanoid; M3X2J8; -.
OMA; RRHYWAR; -.
OrthoDB; 1407693at2759; -.
Proteomes; UP000011712; Chromosome D3.
Bgee; ENSFCAG00000025934; Expressed in 3 organ(s), highest expression level in liver.
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; -; 1.
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:UP000011712};
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:UP000011712};
Transferase {ECO:0000256|HAMAP-Rule:MF_03161};
Transit peptide {ECO:0000256|HAMAP-Rule:MF_03161};
Zinc {ECO:0000256|HAMAP-Rule:MF_03161}.
DOMAIN 45 313 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 259 261 NAD. {ECO:0000256|HAMAP-Rule:MF_03161}.
NP_BIND 285 287 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 222 222 Zinc. {ECO:0000256|HAMAP-Rule:MF_03161}.
BINDING 303 303 NAD; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_03161}.
SEQUENCE 313 AA; 35388 MW; FEDA6B2B6265E8A5 CRC64;
TKMNCRWTLR AAKGRWMVNI SQQCSHGSIG LFVPPSPPLD PEKIRELQRF ITLSKRLLVM
TGAGISTESG IPDYRSEKVG LYARTDRKPI QHGDFLRSAP VRQRYWARNF VGWPRFSSLQ
PNPAHWALSN WERLGKLYWL VTQNVDALHT KAGSQRLTEL HGCMHRVLCL NCGEQIPREV
LQERFEALNP TWSAEAHGLA PDGDVFLTEE QVRSFRVPSC RCGGPLKPDV VFFGDTVNPD
KVDFVHRRVK EADSLLVVGS SLQVYSGYRF ILTAREKKLP IAILNIGPTR SDDLACLKLD
SRCGELLPLI DPC


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