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NAD-dependent protein deacetylase sirtuin-3, mitochondrial (hSIRT3) (EC 3.5.1.-) (Regulatory protein SIR2 homolog 3) (SIR2-like protein 3)

 SIR3_HUMAN              Reviewed;         399 AA.
Q9NTG7; B7Z5U6; Q9Y6E8;
31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
31-OCT-2003, sequence version 2.
22-NOV-2017, entry version 151.
RecName: Full=NAD-dependent protein deacetylase sirtuin-3, mitochondrial;
Short=hSIRT3;
EC=3.5.1.-;
AltName: Full=Regulatory protein SIR2 homolog 3;
AltName: Full=SIR2-like protein 3;
Flags: Precursor;
Name=SIRT3; Synonyms=SIR2L3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Testis;
PubMed=10381378; DOI=10.1006/bbrc.1999.0897;
Frye R.A.;
"Characterization of five human cDNAs with homology to the yeast SIR2
gene: Sir2-like proteins (sirtuins) metabolize NAD and may have
protein ADP-ribosyltransferase activity.";
Biochem. Biophys. Res. Commun. 260:273-279(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 282-399 (ISOFORM 1).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
ENZYME ACTIVITY, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING BY MPP,
AND MUTAGENESIS OF ARG-7; ARG-13; ARG-17; ARG-21; 99-ARG-ARG-100;
ASN-229 AND HIS-248.
PubMed=12186850; DOI=10.1083/jcb.200205057;
Schwer B., North B.J., Frye R.A., Ott M., Verdin E.;
"The human silent information regulator (Sir)2 homologue hSIRT3 is a
mitochondrial nicotinamide adenine dinucleotide-dependent
deacetylase.";
J. Cell Biol. 158:647-657(2002).
[7]
ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12374852; DOI=10.1073/pnas.222538099;
Onyango P., Celic I., McCaffery J.M., Boeke J.D., Feinberg A.P.;
"SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase
localized to mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 99:13653-13658(2002).
[8]
SUBCELLULAR LOCATION.
PubMed=16079181; DOI=10.1091/mbc.E05-01-0033;
Michishita E., Park J.Y., Burneskis J.M., Barrett J.C., Horikawa I.;
"Evolutionarily conserved and nonconserved cellular localizations and
functions of human SIRT proteins.";
Mol. Biol. Cell 16:4623-4635(2005).
[9]
FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-248, AND INTERACTION
WITH ACSS1.
PubMed=16788062; DOI=10.1073/pnas.0603968103;
Schwer B., Bunkenborg J., Verdin R.O., Andersen J.S., Verdin E.;
"Reversible lysine acetylation controls the activity of the
mitochondrial enzyme acetyl-CoA synthetase 2.";
Proc. Natl. Acad. Sci. U.S.A. 103:10224-10229(2006).
[10]
SUBCELLULAR LOCATION.
PubMed=18215119; DOI=10.1042/BJ20071624;
Cooper H.M., Spelbrink J.N.;
"The human SIRT3 protein deacetylase is exclusively mitochondrial.";
Biochem. J. 411:279-285(2008).
[11]
FUNCTION.
PubMed=18680753; DOI=10.1016/j.jmb.2008.07.048;
Schlicker C., Gertz M., Papatheodorou P., Kachholz B., Becker C.F.W.,
Steegborn C.;
"Substrates and regulation mechanisms for the human mitochondrial
sirtuins Sirt3 and Sirt5.";
J. Mol. Biol. 382:790-801(2008).
[12]
MUTAGENESIS OF HIS-248, FUNCTION, AND INTERACTION WITH NDUFA9.
PubMed=18794531; DOI=10.1073/pnas.0803790105;
Ahn B.-H., Kim H.-S., Song S., Lee I.H., Liu J., Vassilopoulos A.,
Deng C.-X., Finkel T.;
"A role for the mitochondrial deacetylase Sirt3 in regulating energy
homeostasis.";
Proc. Natl. Acad. Sci. U.S.A. 105:14447-14452(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
INTERACTION WITH PCCA.
PubMed=23438705; DOI=10.1016/j.mito.2013.02.002;
Wirth M., Karaca S., Wenzel D., Ho L., Tishkoff D., Lombard D.B.,
Verdin E., Urlaub H., Jedrusik-Bode M., Fischle W.;
"Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and
mammals interact with pyruvate carboxylase and other acetylated
biotin-dependent carboxylases.";
Mitochondrion 13:705-720(2013).
[15]
FUNCTION.
PubMed=24252090; DOI=10.1089/ars.2013.5420;
Vassilopoulos A., Pennington D.J., Andresson T., Rees D., Fearnley I.,
Ham A., Yan Y., Flynn C.R., Jones K., Kim H.S., Deng C., Walker J.,
Gius D.;
"SIRT3 deacetylates ATP synthase F1 complex proteins in response to
nutrient and exercise-induced stress.";
Antioxid. Redox Signal. 21:551-564(2014).
[16]
FUNCTION.
PubMed=24121500; DOI=10.1074/jbc.M113.510354;
Bharathi S.S., Zhang Y., Mohsen A.W., Uppala R., Balasubramani M.,
Schreiber E., Uechi G., Beck M.E., Rardin M.J., Vockley J., Verdin E.,
Gibson B.W., Hirschey M.D., Goetzman E.S.;
"SIRT3 regulates long-chain acyl-coA dehydrogenase by deacetylating
conserved lysines near the active site.";
J. Biol. Chem. 288:33837-33847(2013).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[19]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 118-399 IN COMPLEX WITH ZINC
IONS AND ACSS1, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
NAD-BINDING.
PubMed=19535340; DOI=10.1074/jbc.M109.014928;
Jin L., Wei W., Jiang Y., Peng H., Cai J., Mao C., Dai H., Choy W.,
Bemis J.E., Jirousek M.R., Milne J.C., Westphal C.H., Perni R.B.;
"Crystal structures of human SIRT3 displaying substrate-induced
conformational changes.";
J. Biol. Chem. 284:24394-24405(2009).
[20]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 116-399 IN COMPLEX WITH
INHIBITOR, NAD-BINDING SITES, AND ZINC-BINDING SITES.
PubMed=23897466; DOI=10.1107/S0907444913015448;
Nguyen G.T., Schaefer S., Gertz M., Weyand M., Steegborn C.;
"Structures of human sirtuin 3 complexes with ADP-ribose and with
carba-NAD+ and SRT1720: binding details and inhibition mechanism.";
Acta Crystallogr. D 69:1423-1432(2013).
-!- FUNCTION: NAD-dependent protein deacetylase. Activates or
deactivates mitochondrial target proteins by deacetylating key
lysine residues. Known targets include ACSS1, IDH, GDH, SOD2,
PDHA1, LCAD, SDHA and the ATP synthase subunit ATP5O. Contributes
to the regulation of the cellular energy metabolism. Important for
regulating tissue-specific ATP levels.
{ECO:0000269|PubMed:16788062, ECO:0000269|PubMed:18680753,
ECO:0000269|PubMed:18794531, ECO:0000269|PubMed:19535340,
ECO:0000269|PubMed:24121500, ECO:0000269|PubMed:24252090}.
-!- CATALYTIC ACTIVITY: NAD(+) + an acetylprotein = nicotinamide + O-
acetyl-ADP-ribose + a protein. {ECO:0000255|PROSITE-
ProRule:PRU00236, ECO:0000269|PubMed:12186850,
ECO:0000269|PubMed:12374852, ECO:0000269|PubMed:16788062}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=600 uM for NAD {ECO:0000269|PubMed:19535340};
-!- SUBUNIT: Interacts with NDUFA9, ACSS1, IDH2 and GDH
(PubMed:16788062, PubMed:18794531, PubMed:19535340,
PubMed:18680753). Interacts with PCCA (PubMed:23438705).
{ECO:0000269|PubMed:16788062, ECO:0000269|PubMed:18680753,
ECO:0000269|PubMed:18794531, ECO:0000269|PubMed:19535340,
ECO:0000269|PubMed:23438705}.
-!- INTERACTION:
P25705:ATP5A1; NbExp=2; IntAct=EBI-724621, EBI-351437;
O60313:OPA1; NbExp=3; IntAct=EBI-724621, EBI-1054131;
Q13309:SKP2; NbExp=5; IntAct=EBI-724621, EBI-456291;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000269|PubMed:12186850, ECO:0000269|PubMed:12374852,
ECO:0000269|PubMed:16079181, ECO:0000269|PubMed:18215119}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NTG7-1; Sequence=Displayed;
Name=2;
IsoId=Q9NTG7-2; Sequence=VSP_043792;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:10381378, ECO:0000269|PubMed:12374852}.
-!- PTM: Processed by mitochondrial processing peptidase (MPP) to give
a 28 kDa product. Such processing is probably essential for its
enzymatic activity. {ECO:0000269|PubMed:12186850}.
-!- MISCELLANEOUS: Has some ability to deacetylate histones in vitro,
but seeing its subcellular location, this is unlikely in vivo.
-!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
{ECO:0000305}.
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EMBL; AF083108; AAD40851.1; -; mRNA.
EMBL; AK299438; BAH13032.1; -; mRNA.
EMBL; AC136475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001042; AAH01042.1; -; mRNA.
EMBL; AL137276; CAB70674.1; -; mRNA.
CCDS; CCDS53590.1; -. [Q9NTG7-2]
CCDS; CCDS7691.1; -. [Q9NTG7-1]
PIR; T46348; T46348.
RefSeq; NP_001017524.1; NM_001017524.2. [Q9NTG7-2]
RefSeq; NP_036371.1; NM_012239.5. [Q9NTG7-1]
RefSeq; XP_016872919.1; XM_017017430.1. [Q9NTG7-2]
UniGene; Hs.716456; -.
PDB; 3GLR; X-ray; 1.80 A; A=118-399.
PDB; 3GLS; X-ray; 2.70 A; A/B/C/D/E/F=118-399.
PDB; 3GLT; X-ray; 2.10 A; A=118-399.
PDB; 3GLU; X-ray; 2.50 A; A=118-399.
PDB; 4BN4; X-ray; 1.30 A; A=116-399.
PDB; 4BN5; X-ray; 3.25 A; A/B/C/D/E/F/G/H/I/J/K/L=119-399.
PDB; 4BV3; X-ray; 2.00 A; A=116-399.
PDB; 4BVB; X-ray; 2.00 A; A=116-399.
PDB; 4BVE; X-ray; 2.05 A; A=116-399.
PDB; 4BVF; X-ray; 2.70 A; A=116-399.
PDB; 4BVG; X-ray; 2.50 A; A=116-399.
PDB; 4BVH; X-ray; 1.90 A; A/B/C=116-399.
PDB; 4C78; X-ray; 2.00 A; A=116-399.
PDB; 4C7B; X-ray; 2.10 A; A=117-399.
PDB; 4FVT; X-ray; 2.47 A; A=122-395.
PDB; 4FZ3; X-ray; 2.10 A; A=118-399.
PDB; 4HD8; X-ray; 2.30 A; A=116-399.
PDB; 4JSR; X-ray; 1.70 A; A=118-399.
PDB; 4JT8; X-ray; 2.26 A; A=118-399.
PDB; 4JT9; X-ray; 2.24 A; A=118-399.
PDB; 4O8Z; X-ray; 2.00 A; A=116-399.
PDB; 4V1C; X-ray; 2.95 A; A/B/E/G/I/K=121-394.
PDB; 5BWN; X-ray; 1.94 A; A=118-399.
PDB; 5BWO; X-ray; 2.38 A; A=118-399.
PDB; 5D7N; X-ray; 1.83 A; A/B/C/D/E/F=118-395.
PDBsum; 3GLR; -.
PDBsum; 3GLS; -.
PDBsum; 3GLT; -.
PDBsum; 3GLU; -.
PDBsum; 4BN4; -.
PDBsum; 4BN5; -.
PDBsum; 4BV3; -.
PDBsum; 4BVB; -.
PDBsum; 4BVE; -.
PDBsum; 4BVF; -.
PDBsum; 4BVG; -.
PDBsum; 4BVH; -.
PDBsum; 4C78; -.
PDBsum; 4C7B; -.
PDBsum; 4FVT; -.
PDBsum; 4FZ3; -.
PDBsum; 4HD8; -.
PDBsum; 4JSR; -.
PDBsum; 4JT8; -.
PDBsum; 4JT9; -.
PDBsum; 4O8Z; -.
PDBsum; 4V1C; -.
PDBsum; 5BWN; -.
PDBsum; 5BWO; -.
PDBsum; 5D7N; -.
ProteinModelPortal; Q9NTG7; -.
SMR; Q9NTG7; -.
BioGrid; 116982; 55.
DIP; DIP-46861N; -.
IntAct; Q9NTG7; 34.
MINT; MINT-4540133; -.
STRING; 9606.ENSP00000372191; -.
BindingDB; Q9NTG7; -.
ChEMBL; CHEMBL4461; -.
DrugBank; DB02059; Adenosine-5-Diphosphoribose.
GuidetoPHARMACOLOGY; 2709; -.
iPTMnet; Q9NTG7; -.
PhosphoSitePlus; Q9NTG7; -.
BioMuta; SIRT3; -.
DMDM; 38258651; -.
EPD; Q9NTG7; -.
MaxQB; Q9NTG7; -.
PaxDb; Q9NTG7; -.
PeptideAtlas; Q9NTG7; -.
PRIDE; Q9NTG7; -.
Ensembl; ENST00000382743; ENSP00000372191; ENSG00000142082. [Q9NTG7-1]
Ensembl; ENST00000529382; ENSP00000437216; ENSG00000142082. [Q9NTG7-2]
GeneID; 23410; -.
KEGG; hsa:23410; -.
UCSC; uc001lok.5; human. [Q9NTG7-1]
CTD; 23410; -.
DisGeNET; 23410; -.
EuPathDB; HostDB:ENSG00000142082.14; -.
GeneCards; SIRT3; -.
HGNC; HGNC:14931; SIRT3.
HPA; CAB037142; -.
HPA; HPA026809; -.
MIM; 604481; gene.
neXtProt; NX_Q9NTG7; -.
OpenTargets; ENSG00000142082; -.
PharmGKB; PA37936; -.
eggNOG; KOG2682; Eukaryota.
eggNOG; COG0846; LUCA.
GeneTree; ENSGT00870000136486; -.
HOVERGEN; HBG057095; -.
InParanoid; Q9NTG7; -.
KO; K11413; -.
OMA; CTGIVKP; -.
OrthoDB; EOG091G07CT; -.
PhylomeDB; Q9NTG7; -.
TreeFam; TF106181; -.
Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
SIGNOR; Q9NTG7; -.
ChiTaRS; SIRT3; human.
EvolutionaryTrace; Q9NTG7; -.
GeneWiki; SIRT3; -.
GenomeRNAi; 23410; -.
PRO; PR:Q9NTG7; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000142082; -.
CleanEx; HS_SIRT3; -.
ExpressionAtlas; Q9NTG7; baseline and differential.
Genevisible; Q9NTG7; HS.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; TAS:ProtInc.
GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
GO; GO:0017136; F:NAD-dependent histone deacetylase activity; IEA:InterPro.
GO; GO:0034979; F:NAD-dependent protein deacetylase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0009060; P:aerobic respiration; IMP:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0007005; P:mitochondrion organization; TAS:Reactome.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0034983; P:peptidyl-lysine deacetylation; IMP:UniProtKB.
GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
GO; GO:0006471; P:protein ADP-ribosylation; TAS:ProtInc.
GO; GO:0006476; P:protein deacetylation; IDA:UniProtKB.
Gene3D; 3.40.50.1220; -; 1.
InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
InterPro; IPR003000; Sirtuin.
InterPro; IPR017328; Sirtuin_class_I.
InterPro; IPR026590; Ssirtuin_cat_dom.
Pfam; PF02146; SIR2; 1.
PIRSF; PIRSF037938; SIR2_euk; 1.
SUPFAM; SSF52467; SSF52467; 1.
PROSITE; PS50305; SIRTUIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Hydrolase;
Metal-binding; Mitochondrion; NAD; Polymorphism; Reference proteome;
Transit peptide; Zinc.
TRANSIT 1 ? Mitochondrion. {ECO:0000255}.
CHAIN ? 399 NAD-dependent protein deacetylase
sirtuin-3, mitochondrial.
/FTId=PRO_0000032612.
DOMAIN 126 382 Deacetylase sirtuin-type.
{ECO:0000255|PROSITE-ProRule:PRU00236}.
NP_BIND 145 165 NAD.
NP_BIND 228 231 NAD.
NP_BIND 319 321 NAD.
NP_BIND 344 346 NAD.
ACT_SITE 248 248 Proton acceptor.
METAL 256 256 Zinc.
METAL 259 259 Zinc.
METAL 280 280 Zinc.
METAL 283 283 Zinc.
BINDING 366 366 NAD; via amide nitrogen. {ECO:0000250}.
MOD_RES 122 122 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8R104}.
VAR_SEQ 1 142 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043792.
VARIANT 80 80 R -> W (in dbSNP:rs28365927).
/FTId=VAR_051977.
VARIANT 208 208 V -> I (in dbSNP:rs11246020).
/FTId=VAR_051978.
VARIANT 369 369 G -> S (in dbSNP:rs3020901).
/FTId=VAR_051979.
MUTAGEN 7 7 R->G,Q: Suppresses targeting to
mitochondrion; when associated with G-13
or Q-13. {ECO:0000269|PubMed:12186850}.
MUTAGEN 13 13 R->G,Q: Suppresses targeting to
mitochondrion; when associated with G-7
or Q-7. {ECO:0000269|PubMed:12186850}.
MUTAGEN 17 17 R->G,Q: Reduces targeting to
mitochondrion; when associated with G-21
or Q-21. {ECO:0000269|PubMed:12186850}.
MUTAGEN 21 21 R->G,Q: Reduces targeting to
mitochondrion; when associated with G-17
or Q-17. {ECO:0000269|PubMed:12186850}.
MUTAGEN 99 100 RR->GG: Abolishes processing by MPP (in
vitro). {ECO:0000269|PubMed:12186850}.
MUTAGEN 229 229 N->A: Loss of function.
{ECO:0000269|PubMed:12186850}.
MUTAGEN 248 248 H->Y: Loss of function.
{ECO:0000269|PubMed:12186850,
ECO:0000269|PubMed:16788062,
ECO:0000269|PubMed:18794531}.
HELIX 125 133 {ECO:0000244|PDB:4BN4}.
TURN 134 136 {ECO:0000244|PDB:4C7B}.
STRAND 140 144 {ECO:0000244|PDB:4BN4}.
HELIX 146 152 {ECO:0000244|PDB:4BN4}.
STRAND 157 159 {ECO:0000244|PDB:4BN4}.
TURN 160 162 {ECO:0000244|PDB:4BN4}.
HELIX 164 168 {ECO:0000244|PDB:4BN4}.
STRAND 171 175 {ECO:0000244|PDB:4BN4}.
HELIX 176 180 {ECO:0000244|PDB:4BN4}.
HELIX 182 187 {ECO:0000244|PDB:4BN4}.
HELIX 190 199 {ECO:0000244|PDB:4BN4}.
STRAND 201 203 {ECO:0000244|PDB:4BV3}.
HELIX 208 218 {ECO:0000244|PDB:4BN4}.
STRAND 222 227 {ECO:0000244|PDB:4BN4}.
HELIX 233 236 {ECO:0000244|PDB:4BN4}.
HELIX 241 243 {ECO:0000244|PDB:4BN4}.
STRAND 244 246 {ECO:0000244|PDB:4BN4}.
STRAND 249 256 {ECO:0000244|PDB:4BN4}.
TURN 257 259 {ECO:0000244|PDB:4BN4}.
STRAND 262 264 {ECO:0000244|PDB:4BN4}.
HELIX 265 273 {ECO:0000244|PDB:4BN4}.
TURN 281 283 {ECO:0000244|PDB:4BN4}.
STRAND 286 291 {ECO:0000244|PDB:4BN4}.
HELIX 300 304 {ECO:0000244|PDB:4BN4}.
HELIX 305 311 {ECO:0000244|PDB:4BN4}.
STRAND 313 319 {ECO:0000244|PDB:4BN4}.
HELIX 327 330 {ECO:0000244|PDB:4BN4}.
HELIX 331 333 {ECO:0000244|PDB:4C7B}.
STRAND 340 346 {ECO:0000244|PDB:4BN4}.
HELIX 349 353 {ECO:0000244|PDB:4BN4}.
STRAND 359 364 {ECO:0000244|PDB:4BN4}.
HELIX 366 377 {ECO:0000244|PDB:4BN4}.
HELIX 380 391 {ECO:0000244|PDB:4BN4}.
SEQUENCE 399 AA; 43573 MW; 4BA8BD3AC5FC7901 CRC64;
MAFWGWRAAA ALRLWGRVVE RVEAGGGVGP FQACGCRLVL GGRDDVSAGL RGSHGARGEP
LDPARPLQRP PRPEVPRAFR RQPRAAAPSF FFSSIKGGRR SISFSVGASS VVGSGGSSDK
GKLSLQDVAE LIRARACQRV VVMVGAGIST PSGIPDFRSP GSGLYSNLQQ YDLPYPEAIF
ELPFFFHNPK PFFTLAKELY PGNYKPNVTH YFLRLLHDKG LLLRLYTQNI DGLERVSGIP
ASKLVEAHGT FASATCTVCQ RPFPGEDIRA DVMADRVPRC PVCTGVVKPD IVFFGEPLPQ
RFLLHVVDFP MADLLLILGT SLEVEPFASL TEAVRSSVPR LLINRDLVGP LAWHPRSRDV
AQLGDVVHGV ESLVELLGWT EEMRDLVQRE TGKLDGPDK


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