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NAD-dependent protein deacetylase sirtuin-2 (Sirtuin (Silent mating type information regulation 2 homolog) 2 (S. cerevisiae), isoform CRA_a)

 A0A0G2JWM2_RAT          Unreviewed;       388 AA.
A0A0G2JWM2;
22-JUL-2015, integrated into UniProtKB/TrEMBL.
22-JUL-2015, sequence version 1.
05-DEC-2018, entry version 33.
RecName: Full=NAD-dependent protein deacetylase {ECO:0000256|PIRNR:PIRNR037938};
EC=3.5.1.- {ECO:0000256|PIRNR:PIRNR037938};
Name=Sirt2 {ECO:0000313|EMBL:EDM07874.1,
ECO:0000313|Ensembl:ENSRNOP00000069934, ECO:0000313|RGD:621481};
ORFNames=rCG_53640 {ECO:0000313|EMBL:EDM07874.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000069934, ECO:0000313|Proteomes:UP000002494};
[1] {ECO:0000313|Ensembl:ENSRNOP00000069934, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069934,
ECO:0000313|Proteomes:UP000002494};
PubMed=15057822; DOI=10.1038/nature02426;
Rat Genome Sequencing Project Consortium;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[2] {ECO:0000313|EMBL:EDM07874.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDM07874.1};
PubMed=15632090; DOI=10.1101/gr.2889405;
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
Istrail S., Li P., Sutton G.;
"Gene and alternative splicing annotation with AIR.";
Genome Res. 15:54-66(2005).
[3] {ECO:0000313|EMBL:EDM07874.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDM07874.1};
Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000213|PubMed:22673903}
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[5] {ECO:0000313|Ensembl:ENSRNOP00000069934}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069934};
Ensembl;
Submitted (JUN-2015) to UniProtKB.
-!- FUNCTION: NAD-dependent protein deacetylase.
{ECO:0000256|PIRNR:PIRNR037938}.
-!- 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|PIRNR:PIRNR037938};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000256|PIRNR:PIRNR037938};
-!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
{ECO:0000256|PIRNR:PIRNR037938}.
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EMBL; AABR07002849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH473979; EDM07874.1; -; Genomic_DNA.
RefSeq; XP_006228738.1; XM_006228676.3.
UniGene; Rn.59887; -.
Ensembl; ENSRNOT00000084839; ENSRNOP00000069934; ENSRNOG00000020102.
GeneID; 361532; -.
CTD; 22933; -.
RGD; 621481; Sirt2.
GeneTree; ENSGT00940000157514; -.
OMA; PAHYFVR; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000020102; Expressed in 10 organ(s), highest expression level in testis.
GO; GO:0005814; C:centriole; IEA:Ensembl.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0005694; C:chromosome; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0072687; C:meiotic spindle; IEA:Ensembl.
GO; GO:0005874; C:microtubule; IEA:Ensembl.
GO; GO:0030496; C:midbody; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IEA:Ensembl.
GO; GO:0033010; C:paranodal junction; IEA:Ensembl.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0035035; F:histone acetyltransferase binding; IEA:Ensembl.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-UniRule.
GO; GO:0046970; F:NAD-dependent histone deacetylase activity (H4-K16 specific); IEA:Ensembl.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0042903; F:tubulin deacetylase activity; IEA:Ensembl.
GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
GO; GO:0044242; P:cellular lipid catabolic process; IEA:Ensembl.
GO; GO:0061433; P:cellular response to caloric restriction; IEA:Ensembl.
GO; GO:0071872; P:cellular response to epinephrine stimulus; IEA:Ensembl.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
GO; GO:0071219; P:cellular response to molecule of bacterial origin; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0070932; P:histone H3 deacetylation; IEA:Ensembl.
GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl.
GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:1900425; P:negative regulation of defense response to bacterium; IEA:Ensembl.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; IEA:Ensembl.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0045843; P:negative regulation of striated muscle tissue development; IEA:Ensembl.
GO; GO:0061428; P:negative regulation of transcription from RNA polymerase II promoter in response to hypoxia; IEA:Ensembl.
GO; GO:0034983; P:peptidyl-lysine deacetylation; IEA:Ensembl.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IEA:Ensembl.
GO; GO:0051781; P:positive regulation of cell division; IEA:Ensembl.
GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IEA:Ensembl.
GO; GO:0045836; P:positive regulation of meiotic nuclear division; IEA:Ensembl.
GO; GO:1900195; P:positive regulation of oocyte maturation; IEA:Ensembl.
GO; GO:2000777; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
Gene3D; 3.30.1600.10; -; 1.
InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
InterPro; IPR003000; Sirtuin.
InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
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;
Complete proteome {ECO:0000313|Proteomes:UP000002494};
Hydrolase {ECO:0000256|PIRNR:PIRNR037938};
Metal-binding {ECO:0000256|PIRNR:PIRNR037938,
ECO:0000256|PIRSR:PIRSR037938-3};
NAD {ECO:0000256|PIRNR:PIRNR037938, ECO:0000256|PIRSR:PIRSR037938-2};
Proteomics identification {ECO:0000213|PeptideAtlas:A0A0G2JWM2};
Reference proteome {ECO:0000313|Proteomes:UP000002494};
Zinc {ECO:0000256|PIRNR:PIRNR037938, ECO:0000256|PIRSR:PIRSR037938-3}.
DOMAIN 65 340 Deacetylase sirtuin-type.
{ECO:0000259|PROSITE:PS50305}.
NP_BIND 84 104 NAD. {ECO:0000256|PIRSR:PIRSR037938-2}.
NP_BIND 167 170 NAD. {ECO:0000256|PIRSR:PIRSR037938-2}.
NP_BIND 261 263 NAD. {ECO:0000256|PIRSR:PIRSR037938-2}.
NP_BIND 286 288 NAD. {ECO:0000256|PIRSR:PIRSR037938-2}.
ACT_SITE 187 187 Proton acceptor.
{ECO:0000256|PIRSR:PIRSR037938-1}.
METAL 195 195 Zinc. {ECO:0000256|PIRSR:PIRSR037938-3}.
METAL 200 200 Zinc. {ECO:0000256|PIRSR:PIRSR037938-3}.
METAL 221 221 Zinc. {ECO:0000256|PIRSR:PIRSR037938-3}.
METAL 224 224 Zinc. {ECO:0000256|PIRSR:PIRSR037938-3}.
BINDING 324 324 NAD; via amide nitrogen.
{ECO:0000256|PIRSR:PIRSR037938-2}.
SEQUENCE 388 AA; 43163 MW; 73E419C406D5A9B6 CRC64;
MAEPDPSDPL ENQAGKVQEA QDSDSDTEGG ATGGEAEMDF LRNLFTQTLG LGSQKERLLD
ELTLEGVTRY MQSERCRRVI CLVGAGISTS AGIPDFRSPS TGLYANLEKY HLPYPEAIFE
ISYFKKHPEP FFALAKELYP GQFKPTICHY FIRLLKEKGL LLRCYTQNID TLERVAGLEP
QDLVEAHGTF YTSHCVNTSC GKEYTMSWMK EKIFSEATPK CEKCQNVVKP DIVFFGENLP
PRFFSCMQSD FSKVDLLIIM GTSLQVQPFA SLISKAPLAT PRLLINKEKT GQTDPFLGMM
MGLGGGMDFD SKKAYRDVAW LGDCDQGCLA LADLLGWKKE LEDLVRREHA NIDAQSGSQA
SNPSATVSPR KSPPPAKEAA RTKEKEEH


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