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Sirtuin 2

 G1NUJ8_MYOLU            Unreviewed;       389 AA.
G1NUJ8;
19-OCT-2011, integrated into UniProtKB/TrEMBL.
19-OCT-2011, sequence version 1.
28-MAR-2018, entry version 48.
RecName: Full=NAD-dependent protein deacetylase {ECO:0000256|PIRNR:PIRNR037938};
EC=3.5.1.- {ECO:0000256|PIRNR:PIRNR037938};
Name=SIRT2 {ECO:0000313|Ensembl:ENSMLUP00000000900};
Myotis lucifugus (Little brown bat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera;
Vespertilionidae; Myotis.
NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000000900, ECO:0000313|Proteomes:UP000001074};
[1] {ECO:0000313|Ensembl:ENSMLUP00000000900, ECO:0000313|Proteomes:UP000001074}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=21993624; DOI=10.1038/nature10530;
Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J.,
Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E.,
Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J.,
Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S.,
Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I.,
Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I.,
Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J.,
Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D.,
Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L.,
Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S.,
Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G.,
Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K.,
Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T.,
Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J.,
Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S.,
Pedersen J.S., Lander E.S., Kellis M.;
"A high-resolution map of human evolutionary constraint using 29
mammals.";
Nature 478:476-482(2011).
[2] {ECO:0000313|Ensembl:ENSMLUP00000000900}
IDENTIFICATION.
Ensembl;
Submitted (SEP-2011) to UniProtKB.
-!- FUNCTION: NAD-dependent protein deacetylase.
{ECO:0000256|PIRNR:PIRNR037938}.
-!- CATALYTIC ACTIVITY: NAD(+) + an acetylprotein = nicotinamide + O-
acetyl-ADP-ribose + a protein. {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; AAPE02032950; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; XP_006096744.1; XM_006096682.2.
STRING; 59463.ENSMLUP00000000900; -.
Ensembl; ENSMLUT00000000987; ENSMLUP00000000900; ENSMLUG00000000986.
GeneID; 102417115; -.
CTD; 22933; -.
eggNOG; KOG2682; Eukaryota.
eggNOG; COG0846; LUCA.
GeneTree; ENSGT00870000136486; -.
InParanoid; G1NUJ8; -.
OMA; LYPGSFI; -.
OrthoDB; EOG091G07CT; -.
TreeFam; TF106181; -.
Proteomes; UP000001074; Unassembled WGS sequence.
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; -; 2.
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.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000001074};
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};
Reference proteome {ECO:0000313|Proteomes:UP000001074};
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 389 AA; 43078 MW; 5A3E13B140D2AAED CRC64;
MAEPDPSDPL ETQAGKVQEA QDSDSDTEGG AAGGEAEMDF LRNLFSQTLG LGTQKERLLD
NLTLEGVAHY MLSERCRRVI CLVGAGISTS AGIPDFRSPS TGLYANLQKY HLPYPEAIFE
IGYFKKHPEP FFALAKELYP GQFKPTLCHY FIRLLKEKGL LRRCYTQNID TLERVAGLEP
EDLVEAHGTF YTSHCISPLC RKEYTLSWMK EKIFSEVTPK CENCQSVVKP DIVFFGENLP
ARFFSCIQAD FLNVDLLIIM GTSLQVQPFA SLISKTPLST PRLLINKEKT GQTDPFLGMM
MGLGGGMDFD SKKAYRDVAW LGDCDQGCLA LADLLGWKKE LEDLVRKEHA SIDAQSGLGS
PNPTTSASPR KSPPAAKEEA RTTEGEKPQ


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