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NAD-dependent protein deacetylase sirtuin-6 (EC 3.5.1.-) (Regulatory protein SIR2 homolog 6) (SIR2-like protein 6)

 SIR6_MOUSE              Reviewed;         334 AA.
P59941;
31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
31-OCT-2003, sequence version 1.
25-OCT-2017, entry version 119.
RecName: Full=NAD-dependent protein deacetylase sirtuin-6;
EC=3.5.1.-;
AltName: Full=Regulatory protein SIR2 homolog 6;
AltName: Full=SIR2-like protein 6;
Name=Sirt6; Synonyms=Sir2l6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Limb;
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).
[2]
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND MUTAGENESIS OF SER-56 AND HIS-133.
PubMed=15795229; DOI=10.1074/jbc.M413296200;
Liszt G., Ford E., Kurtev M., Guarente L.;
"Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase.";
J. Biol. Chem. 280:21313-21320(2005).
[3]
DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=16439206; DOI=10.1016/j.cell.2005.11.044;
Mostoslavsky R., Chua K.F., Lombard D.B., Pang W.W., Fischer M.R.,
Gellon L., Liu P., Mostoslavsky G., Franco S., Murphy M.M.,
Mills K.D., Patel P., Hsu J.T., Hong A.L., Ford E., Cheng H.-L.,
Kennedy C., Nunez N., Bronson R., Frendewey D., Auerbach W.,
Valenzuela D., Karow M., Hottiger M.O., Hursting S., Barrett J.C.,
Guarente L., Mulligan R., Demple B., Yancopoulos G.D., Alt F.W.;
"Genomic instability and aging-like phenotype in the absence of
mammalian SIRT6.";
Cell 124:315-329(2006).
[4]
FUNCTION.
PubMed=19220062; DOI=10.1021/bi802093g;
Du J., Jiang H., Lin H.;
"Investigating the ADP-ribosyltransferase activity of sirtuins with
NAD analogues and 32P-NAD.";
Biochemistry 48:2878-2890(2009).
[5]
FUNCTION, AND INTERACTION WITH RELA.
PubMed=19135889; DOI=10.1016/j.cell.2008.10.052;
Kawahara T.L.A., Michishita E., Adler A.S., Damian M., Berber E.,
Lin M., McCord R.A., Ongaigui K.C.L., Boxer L.D., Chang H.Y.,
Chua K.F.;
"SIRT6 links histone H3 lysine 9 deacetylation to NF-kappaB-dependent
gene expression and organismal life span.";
Cell 136:62-74(2009).
[6]
FUNCTION, AND MUTAGENESIS OF HIS-133.
PubMed=19597350; DOI=10.4161/cc.8.16.9329;
Yang B., Zwaans B.M.M., Eckersdorff M., Lombard D.B.;
"The sirtuin SIRT6 deacetylates H3 K56Ac in vivo to promote genomic
stability.";
Cell Cycle 8:2662-2663(2009).
[7]
FUNCTION.
PubMed=19151729; DOI=10.1038/nm.1906;
Van Gool F., Galli M., Gueydan C., Kruys V., Prevot P.P., Bedalov A.,
Mostoslavsky R., Alt F.W., De Smedt T., Leo O.;
"Intracellular NAD levels regulate tumor necrosis factor protein
synthesis in a sirtuin-dependent manner.";
Nat. Med. 15:206-210(2009).
[8]
FUNCTION IN REGULATION OF GLUCOSE HOMEOSTASIS.
PubMed=20141841; DOI=10.1016/j.cell.2009.12.041;
Zhong L., D'Urso A., Toiber D., Sebastian C., Henry R.E.,
Vadysirisack D.D., Guimaraes A., Marinelli B., Wikstrom J.D., Nir T.,
Clish C.B., Vaitheesvaran B., Iliopoulos O., Kurland I., Dor Y.,
Weissleder R., Shirihai O.S., Ellisen L.W., Espinosa J.M.,
Mostoslavsky R.;
"The histone deacetylase Sirt6 regulates glucose homeostasis via
Hif1alpha.";
Cell 140:280-293(2010).
[9]
FUNCTION IN REGULATION OF LIFE SPAN.
PubMed=22367546; DOI=10.1038/nature10815;
Kanfi Y., Naiman S., Amir G., Peshti V., Zinman G., Nahum L.,
Bar-Joseph Z., Cohen H.Y.;
"The sirtuin SIRT6 regulates lifespan in male mice.";
Nature 483:218-221(2012).
-!- FUNCTION: NAD-dependent protein deacetylase. Has deacetylase
activity towards histone H3K9Ac and H3K56Ac. Modulates acetylation
of histone H3 in telomeric chromatin during the S-phase of the
cell cycle. Deacetylates histone H3K9Ac at NF-kappa-B target
promoters and may down-regulate the expression of a subset of NF-
kappa-B target genes. Deacetylation of nucleosomes interferes with
RELA binding to target DNA. May be required for the association of
WRN with telomeres during S-phase and for normal telomere
maintenance. On DNA damage, promotes DNA end resection via
deacetylation of RBBP8. Has very weak deacetylase activity and can
bind NAD(+) in the absence of acetylated substrate (By
similarity). Acts as a corepressor of the transcription factor
Hif1a to control the expression of multiple glycolytic genes to
regulate glucose homeostasis. Required for genomic stability.
Required for normal IGF1 serum levels and normal glucose
homeostasis. Modulates cellular senescence and apoptosis.
Regulates the production of TNF protein. Has a role in the
regulation of life span in male mice, but not in female mice.
{ECO:0000250, ECO:0000269|PubMed:16439206,
ECO:0000269|PubMed:19135889, ECO:0000269|PubMed:19151729,
ECO:0000269|PubMed:19220062, ECO:0000269|PubMed:19597350,
ECO:0000269|PubMed:20141841, ECO:0000269|PubMed:22367546}.
-!- CATALYTIC ACTIVITY: NAD(+) + an acetylprotein = nicotinamide + O-
acetyl-ADP-ribose + a protein. {ECO:0000255|PROSITE-
ProRule:PRU00236, ECO:0000269|PubMed:15795229}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBUNIT: Interacts with RBBP8; the interaction deacetylates RBBP8
(By similarity). Interacts with RELA. {ECO:0000250,
ECO:0000269|PubMed:19135889}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15795229,
ECO:0000269|PubMed:16439206}. Note=Predominantly nuclear.
Associated with chromatin.
-!- TISSUE SPECIFICITY: Highest levels are found in muscle, thymus,
spleen, brain and heart (at protein level).
{ECO:0000269|PubMed:15795229, ECO:0000269|PubMed:16439206}.
-!- DEVELOPMENTAL STAGE: Expression peaks at embryonic day 11 and
persists into adulthood. {ECO:0000269|PubMed:15795229}.
-!- DISRUPTION PHENOTYPE: Impaired genomic stability. No visible
phenotype at birth. Normal development during the first two weeks,
except for reduced growth. At about three weeks after birth, the
mice undergo compound degenerative processes, fail to thrive, and
die about 24 days after birth. They exhibit acute loss of
subcutaneous fat, lordokyphosis, erosion of the superficial colon
epithelium, severe lymphopenia, osteopenia, severely reduced IGF1
serum levels and extremely low serum glucose levels.
{ECO:0000269|PubMed:16439206}.
-!- MISCELLANEOUS: The reported ADP-ribosyltransferase activity of
sirtuins is likely some inefficient side reaction of the
deacetylase activity and may not be physiologically relevant.
{ECO:0000305|PubMed:19220062}.
-!- SIMILARITY: Belongs to the sirtuin family. Class IV subfamily.
{ECO:0000305}.
-!- CAUTION: Was originally thought to be a protein ADP-
ribosyltransferase. {ECO:0000305|PubMed:15795229}.
-----------------------------------------------------------------------
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EMBL; BC052763; AAH52763.1; -; mRNA.
CCDS; CCDS24066.1; -.
RefSeq; NP_853617.1; NM_181586.3.
UniGene; Mm.131825; -.
UniGene; Mm.25643; -.
ProteinModelPortal; P59941; -.
SMR; P59941; -.
BioGrid; 206064; 1.
IntAct; P59941; 1.
STRING; 10090.ENSMUSP00000048971; -.
iPTMnet; P59941; -.
PhosphoSitePlus; P59941; -.
EPD; P59941; -.
MaxQB; P59941; -.
PaxDb; P59941; -.
PRIDE; P59941; -.
Ensembl; ENSMUST00000042923; ENSMUSP00000048971; ENSMUSG00000034748.
GeneID; 50721; -.
KEGG; mmu:50721; -.
UCSC; uc007giy.2; mouse.
CTD; 51548; -.
MGI; MGI:1354161; Sirt6.
eggNOG; KOG1905; Eukaryota.
eggNOG; COG0846; LUCA.
GeneTree; ENSGT00530000063706; -.
HOGENOM; HOG000231240; -.
HOVERGEN; HBG060028; -.
InParanoid; P59941; -.
KO; K11416; -.
OMA; NVLDWEH; -.
OrthoDB; EOG091G0FOW; -.
PhylomeDB; P59941; -.
TreeFam; TF106184; -.
Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
ChiTaRS; Sirt6; mouse.
PRO; PR:P59941; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000034748; -.
ExpressionAtlas; P59941; baseline and differential.
Genevisible; P59941; MM.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0005724; C:nuclear telomeric heterochromatin; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003956; F:NAD(P)+-protein-arginine ADP-ribosyltransferase activity; IDA:UniProtKB.
GO; GO:0070403; F:NAD+ binding; ISS:UniProtKB.
GO; GO:0017136; F:NAD-dependent histone deacetylase activity; ISS:UniProtKB.
GO; GO:0046969; F:NAD-dependent histone deacetylase activity (H3-K9 specific); IMP:CACAO.
GO; GO:0003714; F:transcription corepressor activity; IGI:CACAO.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0006284; P:base-excision repair; IMP:CACAO.
GO; GO:0042593; P:glucose homeostasis; IMP:CACAO.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:CACAO.
GO; GO:0046325; P:negative regulation of glucose import; IMP:CACAO.
GO; GO:0045820; P:negative regulation of glycolytic process; IMP:CACAO.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:CACAO.
GO; GO:1905555; P:positive regulation blood vessel branching; ISO:MGI.
GO; GO:1902732; P:positive regulation of chondrocyte proliferation; ISO:MGI.
GO; GO:0031940; P:positive regulation of chromatin silencing at telomere; ISO:MGI.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:CACAO.
GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:CACAO.
GO; GO:0032206; P:positive regulation of telomere maintenance; ISO:MGI.
GO; GO:1905549; P:positive regulation of telomeric heterochromatin assembly; ISO:MGI.
GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:MGI.
GO; GO:0003247; P:post-embryonic cardiac muscle cell growth involved in heart morphogenesis; IEA:Ensembl.
GO; GO:0006471; P:protein ADP-ribosylation; IDA:UniProtKB.
GO; GO:0031648; P:protein destabilization; IMP:CACAO.
GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
Gene3D; 3.40.50.1220; -; 1.
InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
InterPro; IPR003000; Sirtuin.
InterPro; IPR026590; Ssirtuin_cat_dom.
Pfam; PF02146; SIR2; 2.
SUPFAM; SSF52467; SSF52467; 1.
PROSITE; PS50305; SIRTUIN; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Hydrolase; Metal-binding; NAD;
Nucleus; Phosphoprotein; Reference proteome; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q8N6T7}.
CHAIN 2 334 NAD-dependent protein deacetylase
sirtuin-6.
/FTId=PRO_0000110270.
DOMAIN 35 274 Deacetylase sirtuin-type.
{ECO:0000255|PROSITE-ProRule:PRU00236}.
NP_BIND 52 71 NAD. {ECO:0000250}.
NP_BIND 113 116 NAD. {ECO:0000250}.
NP_BIND 214 216 NAD. {ECO:0000250}.
NP_BIND 240 242 NAD. {ECO:0000250}.
ACT_SITE 133 133 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 141 141 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 144 144 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 166 166 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 177 177 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
BINDING 258 258 NAD; via amide nitrogen. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q8N6T7}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:Q8N6T7}.
MUTAGEN 56 56 S->A: Loss of activity.
{ECO:0000269|PubMed:15795229}.
MUTAGEN 133 133 H->Y: Loss of activity.
{ECO:0000269|PubMed:15795229,
ECO:0000269|PubMed:19597350}.
SEQUENCE 334 AA; 36920 MW; 75FD950B42D68A1A CRC64;
MSVNYAAGLS PYADKGKCGL PEIFDPPEEL ERKVWELARL MWQSSSVVFH TGAGISTASG
IPDFRGPHGV WTMEERGLAP KFDTTFENAR PSKTHMALVQ LERMGFLSFL VSQNVDGLHV
RSGFPRDKLA ELHGNMFVEE CPKCKTQYVR DTVVGTMGLK ATGRLCTVAK TRGLRACRGE
LRDTILDWED SLPDRDLMLA DEASRTADLS VTLGTSLQIR PSGNLPLATK RRGGRLVIVN
LQPTKHDRQA DLRIHGYVDE VMCRLMKHLG LEIPAWDGPC VLDKALPPLP RPVALKAEPP
VHLNGAVHVS YKSKPNSPIL HRPPKRVKTE AAPS


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