SIR7_MOUSE
ID SIR7_MOUSE Reviewed; 402 AA.
AC Q8BKJ9; A2ABY7; Q6X7B7; Q8QZZ5;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=NAD-dependent protein deacetylase sirtuin-7;
DE EC=2.3.1.286 {ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:25200183, ECO:0000269|PubMed:31075303};
DE AltName: Full=NAD-dependent protein deacylase sirtuin-7;
DE EC=2.3.1.- {ECO:0000269|PubMed:30026585};
DE AltName: Full=Regulatory protein SIR2 homolog 7;
DE AltName: Full=SIR2-like protein 7;
GN Name=Sirt7 {ECO:0000303|PubMed:16618798, ECO:0000312|MGI:MGI:2385849};
GN Synonyms=Sir2l7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic carcinoma;
RA Poloumienko A., Bakovic M.;
RT "Mus musculus sirtuin 7 (silent mating type information regulation 2,
RT homolog 7) mRNA.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-402.
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16618798; DOI=10.1101/gad.1399706;
RA Ford E., Voit R., Liszt G., Magin C., Grummt I., Guarente L.;
RT "Mammalian Sir2 homolog SIRT7 is an activator of RNA polymerase I
RT transcription.";
RL Genes Dev. 20:1075-1080(2006).
RN [5]
RP FUNCTION, ACTIVE SITE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-188.
RX PubMed=18239138; DOI=10.1161/circresaha.107.164558;
RA Vakhrusheva O., Smolka C., Gajawada P., Kostin S., Boettger T., Kubin T.,
RA Braun T., Bober E.;
RT "Sirt7 increases stress resistance of cardiomyocytes and prevents apoptosis
RT and inflammatory cardiomyopathy in mice.";
RL Circ. Res. 102:703-710(2008).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25200183; DOI=10.1016/j.cmet.2014.08.001;
RA Ryu D., Jo Y.S., Lo Sasso G., Stein S., Zhang H., Perino A., Lee J.U.,
RA Zeviani M., Romand R., Hottiger M.O., Schoonjans K., Auwerx J.;
RT "A SIRT7-dependent acetylation switch of GABPbeta1 controls mitochondrial
RT function.";
RL Cell Metab. 20:856-869(2014).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27225932; DOI=10.15252/embj.201593499;
RA Vazquez B.N., Thackray J.K., Simonet N.G., Kane-Goldsmith N.,
RA Martinez-Redondo P., Nguyen T., Bunting S., Vaquero A., Tischfield J.A.,
RA Serrano L.;
RT "SIRT7 promotes genome integrity and modulates non-homologous end joining
RT DNA repair.";
RL EMBO J. 35:1488-1503(2016).
RN [8]
RP FUNCTION, AND INTERACTION WITH DNMT1 AND SIRT1.
RX PubMed=28842251; DOI=10.1016/j.bbrc.2017.08.081;
RA Ianni A., Hoelper S., Krueger M., Braun T., Bober E.;
RT "Sirt7 stabilizes rDNA heterochromatin through recruitment of DNMT1 and
RT Sirt1.";
RL Biochem. Biophys. Res. Commun. 492:434-440(2017).
RN [9]
RP FUNCTION, INTERACTION WITH SIRT1, AND MUTAGENESIS OF HIS-188.
RX PubMed=28923965; DOI=10.1073/pnas.1706945114;
RA Fang J., Ianni A., Smolka C., Vakhrusheva O., Nolte H., Krueger M.,
RA Wietelmann A., Simonet N.G., Adrian-Segarra J.M., Vaquero A., Braun T.,
RA Bober E.;
RT "Sirt7 promotes adipogenesis in the mouse by inhibiting autocatalytic
RT activation of Sirt1.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E8352-E8361(2017).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, ACTIVE SITE, AND
RP MUTAGENESIS OF HIS-188.
RX PubMed=30026585; DOI=10.1038/s41467-018-05187-4;
RA Fukuda M., Yoshizawa T., Karim M.F., Sobuz S.U., Korogi W., Kobayasi D.,
RA Okanishi H., Tasaki M., Ono K., Sawa T., Sato Y., Chirifu M., Masuda T.,
RA Nakamura T., Tanoue H., Nakashima K., Kobashigawa Y., Morioka H., Bober E.,
RA Ohtsuki S., Yamagata Y., Ando Y., Oike Y., Araki N., Takeda S., Mizuta H.,
RA Yamagata K.;
RT "SIRT7 has a critical role in bone formation by regulating lysine acylation
RT of SP7/Osterix.";
RL Nat. Commun. 9:2833-2833(2018).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF HIS-188.
RX PubMed=31075303; DOI=10.1016/j.bbamcr.2019.05.001;
RA Sobuz S.U., Sato Y., Yoshizawa T., Karim F., Ono K., Sawa T., Miyamoto Y.,
RA Oka M., Yamagata K.;
RT "SIRT7 regulates the nuclear export of NF-kappaB p65 by deacetylating
RT Ran.";
RL Biochim. Biophys. Acta 1866:1355-1367(2019).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31256246; DOI=10.1007/s00412-019-00713-9;
RA Vazquez B.N., Blengini C.S., Hernandez Y., Serrano L., Schindler K.;
RT "SIRT7 promotes chromosome synapsis during prophase I of female meiosis.";
RL Chromosoma 128:369-383(2019).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=31226208; DOI=10.1093/nar/gkz519;
RA Vazquez B.N., Thackray J.K., Simonet N.G., Chahar S., Kane-Goldsmith N.,
RA Newkirk S.J., Lee S., Xing J., Verzi M.P., An W., Vaquero A.,
RA Tischfield J.A., Serrano L.;
RT "SIRT7 mediates L1 elements transcriptional repression and their
RT association with the nuclear lamina.";
RL Nucleic Acids Res. 47:7870-7885(2019).
CC -!- FUNCTION: NAD-dependent protein-lysine deacylase that can act both as a
CC deacetylase or deacylase (desuccinylase, depropionylase and
CC deglutarylase), depending on the context (PubMed:25200183,
CC PubMed:30026585, PubMed:31075303). Specifically mediates deacetylation
CC of histone H3 at 'Lys-18' (H3K18Ac) (By similarity). In contrast to
CC other histone deacetylases, displays strong preference for a specific
CC histone mark, H3K18Ac, directly linked to control of gene expression
CC (By similarity). H3K18Ac is mainly present around the transcription
CC start site of genes and has been linked to activation of nuclear
CC hormone receptors; SIRT7 thereby acts as a transcription repressor (By
CC similarity). Moreover, H3K18 hypoacetylation has been reported as a
CC marker of malignancy in various cancers and seems to maintain the
CC transformed phenotype of cancer cells (By similarity). Also able to
CC mediate deacetylation of histone H3 at 'Lys-36' (H3K36Ac) in the
CC context of nucleosomes (By similarity). Also mediates deacetylation of
CC non-histone proteins, such as ATM, CDK9, DDX21, DDB1, FBL,
CC FKBP5/FKBP51, GABPB1, RAN, RRP9/U3-55K and POLR1E/PAF53 (By
CC similarity). Enriched in nucleolus where it stimulates transcription
CC activity of the RNA polymerase I complex (PubMed:16618798). Acts by
CC mediating the deacetylation of the RNA polymerase I subunit
CC POLR1E/PAF53, thereby promoting the association of RNA polymerase I
CC with the rDNA promoter region and coding region (By similarity). In
CC response to metabolic stress, SIRT7 is released from nucleoli leading
CC to hyperacetylation of POLR1E/PAF53 and decreased RNA polymerase I
CC transcription (By similarity). Required to restore the transcription of
CC ribosomal RNA (rRNA) at the exit from mitosis (PubMed:16618798).
CC Promotes pre-ribosomal RNA (pre-rRNA) cleavage at the 5'-terminal
CC processing site by mediating deacetylation of RRP9/U3-55K, a core
CC subunit of the U3 snoRNP complex (By similarity). Mediates 'Lys-37'
CC deacetylation of Ran, thereby regulating the nuclear export of NF-
CC kappa-B subunit RELA/p65 (PubMed:31075303). Acts as a regulator of DNA
CC damage repair by mediating deacetylation of ATM during the late stages
CC of DNA damage response, promoting ATM dephosphorylation and
CC deactivation (By similarity). May also deacetylate p53/TP53 and
CC promotes cell survival, however such data need additional confirmation
CC (PubMed:18239138). Suppresses the activity of the DCX (DDB1-CUL4-X-box)
CC E3 ubiquitin-protein ligase complexes by mediating deacetylation of
CC DDB1, which prevents the interaction between DDB1 and CUL4 (CUL4A or
CC CUL4B) (By similarity). Activates RNA polymerase II transcription by
CC mediating deacetylation of CDK9, thereby promoting 'Ser-2'
CC phosphorylation of the C-terminal domain (CTD) of RNA polymerase II (By
CC similarity). Deacetylates FBL, promoting histone-glutamine
CC methyltransferase activity of FBL (By similarity). Acts as a regulator
CC of mitochondrial function by catalyzing deacetylation of GABPB1
CC (PubMed:25200183). Regulates Akt/AKT1 activity by mediating
CC deacetylation of FKBP5/FKBP51 (By similarity). Required to prevent R-
CC loop-associated DNA damage and transcription-associated genomic
CC instability by mediating deacetylation and subsequent activation of
CC DDX21, thereby overcoming R-loop-mediated stalling of RNA polymerases
CC (By similarity). In addition to protein deacetylase activity, also acts
CC as protein-lysine deacylase (By similarity). Acts as a protein
CC depropionylase by mediating depropionylation of Osterix (SP7), thereby
CC regulating bone formation by osteoblasts (PubMed:30026585). Acts as a
CC histone deglutarylase by mediating deglutarylation of histone H4 on
CC 'Lys-91' (H4K91glu); a mark that destabilizes nucleosomes by promoting
CC dissociation of the H2A-H2B dimers from nucleosomes (By similarity).
CC Acts as a histone desuccinylase: in response to DNA damage, recruited
CC to DNA double-strand breaks (DSBs) and catalyzes desuccinylation of
CC histone H3 on 'Lys-122' (H3K122succ), thereby promoting chromatin
CC condensation and DSB repair (By similarity). Also promotes DSB repair
CC by promoting H3K18Ac deacetylation, regulating non-homologous end
CC joining (NHEJ) (PubMed:27225932). Along with its role in DNA repair,
CC required for chromosome synapsis during prophase I of female meiosis by
CC catalyzing H3K18Ac deacetylation (PubMed:31256246). Involved in
CC transcriptional repression of LINE-1 retrotransposon via H3K18Ac
CC deacetylation, and promotes their association with the nuclear lamina
CC (PubMed:31226208). Required to stabilize ribosomal DNA (rDNA)
CC heterochromatin and prevent cellular senescence induced by rDNA
CC instability (PubMed:28842251). Acts as a negative regulator of SIRT1 by
CC preventing autodeacetylation of SIRT1, restricting SIRT1 deacetylase
CC activity (PubMed:28923965). {ECO:0000250|UniProtKB:Q9NRC8,
CC ECO:0000269|PubMed:16618798, ECO:0000269|PubMed:18239138,
CC ECO:0000269|PubMed:25200183, ECO:0000269|PubMed:27225932,
CC ECO:0000269|PubMed:28842251, ECO:0000269|PubMed:28923965,
CC ECO:0000269|PubMed:30026585, ECO:0000269|PubMed:31075303,
CC ECO:0000269|PubMed:31226208, ECO:0000269|PubMed:31256246}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-
CC ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767;
CC EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236,
CC ECO:0000269|PubMed:25200183, ECO:0000269|PubMed:31075303};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43637;
CC Evidence={ECO:0000269|PubMed:25200183, ECO:0000269|PubMed:31075303};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-glutaryl-L-lysyl-[protein] + NAD(+) = 2''-O-
CC glutaryl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:47664, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11875,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:87828, ChEBI:CHEBI:87829;
CC Evidence={ECO:0000250|UniProtKB:Q9NRC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47665;
CC Evidence={ECO:0000250|UniProtKB:Q9NRC8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-succinyl-L-lysyl-[protein] + NAD(+) = 2''-O-
CC succinyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:47668, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:11877,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:87830, ChEBI:CHEBI:87832;
CC Evidence={ECO:0000250|UniProtKB:Q9NRC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47669;
CC Evidence={ECO:0000250|UniProtKB:Q9NRC8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-propanoyl-L-lysyl-[protein] + NAD(+) = 3''-O-
CC propanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:23500, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13758,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:138019, ChEBI:CHEBI:145015;
CC Evidence={ECO:0000269|PubMed:30026585};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23501;
CC Evidence={ECO:0000269|PubMed:30026585};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9NXA8};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9NXA8};
CC -!- ACTIVITY REGULATION: NAD-dependent protein-lysine deacetylase and
CC deacylase activities are activated by nucleic acids. Histone
CC deacetylase activity is activated by DNA. Protein-lysine deacylase
CC activity is activated by RNA. H3K18Ac histone deacetylase activity is
CC inhibited by methylation at Arg-390. H3K18Ac histone deacetylase
CC activity is inhibited by deubiquitination by USP7.
CC {ECO:0000250|UniProtKB:Q9NRC8}.
CC -!- SUBUNIT: Interacts with UBTF and the RNA polymerase I complex (By
CC similarity). Interacts with components of the B-WICH complex, such as
CC MYBBP1A, SMARCA5/SNF2H and BAZ1B/WSTF (By similarity). Interacts with
CC ELK4, leading to stabilization at target promoters for H3K18Ac
CC deacetylation (By similarity). Interacts with histone H2A and/or
CC histone H2B (By similarity). Interacts with DNMT1 (PubMed:28842251).
CC Interacts with SIRT1 (PubMed:28842251, PubMed:28923965).
CC {ECO:0000250|UniProtKB:Q9NRC8, ECO:0000269|PubMed:28842251,
CC ECO:0000269|PubMed:28923965}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16618798,
CC ECO:0000269|PubMed:25200183}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:25200183}. Chromosome {ECO:0000269|PubMed:27225932,
CC ECO:0000269|PubMed:31226208}. Cytoplasm {ECO:0000250|UniProtKB:Q9NRC8}.
CC Note=Mainly localizes in the nucleolus and nucleoplasm (By similarity).
CC Associated with rDNA promoter and transcribed region (By similarity).
CC Associated with nucleolar organizer regions during mitosis (By
CC similarity). In response to stress, released from nucleolus to
CC nucleoplasm (By similarity). Associated with chromatin (By similarity).
CC In response to DNA damage, recruited to DNA double-strand breaks (DSBs)
CC sites (PubMed:27225932). Located close to the nuclear membrane when in
CC the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q9NRC8,
CC ECO:0000269|PubMed:27225932}.
CC -!- TISSUE SPECIFICITY: Detected in liver, spleen and testis
CC (PubMed:16618798). Detected in embryos (PubMed:16618798).
CC {ECO:0000269|PubMed:16618798}.
CC -!- PTM: Phosphorylated during mitosis. {ECO:0000250|UniProtKB:Q9NRC8}.
CC -!- PTM: Methylation at Arg-390 by PRMT6 inhibits the H3K18Ac histone
CC deacetylase activity, promoting mitochondria biogenesis and maintaining
CC mitochondria respiration. {ECO:0000250|UniProtKB:Q9NRC8}.
CC -!- PTM: Ubiquitinated via 'Lys-63'-linked ubiquitin chains.
CC Deubiquitinated by USP7, inhibiting the H3K18Ac histone deacetylase
CC activity and regulating gluconeogenesis.
CC {ECO:0000250|UniProtKB:Q9NRC8}.
CC -!- DISRUPTION PHENOTYPE: Mice show a reduction in lifespan and develop
CC heart hypertrophy (PubMed:18239138). The mean and maximum lifespan is
CC reduced by 59% and 55% (PubMed:18239138). Mice develop kyphosis and
CC lose subcutaneous fat early in life; they also show a general decrease
CC in stress-resistance mechanisms (PubMed:18239138). Mice suffer from
CC degenerative heart hypertrophy and inflammatory cardiomyopathy
CC (PubMed:18239138). Hearts are also characterized by an extensive
CC fibrosis (PubMed:18239138). Mice also display multisystemic
CC mitochondrial dysfunction, characterized by increased blood lactate
CC levels, reduced exercise performance, cardiac dysfunction, hepatic
CC microvesicular steatosis and age-related hearing loss
CC (PubMed:25200183). Cells show impaired oxidative phosphorylation
CC (OxPhos) (PubMed:25200183). A substantial proportion of mice also show
CC perinatal lethality and an accelerated aging phenotype, probably caused
CC by increased replication stress and impaired DNA caused repair
CC (PubMed:27225932). Females display reduced fertility and produce fewer
CC oocytes and ovulate fewer eggs (PubMed:31256246). Oocytes show impaired
CC meiotic progression with reduced levels of crossovers and chromosome
CC synapsis defects (PubMed:31256246). Mice also show severe osteopenia
CC characterized by decreased bone formation and an increase of
CC osteoclasts (PubMed:30026585). {ECO:0000269|PubMed:18239138,
CC ECO:0000269|PubMed:25200183, ECO:0000269|PubMed:27225932,
CC ECO:0000269|PubMed:30026585, ECO:0000269|PubMed:31256246}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class IV subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26403.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH26650.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY251540; AAP83960.1; -; mRNA.
DR EMBL; AL663030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026403; AAH26403.1; ALT_INIT; mRNA.
DR EMBL; BC026650; AAH26650.1; ALT_INIT; mRNA.
DR CCDS; CCDS49006.1; -.
DR RefSeq; NP_694696.2; NM_153056.2.
DR AlphaFoldDB; Q8BKJ9; -.
DR SMR; Q8BKJ9; -.
DR BioGRID; 229037; 5.
DR IntAct; Q8BKJ9; 1.
DR STRING; 10090.ENSMUSP00000079093; -.
DR PhosphoSitePlus; Q8BKJ9; -.
DR EPD; Q8BKJ9; -.
DR MaxQB; Q8BKJ9; -.
DR PaxDb; Q8BKJ9; -.
DR PeptideAtlas; Q8BKJ9; -.
DR PRIDE; Q8BKJ9; -.
DR ProteomicsDB; 261239; -.
DR Antibodypedia; 19848; 506 antibodies from 42 providers.
DR DNASU; 209011; -.
DR Ensembl; ENSMUST00000080202; ENSMUSP00000079093; ENSMUSG00000025138.
DR GeneID; 209011; -.
DR KEGG; mmu:209011; -.
DR UCSC; uc011yjf.1; mouse.
DR CTD; 51547; -.
DR MGI; MGI:2385849; Sirt7.
DR VEuPathDB; HostDB:ENSMUSG00000025138; -.
DR eggNOG; KOG1905; Eukaryota.
DR GeneTree; ENSGT00940000159703; -.
DR HOGENOM; CLU_023643_6_2_1; -.
DR InParanoid; Q8BKJ9; -.
DR OMA; HFGERGI; -.
DR OrthoDB; 1459156at2759; -.
DR PhylomeDB; Q8BKJ9; -.
DR TreeFam; TF106184; -.
DR BioGRID-ORCS; 209011; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Sirt7; mouse.
DR PRO; PR:Q8BKJ9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BKJ9; protein.
DR Bgee; ENSMUSG00000025138; Expressed in granulocyte and 252 other tissues.
DR ExpressionAtlas; Q8BKJ9; baseline and differential.
DR Genevisible; Q8BKJ9; MM.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005731; C:nucleolus organizer region; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0035861; C:site of double-strand break; IMP:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0097372; F:NAD-dependent histone deacetylase activity (H3-K18 specific); IMP:UniProtKB.
DR GO; GO:0034979; F:NAD-dependent protein deacetylase activity; IDA:UniProtKB.
DR GO; GO:0061697; F:protein-glutaryllysine deglutarylase activity; ISS:UniProtKB.
DR GO; GO:0106231; F:protein-propionyllysine depropionylase activity; IDA:UniProtKB.
DR GO; GO:0036055; F:protein-succinyllysine desuccinylase activity; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:1990258; P:histone glutamine methylation; ISS:UniProtKB.
DR GO; GO:0070932; P:histone H3 deacetylation; IMP:UniProtKB.
DR GO; GO:0016570; P:histone modification; ISS:UniProtKB.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0010529; P:negative regulation of transposition; IMP:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:UniProtKB.
DR GO; GO:0036049; P:peptidyl-lysine desuccinylation; ISS:UniProtKB.
DR GO; GO:2000234; P:positive regulation of rRNA processing; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0007072; P:positive regulation of transcription involved in exit from mitosis; ISS:UniProtKB.
DR GO; GO:0006476; P:protein deacetylation; IDA:UniProtKB.
DR GO; GO:0061698; P:protein deglutarylation; ISS:UniProtKB.
DR GO; GO:0106230; P:protein depropionylation; IDA:UniProtKB.
DR GO; GO:0062176; P:R-loop disassembly; ISS:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
DR GO; GO:0006111; P:regulation of gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0046825; P:regulation of protein export from nucleus; IMP:UniProtKB.
DR GO; GO:1901836; P:regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISS:UniProtKB.
DR GO; GO:0009303; P:rRNA transcription; ISS:UniProtKB.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF02146; SIR2; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Cytoplasm; DNA damage; DNA repair;
KW Metal-binding; Methylation; NAD; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation; Zinc.
FT CHAIN 1..402
FT /note="NAD-dependent protein deacetylase sirtuin-7"
FT /id="PRO_0000110272"
FT DOMAIN 91..332
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:18239138,
FT ECO:0000269|PubMed:30026585"
FT BINDING 108..127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT BINDING 168..171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 269..271
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT BINDING 298..300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT BINDING 316
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT MOD_RES 390
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NRC8"
FT MOD_RES 390
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9NRC8"
FT MUTAGEN 188
FT /note="H->Y: Abolishes deacylase and deacetylase
FT activities. Reduced interaction with SIRT1, without
FT abolishing it."
FT /evidence="ECO:0000269|PubMed:18239138,
FT ECO:0000269|PubMed:28923965, ECO:0000269|PubMed:30026585,
FT ECO:0000269|PubMed:31075303"
FT CONFLICT 95
FT /note="G -> R (in Ref. 1; AAP83960)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="M -> I (in Ref. 1; AAP83960)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="N -> S (in Ref. 1; AAP83960)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 45146 MW; AE43102816173958 CRC64;
MAAGGGLSRS ERKAAERVRR LREEQQRERL RQVSRILRKA AAERSAEEGR LLAESEDLVT
ELQGRSRRRE GLKRRQEEVC DDPEELRRKV RELAGAVRSA RHLVVYTGAG ISTAASIPDY
RGPNGVWTLL QKGRPVSAAD LSEAEPTLTH MSITRLHEQK LVQHVVSQNC DGLHLRSGLP
RTAISELHGN MYIEVCTSCI PNREYVRVFD VTERTALHRH LTGRTCHKCG TQLRDTIVHF
GERGTLGQPL NWEAATEAAS KADTILCLGS SLKVLKKYPR LWCMTKPPSR RPKLYIVNLQ
WTPKDDWAAL KLHGKCDDVM QLLMNELGLE IPVYNRWQDP IFSLATPLRA GEEGSHSRKS
LCRSREEAPP GDQSDPLASA PPILGGWFGR GCAKRAKRKK VA
