SIR24_CAEEL
ID SIR24_CAEEL Reviewed; 292 AA.
AC Q95Q89;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=NAD-dependent protein deacetylase sir-2.4;
DE EC=2.3.1.286;
DE AltName: Full=Regulatory protein SIR2 homolog 4;
DE AltName: Full=SIR2-like protein 4;
GN Name=sir-2.4; ORFNames=C06A5.11;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: NAD-dependent protein deacetylase. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the sirtuin family. Class IV subfamily.
CC {ECO:0000305}.
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DR EMBL; FO080102; CCD61225.1; -; Genomic_DNA.
DR RefSeq; NP_491733.2; NM_059332.2.
DR AlphaFoldDB; Q95Q89; -.
DR SMR; Q95Q89; -.
DR BioGRID; 47141; 3.
DR STRING; 6239.C06A5.11; -.
DR EPD; Q95Q89; -.
DR PaxDb; Q95Q89; -.
DR PeptideAtlas; Q95Q89; -.
DR EnsemblMetazoa; C06A5.11a.1; C06A5.11a.1; WBGene00004803.
DR GeneID; 182284; -.
DR KEGG; cel:CELE_C06A5.11; -.
DR UCSC; C06A5.11; c. elegans.
DR CTD; 182284; -.
DR WormBase; C06A5.11a; CE45549; WBGene00004803; sir-2.4.
DR eggNOG; KOG1905; Eukaryota.
DR GeneTree; ENSGT00940000160088; -.
DR HOGENOM; CLU_023643_6_0_1; -.
DR InParanoid; Q95Q89; -.
DR OMA; EQCKKCR; -.
DR OrthoDB; 1503290at2759; -.
DR PhylomeDB; Q95Q89; -.
DR Reactome; R-CEL-5693607; Processing of DNA double-strand break ends.
DR PRO; PR:Q95Q89; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004803; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:WormBase.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0005643; C:nuclear pore; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IDA:WormBase.
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:0046969; F:NAD-dependent histone deacetylase activity (H3-K9 specific); IBA:GO_Central.
DR GO; GO:0034979; F:NAD-dependent protein deacetylase activity; ISS:WormBase.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0008134; F:transcription factor binding; IPI:WormBase.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0070932; P:histone H3 deacetylation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:1903863; P:P granule assembly; IMP:WormBase.
DR GO; GO:0006476; P:protein deacetylation; ISS:WormBase.
DR GO; GO:0009408; P:response to heat; IMP:WormBase.
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 3: Inferred from homology;
KW Metal-binding; NAD; Reference proteome; Transferase; Zinc.
FT CHAIN 1..292
FT /note="NAD-dependent protein deacetylase sir-2.4"
FT /id="PRO_0000417364"
FT DOMAIN 35..276
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT ACT_SITE 136
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 56..75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 116..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 216..218
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 242..244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 292 AA; 32217 MW; 1B67386B8BFCA429 CRC64;
MTSVYESLLS DYPDKGVIGK PEIRDTETEI IEKLRTLYNH FVQAKQTGKP IFVLIGAGVS
TGSKLPDFRG KQGVWTLQAE GKHAEGVDFQ VARPGVSHKS ILALHKAGYI KTIITQNVDG
LDRKVGIPVE DLIEVHGNLF LEVCQSCFSE YVREEIVMSV GLCPTGRNCE GNKRTGRSCR
GKLRDATLDW DTEISLNHLD RIRKAWKQTS HLLCIGTSLE IIPMGSLPLD AKSKGIKTTT
INYQETAHEK IVETAIHADV KLILYSLCNA LGVNVDLGDD LPDEVPIPLK IS
