ID Q4FJK3_MOUSE Unreviewed; 257 AA. AC Q4FJK3; DT 30-AUG-2005, integrated into UniProtKB/TrEMBL. DT 30-AUG-2005, sequence version 1. DT 27-MAR-2024, entry version 131. DE RecName: Full=NAD-dependent protein deacetylase {ECO:0000256|PIRNR:PIRNR037938}; DE EC=2.3.1.286 {ECO:0000256|PIRNR:PIRNR037938}; GN Name=Sirt3 {ECO:0000313|MGI:MGI:1927665}; 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 {ECO:0000313|EMBL:CAJ18608.1}; RN [1] {ECO:0000313|EMBL:CAJ18608.1} RP NUCLEOTIDE SEQUENCE. RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., RA Wiemann S., Schick M., Korn B.; RT "Cloning of mouse full open reading frames in Gateway(R) system entry RT vector (pDONR201)."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: NAD-dependent protein deacetylase. CC {ECO:0000256|PIRNR:PIRNR037938}. 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:0000256|PIRNR:PIRNR037938}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|PIRSR:PIRSR037938-3}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037938-3}; CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily. CC {ECO:0000256|PIRNR:PIRNR037938}. 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; CT010402; CAJ18608.1; -; mRNA. DR RefSeq; NP_001120823.1; NM_001127351.1. DR RefSeq; NP_071878.2; NM_022433.2. DR AlphaFoldDB; Q4FJK3; -. DR SMR; Q4FJK3; -. DR Antibodypedia; 9472; 875 antibodies from 47 providers. DR DNASU; 64384; -. DR GeneID; 64384; -. DR AGR; MGI:1927665; -. DR CTD; 23410; -. DR MGI; MGI:1927665; Sirt3. DR VEuPathDB; HostDB:ENSMUSG00000025486; -. DR OMA; PYCQVPD; -. DR OrthoDB; 10545at2759; -. DR BioGRID-ORCS; 64384; 3 hits in 80 CRISPR screens. DR ChiTaRS; Sirt3; mouse. DR ExpressionAtlas; Q4FJK3; baseline and differential. DR GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-UniRule. DR GO; GO:0017136; F:NAD-dependent histone deacetylase activity; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR CDD; cd01408; SIRT1; 1. DR Gene3D; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 1. DR Gene3D; 3.40.50.1220; TPP-binding domain; 1. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR003000; Sirtuin. DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf. DR InterPro; IPR017328; Sirtuin_class_I. DR InterPro; IPR026590; Ssirtuin_cat_dom. DR PANTHER; PTHR11085:SF15; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-3, MITOCHONDRIAL; 1. DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1. DR Pfam; PF02146; SIR2; 1. DR PIRSF; PIRSF037938; SIR2_euk; 1. DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1. DR PROSITE; PS50305; SIRTUIN; 1. PE 2: Evidence at transcript level; KW Metal-binding {ECO:0000256|PIRNR:PIRNR037938, KW ECO:0000256|PIRSR:PIRSR037938-3}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR037938}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037938}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR037938}. FT DOMAIN 1..238 FT /note="Deacetylase sirtuin-type" FT /evidence="ECO:0000259|PROSITE:PS50305" FT ACT_SITE 106 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR037938-1, FT ECO:0000256|PROSITE-ProRule:PRU00236" FT BINDING 4..8 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2" FT BINDING 14..16 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2" FT BINDING 86..89 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2" FT BINDING 114 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR037938-3, FT ECO:0000256|PROSITE-ProRule:PRU00236" FT BINDING 117 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR037938-3, FT ECO:0000256|PROSITE-ProRule:PRU00236" FT BINDING 138 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR037938-3, FT ECO:0000256|PROSITE-ProRule:PRU00236" FT BINDING 141 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR037938-3, FT ECO:0000256|PROSITE-ProRule:PRU00236" FT BINDING 178..179 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2" FT BINDING 202..204 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2" SQ SEQUENCE 257 AA; 28822 MW; F756041FBC9B985E CRC64; MVGAGISTPS GIPDFRSPGS GLYSNLQQYD IPYPEAIFEL GFFFHNPKPF FMLAKELYPG HYRPNVTHYF LRLLHDKELL LRLYTQNIDG LERASGIPAS KLVEAHGTFV TATCTVCRRS FPGEDIWADV MADRVPRCPV CTGVVKPDIV FFGEQLPARF LLHMADFALA DLLLILGTSL EVEPFASLSE AVQKSVPRLL INRDLVGPFV LSPRRKDVVQ LGDVVHGVER LVDLLGWTQE LLDLMQRERG KLDGQDR //