SIR42_CAEEL
ID SIR42_CAEEL Reviewed; 287 AA.
AC Q20481;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=NAD-dependent protein deacylase sir-2.3 {ECO:0000255|HAMAP-Rule:MF_03161};
DE EC=2.3.1.286 {ECO:0000255|HAMAP-Rule:MF_03161};
DE AltName: Full=Regulatory protein SIR2 homolog 3 {ECO:0000255|HAMAP-Rule:MF_03161};
GN Name=sir-2.3; ORFNames=F46G10.3;
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).
RN [2]
RP FUNCTION, INTERACTION WITH PYC-1; PCCA-1 AND MCCC-1, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=23438705; DOI=10.1016/j.mito.2013.02.002;
RA Wirth M., Karaca S., Wenzel D., Ho L., Tishkoff D., Lombard D.B.,
RA Verdin E., Urlaub H., Jedrusik-Bode M., Fischle W.;
RT "Mitochondrial SIRT4-type proteins in Caenorhabditis elegans and mammals
RT interact with pyruvate carboxylase and other acetylated biotin-dependent
RT carboxylases.";
RL Mitochondrion 13:705-720(2013).
RN [3]
RP FUNCTION.
RX PubMed=28820880; DOI=10.1371/journal.pgen.1006965;
RA Sangaletti R., D'Amico M., Grant J., Della-Morte D., Bianchi L.;
RT "Knock-out of a mitochondrial sirtuin protects neurons from degeneration in
RT Caenorhabditis elegans.";
RL PLoS Genet. 13:E1006965-E1006965(2017).
CC -!- FUNCTION: NAD-dependent protein deacylase. Catalyzes the NAD-dependent
CC hydrolysis of acyl groups from lysine residues. Plays a role in
CC oxidative stress resistance (PubMed:23438705). Might promote neuronal
CC cell death under ischemic conditions and cell death in touch neurons
CC induced by mec-4 channel hyperactivation, possibly downstream of the
CC insulin-like receptor daf-2 (PubMed:28820880). Might attenuate the
CC reactive oxygen species (ROS) scavenging system, that eliminates ROS in
CC ischemic conditions, under dietary deprivation and when glycolysis is
CC blocked (PubMed:28820880). {ECO:0000255|HAMAP-Rule:MF_03161,
CC ECO:0000269|PubMed:23438705, ECO:0000269|PubMed:28820880}.
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|HAMAP-Rule:MF_03161};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03161};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03161};
CC -!- SUBUNIT: Interacts with pyc-1, pcca-1 and mccc-1.
CC {ECO:0000269|PubMed:23438705}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03161}. Mitochondrion {ECO:0000269|PubMed:23438705}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with high expression in the
CC pharynx, body wall muscles and gonad. Strong expression in a subset of
CC non-neuronal cells in the head. {ECO:0000269|PubMed:23438705}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at the 100 cell stage during
CC embryogenesis and is expressed throughout development until adulthood.
CC {ECO:0000269|PubMed:23438705}.
CC -!- MISCELLANEOUS: This protein may be expected to contain an N-terminal
CC transit peptide but none has been predicted. {ECO:0000255|HAMAP-
CC Rule:MF_03161}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class II subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03161}.
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DR EMBL; Z50177; CAA90547.1; -; Genomic_DNA.
DR PIR; T22325; T22325.
DR RefSeq; NP_510220.1; NM_077819.1.
DR AlphaFoldDB; Q20481; -.
DR SMR; Q20481; -.
DR BioGRID; 50633; 3.
DR STRING; 6239.F46G10.3; -.
DR PaxDb; Q20481; -.
DR EnsemblMetazoa; F46G10.3.1; F46G10.3.1; WBGene00004802.
DR EnsemblMetazoa; F46G10.3.2; F46G10.3.2; WBGene00004802.
DR GeneID; 185876; -.
DR KEGG; cel:CELE_F46G10.3; -.
DR UCSC; F46G10.3; c. elegans.
DR CTD; 185876; -.
DR WormBase; F46G10.3; CE02239; WBGene00004802; sir-2.3.
DR eggNOG; KOG2683; Eukaryota.
DR GeneTree; ENSGT00940000158891; -.
DR HOGENOM; CLU_023643_3_2_1; -.
DR InParanoid; Q20481; -.
DR OMA; KINSRCG; -.
DR OrthoDB; 1407693at2759; -.
DR PhylomeDB; Q20481; -.
DR PRO; PR:Q20481; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00004802; Expressed in embryo and 2 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0019213; F:deacetylase activity; IBA:GO_Central.
DR GO; GO:0070403; F:NAD+ binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034979; F:NAD-dependent protein deacetylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006471; P:protein ADP-ribosylation; IEA:UniProtKB-UniRule.
DR GO; GO:0006476; P:protein deacetylation; IBA:GO_Central.
DR Gene3D; 3.30.1600.10; -; 1.
DR HAMAP; MF_01967; Sirtuin_ClassII; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR026587; Sirtuin_class_II.
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 Metal-binding; Mitochondrion; NAD; Reference proteome; Transferase; Zinc.
FT CHAIN 1..287
FT /note="NAD-dependent protein deacylase sir-2.3"
FT /id="PRO_0000417346"
FT DOMAIN 18..287
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 35..55
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 116..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 236..238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 262..264
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 280
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
SQ SEQUENCE 287 AA; 32464 MW; 7DF9054E25A9126F CRC64;
MARKYVPHTT ELCENSLKKF KSLVGTVDKL LIITGAGIST ESGIPDYRSK DVGLYTKTAL
EPIYFQDFMK SKKCRQRYWS RSYLNWPRFA QALPNFNHYA LSKWEAANKF HWLITQNVDG
LHLKAGSKMI TELHGNALQV KCTSCEYIET RQTYQDRLNY ANPGFKEQFV SPGQQELDAD
TALPLGSEQG FKIPECLNCG GLMKTDVTLF GENLNTDKIK VCGKKVNECN GVLTLGTSLE
VLSGYQIVNH AHMQNKPIFI VNIGPTRADQ MATMKLDYRI SDVLKEM
