SIR4_ARATH
ID SIR4_ARATH Reviewed; 373 AA.
AC Q94AQ6; B9DFU7; F4KCI0; Q9FY91;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=NAD-dependent protein deacylase SRT2 {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 2 {ECO:0000255|HAMAP-Rule:MF_03161};
DE Flags: Precursor;
GN Name=SRT2 {ECO:0000303|PubMed:20573705};
GN OrderedLocusNames=At5g09230 {ECO:0000312|Araport:AT5G09230};
GN ORFNames=T5E8_30 {ECO:0000312|EMBL:CAC05449.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=20573705; DOI=10.1093/pcp/pcq087;
RA Wang C., Gao F., Wu J., Dai J., Wei C., Li Y.;
RT "Arabidopsis putative deacetylase AtSRT2 regulates basal defense by
RT suppressing PAD4, EDS5 and SID2 expression.";
RL Plant Cell Physiol. 51:1291-1299(2010).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ENAP1, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=29298835; DOI=10.1105/tpc.17.00671;
RA Zhang F., Wang L., Ko E.E., Shao K., Qiao H.;
RT "Histone deacetylases SRT1 and SRT2 interact with ENAP1 to mediate
RT ethylene-induced transcriptional repression.";
RL Plant Cell 30:153-166(2018).
CC -!- FUNCTION: NAD-dependent protein deacylase. Catalyzes the NAD-dependent
CC hydrolysis of acyl groups from lysine residues (By similarity).
CC Involved in responses to ethylene leading to the transcriptional
CC repression of some ethylene-responsive genes via the regulation of
CC histone acetylation H3K9Ac (PubMed:29298835). Negatively regulates
CC plant basal defense against plant pathogens, possibly by suppressing
CC salicylic acid biosynthesis (PubMed:20573705). {ECO:0000255|HAMAP-
CC Rule:MF_03161, ECO:0000269|PubMed:20573705,
CC ECO:0000269|PubMed:29298835}.
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: Binds to the promoter region of genes influenced by ethylene
CC (PubMed:29298835). Interacts with ENAP1; this interaction is enhanced
CC in the presence of ethylene (PubMed:29298835).
CC {ECO:0000269|PubMed:29298835}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-
CC Rule:MF_03161}. Nucleus {ECO:0000269|PubMed:20573705}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q94AQ6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q94AQ6-2; Sequence=VSP_043537;
CC Name=3;
CC IsoId=Q94AQ6-3; Sequence=VSP_043536;
CC -!- INDUCTION: Repressed by pathogen infection.
CC {ECO:0000269|PubMed:20573705}.
CC -!- DISRUPTION PHENOTYPE: Reduced ethylene sensitivity in the double mutant
CC srt1 srt2. {ECO:0000269|PubMed:29298835}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class II subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03161}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC05449.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391712; CAC05449.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91355.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91356.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91358.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91360.1; -; Genomic_DNA.
DR EMBL; AY045873; AAK76547.1; -; mRNA.
DR EMBL; AY122995; AAM67528.1; -; mRNA.
DR EMBL; AK316908; BAH19614.1; -; mRNA.
DR RefSeq; NP_001078550.1; NM_001085081.2. [Q94AQ6-2]
DR RefSeq; NP_568207.1; NM_120959.4. [Q94AQ6-1]
DR RefSeq; NP_850795.1; NM_180464.4. [Q94AQ6-1]
DR RefSeq; NP_974753.1; NM_203024.3. [Q94AQ6-3]
DR AlphaFoldDB; Q94AQ6; -.
DR SMR; Q94AQ6; -.
DR BioGRID; 16060; 15.
DR STRING; 3702.AT5G09230.7; -.
DR PaxDb; Q94AQ6; -.
DR ProteomicsDB; 234565; -. [Q94AQ6-1]
DR EnsemblPlants; AT5G09230.1; AT5G09230.1; AT5G09230. [Q94AQ6-1]
DR EnsemblPlants; AT5G09230.2; AT5G09230.2; AT5G09230. [Q94AQ6-1]
DR EnsemblPlants; AT5G09230.5; AT5G09230.5; AT5G09230. [Q94AQ6-3]
DR EnsemblPlants; AT5G09230.7; AT5G09230.7; AT5G09230. [Q94AQ6-2]
DR GeneID; 830782; -.
DR Gramene; AT5G09230.1; AT5G09230.1; AT5G09230. [Q94AQ6-1]
DR Gramene; AT5G09230.2; AT5G09230.2; AT5G09230. [Q94AQ6-1]
DR Gramene; AT5G09230.5; AT5G09230.5; AT5G09230. [Q94AQ6-3]
DR Gramene; AT5G09230.7; AT5G09230.7; AT5G09230. [Q94AQ6-2]
DR KEGG; ath:AT5G09230; -.
DR Araport; AT5G09230; -.
DR TAIR; locus:2184717; AT5G09230.
DR eggNOG; KOG2683; Eukaryota.
DR InParanoid; Q94AQ6; -.
DR OMA; RRHYWAR; -.
DR OrthoDB; 1407693at2759; -.
DR PhylomeDB; Q94AQ6; -.
DR PRO; PR:Q94AQ6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q94AQ6; baseline and differential.
DR Genevisible; Q94AQ6; AT.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0019213; F:deacetylase activity; IDA:TAIR.
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:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IGI:TAIR.
DR GO; GO:0043970; P:histone H3-K9 acetylation; IGI:TAIR.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
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 Alternative splicing; Ethylene signaling pathway; Metal-binding;
KW Mitochondrion; NAD; Nucleus; Reference proteome; Transferase;
KW Transit peptide; Zinc.
FT TRANSIT 1..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT CHAIN 48..373
FT /note="NAD-dependent protein deacylase SRT2"
FT /id="PRO_0000417348"
FT DOMAIN 83..371
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 100..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 179..182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 311..313
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 337..339
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT BINDING 355
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03161"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_043536"
FT VAR_SEQ 1
FT /note="M -> MLSM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_043537"
SQ SEQUENCE 373 AA; 41536 MW; 6DD937F4237A5A43 CRC64;
MNMRRVFGGV STDLFPSRSM YRPLQSGGNL VMLFKGCRRF VRTTCRVSIP GGSLGNESKA
PPRFLRDRKI VPDADPPNME DIHKLYRLFE QSSRLTILTG AGVSTECGIP DYRSPNGAYS
SGFKPITHQE FTRSSRARRR YWARSYAGWR RFTAAQPGPA HTALASLEKA GRINFMITQN
VDRLHHRAGS DPLELHGTVY TVMCLECGFS FPRDLFQDQL KAINPKWAEA IESIDHGDPG
SEKSFGMKQR PDGDIEIDEK FWEEGFHIPV CEKCKGVLKP DVIFFGDNIP KERATQAMEV
AKQSDAFLVL GSSLMTMSAF RLCRAAHEAG AMTAIVNIGE TRADDIVPLK INARVGEILH
RVLDVGSLSV PAL
