SIR1_ARATH
ID SIR1_ARATH Reviewed; 473 AA.
AC Q9FE17; Q7Y032;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=NAD-dependent protein deacetylase SRT1 {ECO:0000303|Ref.1};
DE EC=2.3.1.286 {ECO:0000255|PROSITE-ProRule:PRU00236};
DE AltName: Full=Regulatory protein SIR2 homolog 1 {ECO:0000303|Ref.1};
DE AltName: Full=SIR2-like protein 1 {ECO:0000303|Ref.1};
GN Name=SRT1 {ECO:0000303|Ref.1};
GN OrderedLocusNames=At5g55760 {ECO:0000312|Araport:AT5G55760};
GN ORFNames=MDF20.20 {ECO:0000312|EMBL:BAB09243.1};
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 [MRNA].
RC STRAIN=cv. Columbia;
RA Adachi Y., Oguchi K., Tamura K., Takahashi H.;
RT "Molecular cloning and characterization of sir2 homolog in Arabidopsis
RT thaliana.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH ENAP1.
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 deacetylase (By similarity). Has
CC deacetylase activity towards H3K9Ac (By similarity). May have a
CC function in the safeguard against genome instabiliy and DNA damage to
CC ensure plant cell growth (By similarity). Involved in responses to
CC ethylene leading to the transcriptional repression of some ethylene-
CC responsive genes via the regulation of histone acetylation H3K9Ac
CC (PubMed:29298835). {ECO:0000250|UniProtKB:P59941,
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|PROSITE-ProRule:PRU00236};
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 -!- SUBUNIT: Binds to the promoter region of genes influenced by ethylene
CC (By similarity). Interacts with ENAP1; this interaction is enhanced in
CC the presence of ethylene (PubMed:29298835).
CC {ECO:0000250|UniProtKB:Q94AQ6, ECO:0000269|PubMed:29298835}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P59941}.
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 IV subfamily.
CC {ECO:0000305}.
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DR EMBL; AF283757; AAG44850.1; -; mRNA.
DR EMBL; AB009050; BAB09243.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96677.1; -; Genomic_DNA.
DR EMBL; BT008767; AAP68206.1; -; mRNA.
DR EMBL; AK227432; BAE99436.1; -; mRNA.
DR RefSeq; NP_200387.1; NM_124958.3.
DR AlphaFoldDB; Q9FE17; -.
DR SMR; Q9FE17; -.
DR BioGRID; 20914; 1.
DR STRING; 3702.AT5G55760.1; -.
DR PaxDb; Q9FE17; -.
DR PRIDE; Q9FE17; -.
DR ProteomicsDB; 234564; -.
DR EnsemblPlants; AT5G55760.1; AT5G55760.1; AT5G55760.
DR GeneID; 835670; -.
DR Gramene; AT5G55760.1; AT5G55760.1; AT5G55760.
DR KEGG; ath:AT5G55760; -.
DR Araport; AT5G55760; -.
DR TAIR; locus:2162112; AT5G55760.
DR eggNOG; KOG1905; Eukaryota.
DR HOGENOM; CLU_023643_6_4_1; -.
DR InParanoid; Q9FE17; -.
DR OMA; HMDAIGC; -.
DR OrthoDB; 1503290at2759; -.
DR PhylomeDB; Q9FE17; -.
DR PRO; PR:Q9FE17; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FE17; baseline and differential.
DR Genevisible; Q9FE17; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:TAIR.
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:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IGI:TAIR.
DR GO; GO:0070932; P:histone H3 deacetylation; IBA:GO_Central.
DR GO; GO:0043970; P:histone H3-K9 acetylation; IGI:TAIR.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR Pfam; PF02146; SIR2; 2.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 1: Evidence at protein level;
KW Ethylene signaling pathway; Metal-binding; NAD; Nucleus;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1..473
FT /note="NAD-dependent protein deacetylase SRT1"
FT /id="PRO_0000417365"
FT DOMAIN 35..269
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT REGION 447..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 134
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 52..71
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT BINDING 114..117
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 209..211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT BINDING 235..237
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT BINDING 253
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9NXA8"
FT CONFLICT 14
FT /note="D -> G (in Ref. 4; AAP68206 and 5; BAE99436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 52642 MW; C265296654DE3E9D CRC64;
MSLGYAEKLS FIEDVGQVGM AEFFDPSHLL QCKIEELAKL IQKSKHLVVF TGAGISTSCG
IPDFRGPKGI WTLQREGKDL PKASLPFHRA MPSMTHMALV ELERAGILKF VISQNVDGLH
LRSGIPREKL SELHGDSFME MCPSCGAEYL RDFEVETIGL KETSRKCSVE KCGAKLKDTV
LDWEDALPPK EIDPAEKHCK KADLVLCLGT SLQITPACNL PLKCLKGGGK IVIVNLQKTP
KDKKANVVIH GLVDKVVAGV MESLNMKIPP YVRIDLFQII LTQSISGDQR FINWTLRVAS
VHGLTSQLPF IKSIEVSFSD NHNYKDAVLD KQPFLMKRRT ARNETFDIFF KVNYSDGCDC
VSTQLSLPFE FKISTEEHVE IIDKEAVLQS LREKAVEESS CGQSGVVERR VVSEPRSEAV
VYATVTSLRT YHSQQSLLAN GDLKWKLEGS GTSRKRSRTG KRKSKALAEE TKA
