SIR1_ORYSI
ID SIR1_ORYSI Reviewed; 484 AA.
AC B8ARK7; Q9XGT1;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=NAD-dependent protein deacetylase SRT1;
DE EC=2.3.1.286;
DE AltName: Full=Regulatory protein SIR2 homolog 1;
DE AltName: Full=SIR2-like protein 1;
GN Name=SRT1; ORFNames=OsI_15145;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Anther;
RA Yau C.P., Zhuang C.X., Zee S.Y.;
RT "The first putative silent information regulatory protein (SIR2-like) in
RT plants.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17468215; DOI=10.1104/pp.107.099473;
RA Huang L., Sun Q., Qin F., Li C., Zhao Y., Zhou D.X.;
RT "Down-regulation of a SILENT INFORMATION REGULATOR2-related histone
RT deacetylase gene, OsSRT1, induces DNA fragmentation and cell death in
RT rice.";
RL Plant Physiol. 144:1508-1519(2007).
CC -!- FUNCTION: NAD-dependent protein deacetylase. Has deacetylase activity
CC towards H3K9Ac. May have a function in the safeguard against genome
CC instabiliy and DNA damage to ensure plant cell growth.
CC {ECO:0000269|PubMed:17468215}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17468215}.
CC -!- DISRUPTION PHENOTYPE: Enhances histone H3K9 acetylation on transposable
CC elements and promoters of hypersensitive response (HR)-related genes.
CC This leads to increased HR-related gene expression, hydrogen peroxide
CC production, DNA fragmentation, and programmed cell death.
CC {ECO:0000269|PubMed:17468215}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class IV subfamily.
CC {ECO:0000305}.
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DR EMBL; AF159133; AAD42226.1; -; mRNA.
DR EMBL; CM000129; EEC76908.1; -; Genomic_DNA.
DR AlphaFoldDB; B8ARK7; -.
DR SMR; B8ARK7; -.
DR STRING; 39946.B8ARK7; -.
DR EnsemblPlants; BGIOSGA015454-TA; BGIOSGA015454-PA; BGIOSGA015454.
DR Gramene; BGIOSGA015454-TA; BGIOSGA015454-PA; BGIOSGA015454.
DR HOGENOM; CLU_023643_6_4_1; -.
DR OMA; HMDAIGC; -.
DR Proteomes; UP000007015; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:EnsemblPlants.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0033558; F:protein lysine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:EnsemblPlants.
DR GO; GO:0043970; P:histone H3-K9 acetylation; IEA:EnsemblPlants.
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 2: Evidence at transcript level;
KW Metal-binding; NAD; Nucleus; Reference proteome; Transferase; Zinc.
FT CHAIN 1..484
FT /note="NAD-dependent protein deacetylase SRT1"
FT /id="PRO_0000417366"
FT DOMAIN 35..270
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT ACT_SITE 135
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"
FT BINDING 115..118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00236"
FT BINDING 210..212
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 236..238
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 54
FT /note="G -> S (in Ref. 1; AAD42226)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="Missing (in Ref. 1; AAD42226)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="S -> T (in Ref. 1; AAD42226)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="H -> Q (in Ref. 1; AAD42226)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="T -> N (in Ref. 1; AAD42226)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 53968 MW; D79F87086C43DEC6 CRC64;
MSLGYAEKLS YREDVGNVGM PEIFDSPELL HKKIEELAVM VRESKHLVVF TGAGISTSSG
IPDFRGPKGV WTLQVRSGKG VPGASLPFHR AVPTLTHMAL VELEKTGRLK FVISQNVDSL
HLRSGLPREK LAELHGNSFK EICPSCKKEY LRDFEIETIG LKDTPRRCSD KNCGARLKDT
VLDWEDALPP EEMDAAKEQC QTADLVLCLG TSLQITPACN MPLLSLKNGG RVAIVNLQAT
PKDKKASLVI HGLVDKVIAG VMYMMNLRIP PYIRTDFVQI SLRNSVKKKC VRWTLRVTSI
HGLRAPLPFL RSVEVSFPER PDMKPVVLKE QPFSLQRETS MNRPFVMLLT FNFSDGCGCS
SSSIEWPVDF LKQKDSFVRD RSLVLQELQH AAEHRSRAGQ HAILEREGVP RAETSIHALV
TNIVRYDTED SKAAVPMATW MNSNGSLSKR HMDAIGCNPA SSKKQKLVAT RHRRKGLNPA
TQKV
