WRK53_ARATH
ID WRK53_ARATH Reviewed; 324 AA.
AC Q9SUP6; Q0WSJ2;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Probable WRKY transcription factor 53 {ECO:0000303|PubMed:17369373};
DE AltName: Full=WRKY DNA-binding protein 53 {ECO:0000303|PubMed:17369373};
GN Name=WRKY53 {ECO:0000303|PubMed:17369373};
GN OrderedLocusNames=At4g23810 {ECO:0000312|Araport:AT4G23810};
GN ORFNames=F9D16.280 {ECO:0000312|EMBL:CAA23047.1};
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], AND INDUCTION.
RX PubMed=11449049; DOI=10.2307/3871384;
RA Yu D., Chen C., Chen Z.;
RT "Evidence for an important role of WRKY DNA binding proteins in the
RT regulation of NPR1 gene expression.";
RL Plant Cell 13:1527-1540(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA De Los Reyes C., Quan R., Chen H., Bautista V.R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=11506370; DOI=10.1007/s004250000512;
RA Hinderhofer K., Zentgraf U.;
RT "Identification of a transcription factor specifically expressed at the
RT onset of leaf senescence.";
RL Planta 213:469-473(2001).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH ESP, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=17369373; DOI=10.1105/tpc.106.042705;
RA Miao Y., Zentgraf U.;
RT "The antagonist function of Arabidopsis WRKY53 and ESR/ESP in leaf
RT senescence is modulated by the jasmonic and salicylic acid equilibrium.";
RL Plant Cell 19:819-830(2007).
RN [9]
RP FUNCTION, INTERACTION WITH UPL5, AND UBIQUITINATION.
RX PubMed=20409006; DOI=10.1111/j.1365-313x.2010.04233.x;
RA Miao Y., Zentgraf U.;
RT "A HECT E3 ubiquitin ligase negatively regulates Arabidopsis leaf
RT senescence through degradation of the transcription factor WRKY53.";
RL Plant J. 63:179-188(2010).
RN [10]
RP FUNCTION, INTERACTION WITH WRKY30, INDUCTION BY SALICYLIC ACID, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=22268143; DOI=10.1093/jxb/err450;
RA Besseau S., Li J., Palva E.T.;
RT "WRKY54 and WRKY70 co-operate as negative regulators of leaf senescence in
RT Arabidopsis thaliana.";
RL J. Exp. Bot. 63:2667-2679(2012).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY SALICYLIC ACID AND
RP PSEUDOMONAS SYRINGAE.
RC STRAIN=cv. Columbia;
RX PubMed=22325892; DOI=10.1016/j.plantsci.2011.12.003;
RA Hu Y., Dong Q., Yu D.;
RT "Arabidopsis WRKY46 coordinates with WRKY70 and WRKY53 in basal resistance
RT against pathogen Pseudomonas syringae.";
RL Plant Sci. 185:288-297(2012).
CC -!- FUNCTION: Transcription factor. Interacts specifically with the W box
CC (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-
CC acting element (PubMed:20409006). May regulate the early events of leaf
CC senescence (PubMed:17369373, PubMed:20409006). Negatively regulates the
CC expression of ESR/ESP (PubMed:20409006). Together with WRKY46 and
CC WRKY70, promotes resistance to P.syringae, probably by enhancing
CC salicylic acid (SA)- dependent genes. Contributes to the suppression of
CC jasmonic acid (MeJA)-induced expression of PDF1.2 (PubMed:22325892).
CC {ECO:0000269|PubMed:17369373, ECO:0000269|PubMed:20409006,
CC ECO:0000269|PubMed:22325892}.
CC -!- SUBUNIT: Interacts with ESR/ESP and UPL5 (PubMed:17369373,
CC PubMed:20409006). Binds to WRKY30 (PubMed:22268143).
CC {ECO:0000269|PubMed:17369373, ECO:0000269|PubMed:20409006,
CC ECO:0000269|PubMed:22268143}.
CC -!- INTERACTION:
CC Q9SUP6; P25854: CAM4; NbExp=2; IntAct=EBI-1235980, EBI-1235664;
CC Q9SUP6; Q03509: CAM6; NbExp=2; IntAct=EBI-1235980, EBI-1236097;
CC Q9SUP6; Q9S744: CML9; NbExp=2; IntAct=EBI-1235980, EBI-1236048;
CC Q9SUP6; Q8RY71: ESP; NbExp=6; IntAct=EBI-1235980, EBI-1997188;
CC Q9SUP6; Q39008: MEKK1; NbExp=5; IntAct=EBI-1235980, EBI-994439;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00223,
CC ECO:0000269|PubMed:17369373}.
CC -!- DEVELOPMENTAL STAGE: Accumulates during developmental leaf senescence.
CC {ECO:0000269|PubMed:22268143}.
CC -!- INDUCTION: By salicylic acid (SA) (PubMed:22268143, PubMed:22325892).
CC Strong accumulation during leaf senescence (PubMed:22268143). Down-
CC regulated by jasmonate. Triggered by P.syringae (PubMed:22325892).
CC {ECO:0000269|PubMed:11449049, ECO:0000269|PubMed:11506370,
CC ECO:0000269|PubMed:17369373, ECO:0000269|PubMed:22268143,
CC ECO:0000269|PubMed:22325892}.
CC -!- PTM: Ubiquitinated by UPL5. Ubiquitination leads to its subsequent
CC degradation, thus controlling the timing of leaf senescence.
CC {ECO:0000269|PubMed:20409006}.
CC -!- DISRUPTION PHENOTYPE: Retarded leaf senescence, but no effects on
CC pathogen resistance (PubMed:17369373). Increased susceptibility to
CC P.syringae associated with reduced PR1 induction; stronger symptoms in
CC double mutants wrky46 wrky70 and wrky46 wrky53, and triple mutant
CC wrky46 wrky70 wrky53. In these mutants, higher induction of PDF1.2 upon
CC jasmonic acid (MeJA) treatment (PubMed:22325892).
CC {ECO:0000269|PubMed:17369373, ECO:0000269|PubMed:22325892}.
CC -!- SIMILARITY: Belongs to the WRKY group III family. {ECO:0000305}.
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DR EMBL; AF272748; AAK28442.1; -; mRNA.
DR EMBL; AL035394; CAA23047.1; -; Genomic_DNA.
DR EMBL; AL161560; CAB81299.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84809.1; -; Genomic_DNA.
DR EMBL; AF370614; AAK43933.1; -; mRNA.
DR EMBL; BT033113; ACF20468.1; -; mRNA.
DR EMBL; AK227938; BAE99906.1; -; mRNA.
DR PIR; T05613; T05613.
DR RefSeq; NP_194112.1; NM_118512.3.
DR AlphaFoldDB; Q9SUP6; -.
DR SMR; Q9SUP6; -.
DR BioGRID; 13770; 17.
DR IntAct; Q9SUP6; 10.
DR STRING; 3702.AT4G23810.1; -.
DR iPTMnet; Q9SUP6; -.
DR PaxDb; Q9SUP6; -.
DR PRIDE; Q9SUP6; -.
DR ProteomicsDB; 234416; -.
DR EnsemblPlants; AT4G23810.1; AT4G23810.1; AT4G23810.
DR GeneID; 828481; -.
DR Gramene; AT4G23810.1; AT4G23810.1; AT4G23810.
DR KEGG; ath:AT4G23810; -.
DR Araport; AT4G23810; -.
DR TAIR; locus:2128514; AT4G23810.
DR eggNOG; ENOG502QPRM; Eukaryota.
DR HOGENOM; CLU_058534_0_0_1; -.
DR InParanoid; Q9SUP6; -.
DR OMA; FRNTQGC; -.
DR OrthoDB; 1331082at2759; -.
DR PhylomeDB; Q9SUP6; -.
DR PRO; PR:Q9SUP6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SUP6; baseline and differential.
DR Genevisible; Q9SUP6; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0031347; P:regulation of defense response; IMP:TAIR.
DR GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
DR GO; GO:0010193; P:response to ozone; IEP:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR Gene3D; 2.20.25.80; -; 1.
DR InterPro; IPR003657; WRKY_dom.
DR InterPro; IPR036576; WRKY_dom_sf.
DR InterPro; IPR044810; WRKY_plant.
DR PANTHER; PTHR32096; PTHR32096; 1.
DR Pfam; PF03106; WRKY; 1.
DR SMART; SM00774; WRKY; 1.
DR SUPFAM; SSF118290; SSF118290; 1.
DR PROSITE; PS50811; WRKY; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Jasmonic acid signaling pathway; Nucleus; Plant defense;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..324
FT /note="Probable WRKY transcription factor 53"
FT /id="PRO_0000133694"
FT DNA_BIND 152..220
FT /note="WRKY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT REGION 93..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 36273 MW; 017A5316B2C27578 CRC64;
MEGRDMLSWE QKTLLSELIN GFDAAKKLQA RLREAPSPSS SFSSPATAVA ETNEILVKQI
VSSYERSLLL LNWSSSPSVQ LIPTPVTVVP VANPGSVPES PASINGSPRS EEFADGGGSS
ESHHRQDYIF NSKKRKMLPK WSEKVRISPE RGLEGPQDDV FSWRKYGQKD ILGAKFPRSY
YRCTHRSTQN CWATKQVQRS DGDATVFEVT YRGTHTCSQA ITRTPPLASP EKRQDTRVKP
AITQKPKDIL ESLKSNLTVR TDGLDDGKDV FSFPDTPPFY NYGTINGEFG HVESSPIFDV
VDWFNPTVEI DTTFPAFLHE SIYY
