WRK20_ARATH
ID WRK20_ARATH Reviewed; 557 AA.
AC Q93WV0; Q8H1E9; Q94AP6; Q9SUA0;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Probable WRKY transcription factor 20;
DE AltName: Full=WRKY DNA-binding protein 20;
GN Name=WRKY20; OrderedLocusNames=At4g26640; ORFNames=T15N24.90;
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] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Flower;
RA Ulker B., Kushnir S., Somssich I.E.;
RT "Arabidopsis thaliana transcription factor WRKY20.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORM 2).
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).
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. {ECO:0000250|UniProtKB:Q9SI37}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9SI37}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q93WV0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q93WV0-2; Sequence=VSP_007247, VSP_007248;
CC -!- SIMILARITY: Belongs to the WRKY group I family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB43860.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79519.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF425837; AAL13050.1; -; mRNA.
DR EMBL; AL078465; CAB43860.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161565; CAB79519.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85230.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85231.1; -; Genomic_DNA.
DR EMBL; AY045892; AAK76566.1; -; mRNA.
DR EMBL; AY150436; AAN12978.1; -; mRNA.
DR PIR; T08930; T08930.
DR RefSeq; NP_567752.1; NM_118798.2. [Q93WV0-2]
DR RefSeq; NP_849450.1; NM_179119.5. [Q93WV0-1]
DR AlphaFoldDB; Q93WV0; -.
DR SMR; Q93WV0; -.
DR BioGRID; 14058; 14.
DR IntAct; Q93WV0; 13.
DR STRING; 3702.AT4G26640.2; -.
DR iPTMnet; Q93WV0; -.
DR PaxDb; Q93WV0; -.
DR PRIDE; Q93WV0; -.
DR ProteomicsDB; 232453; -. [Q93WV0-1]
DR EnsemblPlants; AT4G26640.1; AT4G26640.1; AT4G26640. [Q93WV0-2]
DR EnsemblPlants; AT4G26640.2; AT4G26640.2; AT4G26640. [Q93WV0-1]
DR GeneID; 828771; -.
DR Gramene; AT4G26640.1; AT4G26640.1; AT4G26640. [Q93WV0-2]
DR Gramene; AT4G26640.2; AT4G26640.2; AT4G26640. [Q93WV0-1]
DR KEGG; ath:AT4G26640; -.
DR Araport; AT4G26640; -.
DR TAIR; locus:2133852; AT4G26640.
DR eggNOG; ENOG502QRXJ; Eukaryota.
DR HOGENOM; CLU_012086_4_1_1; -.
DR InParanoid; Q93WV0; -.
DR OMA; MSIQVER; -.
DR PhylomeDB; Q93WV0; -.
DR PRO; PR:Q93WV0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93WV0; baseline and differential.
DR Genevisible; Q93WV0; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0009961; P:response to 1-aminocyclopropane-1-carboxylic acid; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR Gene3D; 2.20.25.80; -; 2.
DR InterPro; IPR003657; WRKY_dom.
DR InterPro; IPR036576; WRKY_dom_sf.
DR InterPro; IPR044810; WRKY_plant.
DR PANTHER; PTHR31221; PTHR31221; 1.
DR Pfam; PF03106; WRKY; 2.
DR SMART; SM00774; WRKY; 2.
DR SUPFAM; SSF118290; SSF118290; 2.
DR PROSITE; PS50811; WRKY; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..557
FT /note="Probable WRKY transcription factor 20"
FT /id="PRO_0000133662"
FT DNA_BIND 205..269
FT /note="WRKY 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT DNA_BIND 375..440
FT /note="WRKY 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 437
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT VAR_SEQ 1..72
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_007247"
FT VAR_SEQ 73..76
FT /note="SNIK -> MILL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_007248"
FT CONFLICT 108
FT /note="Q -> R (in Ref. 4; AAK76566)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 61034 MW; 6179384AA4CEF0D9 CRC64;
MNPQANDRKE FQGDCSATGD LTAKHDSAGG NGGGGARYKL MSPAKLPISR STDITIPPGL
SPTSFLESPV FISNIKPEPS PTTGSLFKPR PVHISASSSS YTGRGFHQNT FTEQKSSEFE
FRPPASNMVY AELGKIRSEP PVHFQGQGHG SSHSPSSISD AAGSSSELSR PTPPCQMTPT
SSDIPAGSDQ EESIQTSQND SRGSTPSILA DDGYNWRKYG QKHVKGSEFP RSYYKCTHPN
CEVKKLFERS HDGQITDIIY KGTHDHPKPQ PGRRNSGGMA AQEERLDKYP SSTGRDEKGS
GVYNLSNPNE QTGNPEVPPI SASDDGGEAA ASNRNKDEPD DDDPFSKRRR MEGAMEITPL
VKPIREPRVV VQTLSEVDIL DDGYRWRKYG QKVVRGNPNP RSYYKCTAHG CPVRKHVERA
SHDPKAVITT YEGKHDHDVP TSKSSSNHEI QPRFRPDETD TISLNLGVGI SSDGPNHASN
EHQHQNQQLV NQTHPNGVNF RFVHASPMSS YYASLNSGMN QYGQRETKNE TQNGDISSLN
NSSYPYPPNM GRVQSGP
