WRKY4_ARATH
ID WRKY4_ARATH Reviewed; 514 AA.
AC Q9XI90; Q93WN8; Q9LMG1;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable WRKY transcription factor 4;
DE AltName: Full=WRKY DNA-binding protein 4;
GN Name=WRKY4; OrderedLocusNames=At1g13960; ORFNames=F16A14.18, F7A19.5;
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 2), 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 [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Flower;
RA Ulker B., Kushnir S., Somssich I.E.;
RT "Arabidopsis thaliana transcription factor WRKY4.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
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 [6]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11722756; DOI=10.1046/j.1365-313x.2001.01131.x;
RA Robatzek S., Somssich I.E.;
RT "A new member of the Arabidopsis WRKY transcription factor family, AtWRKY6,
RT is associated with both senescence- and defence-related processes.";
RL Plant J. 28:123-133(2001).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INDUCTION BY
RP BIOTIC AND ABIOTIC STRESSES.
RX PubMed=18570649; DOI=10.1186/1471-2229-8-68;
RA Lai Z., Vinod K., Zheng Z., Fan B., Chen Z.;
RT "Roles of Arabidopsis WRKY3 and WRKY4 transcription factors in plant
RT responses to pathogens.";
RL BMC Plant Biol. 8:68-68(2008).
RN [8]
RP STRUCTURE BY NMR OF 399-469 IN COMPLEX WITH ZINC, AND DNA BINDING.
RX PubMed=15705956; DOI=10.1105/tpc.104.026435;
RA Yamasaki K., Kigawa T., Inoue M., Tateno M., Yamasaki T., Yabuki T.,
RA Aoki M., Seki E., Matsuda T., Tomo Y., Hayami N., Terada T., Shirouzu M.,
RA Tanaka A., Seki M., Shinozaki K., Yokoyama S.;
RT "Solution structure of an Arabidopsis WRKY DNA binding domain.";
RL Plant Cell 17:944-956(2005).
RN [9]
RP STRUCTURE BY NMR OF 399-469 IN COMPLEX WITH ZINC AND W-BOX DNA, DNA
RP BINDING, AND FUNCTION.
RX PubMed=22219184; DOI=10.1074/jbc.m111.279844;
RA Yamasaki K., Kigawa T., Watanabe S., Inoue M., Yamasaki T., Seki M.,
RA Shinozaki K., Yokoyama S.;
RT "Structural basis for sequence-specific DNA recognition by an Arabidopsis
RT WRKY transcription factor.";
RL J. Biol. Chem. 287:7683-7691(2012).
CC -!- FUNCTION: Transcription factor that binds specifically to the W box
CC (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-
CC acting element. Has a positive role in resistance to necrotrophic
CC pathogens (e.g. Botrytis cinerea), but a negative effect on plant
CC resistance to biotrophic pathogens (e.g. Pseudomonas syringae).
CC {ECO:0000269|PubMed:18570649, ECO:0000269|PubMed:22219184}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00223,
CC ECO:0000269|PubMed:18570649}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9XI90-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9XI90-2; Sequence=VSP_008969;
CC -!- TISSUE SPECIFICITY: In young, mature and senescent leaves.
CC {ECO:0000269|PubMed:11722756}.
CC -!- INDUCTION: By biotic and abiotic stresses such as pathogen infection
CC (e.g. Botrytis cinerea and Pseudomonas syringae), salicylic acid (SA),
CC jasmonic acid (JA), ethylene (ACC), liquid infiltration or spraying,
CC and strongly during leaf senescence. {ECO:0000269|PubMed:11449049,
CC ECO:0000269|PubMed:11722756, ECO:0000269|PubMed:18570649}.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to the necrotrophic fungal
CC pathogen Botrytis cinerea. {ECO:0000269|PubMed:18570649}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD39282.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF79402.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF224703; AAK28313.1; -; mRNA.
DR EMBL; AF425835; AAL13048.1; -; mRNA.
DR EMBL; AC007576; AAD39282.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC068197; AAF79402.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29089.1; -; Genomic_DNA.
DR EMBL; AY045676; AAK74034.1; -; mRNA.
DR EMBL; BT002629; AAO11545.1; -; mRNA.
DR PIR; G86272; G86272.
DR RefSeq; NP_172849.1; NM_101262.3. [Q9XI90-1]
DR PDB; 1WJ2; NMR; -; A=399-469.
DR PDB; 2LEX; NMR; -; A=399-469.
DR PDBsum; 1WJ2; -.
DR PDBsum; 2LEX; -.
DR AlphaFoldDB; Q9XI90; -.
DR SMR; Q9XI90; -.
DR BioGRID; 23196; 1.
DR STRING; 3702.AT1G13960.1; -.
DR iPTMnet; Q9XI90; -.
DR PaxDb; Q9XI90; -.
DR PRIDE; Q9XI90; -.
DR ProteomicsDB; 234293; -. [Q9XI90-1]
DR EnsemblPlants; AT1G13960.1; AT1G13960.1; AT1G13960. [Q9XI90-1]
DR GeneID; 837956; -.
DR Gramene; AT1G13960.1; AT1G13960.1; AT1G13960. [Q9XI90-1]
DR KEGG; ath:AT1G13960; -.
DR Araport; AT1G13960; -.
DR TAIR; locus:2014799; AT1G13960.
DR eggNOG; ENOG502QTWW; Eukaryota.
DR HOGENOM; CLU_012086_7_0_1; -.
DR InParanoid; Q9XI90; -.
DR OMA; PQTEYPH; -.
DR OrthoDB; 847761at2759; -.
DR PhylomeDB; Q9XI90; -.
DR EvolutionaryTrace; Q9XI90; -.
DR PRO; PR:Q9XI90; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XI90; baseline and differential.
DR Genevisible; Q9XI90; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:TAIR.
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:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:1900425; P:negative regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; IDA:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IDA:UniProtKB.
DR GO; GO:0009751; P:response to salicylic acid; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Plant defense; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..514
FT /note="Probable WRKY transcription factor 4"
FT /id="PRO_0000133647"
FT DNA_BIND 223..287
FT /note="WRKY 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT DNA_BIND 403..468
FT /note="WRKY 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 434
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15705956,
FT ECO:0000269|PubMed:22219184"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15705956,
FT ECO:0000269|PubMed:22219184"
FT BINDING 439
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15705956,
FT ECO:0000269|PubMed:22219184"
FT BINDING 463
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15705956,
FT ECO:0000269|PubMed:22219184"
FT BINDING 465
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:15705956,
FT ECO:0000269|PubMed:22219184"
FT VAR_SEQ 112..147
FT /note="GLMISQSQSPSMFTVPPGLSPAMLLDSPSFLGLFSP -> AVLDLICNI
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11449049"
FT /id="VSP_008969"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:1WJ2"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:1WJ2"
FT TURN 423..426
FT /evidence="ECO:0007829|PDB:2LEX"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:1WJ2"
FT STRAND 440..448
FT /evidence="ECO:0007829|PDB:1WJ2"
FT TURN 449..452
FT /evidence="ECO:0007829|PDB:1WJ2"
FT STRAND 453..461
FT /evidence="ECO:0007829|PDB:1WJ2"
SQ SEQUENCE 514 AA; 55816 MW; 01010F8745C420C5 CRC64;
MSEKEEAPST SKSTGAPSRP TLSLPPRPFS EMFFNGGVGF SPGPMTLVSN MFPDSDEFRS
FSQLLAGAMS SPATAAAAAA AATASDYQRL GEGTNSSSGD VDPRFKQNRP TGLMISQSQS
PSMFTVPPGL SPAMLLDSPS FLGLFSPVQG SYGMTHQQAL AQVTAQAVQA NANMQPQTEY
PPPSQVQSFS SGQAQIPTSA PLPAQRETSD VTIIEHRSQQ PLNVDKPADD GYNWRKYGQK
QVKGSEFPRS YYKCTNPGCP VKKKVERSLD GQVTEIIYKG QHNHEPPQNT KRGNKDNTAN
INGSSINNNR GSSELGASQF QTNSSNKTKR EQHEAVSQAT TTEHLSEASD GEEVGNGETD
VREKDENEPD PKRRSTEVRI SEPAPAASHR TVTEPRIIVQ TTSEVDLLDD GYRWRKYGQK
VVKGNPYPRS YYKCTTPGCG VRKHVERAAT DPKAVVTTYE GKHNHDLPAA KSSSHAAAAA
QLRPDNRPGG LANLNQQQQQ QPVARLRLKE EQTT
