WRK25_ARATH
ID WRK25_ARATH Reviewed; 393 AA.
AC O22921; Q94AT4;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Probable WRKY transcription factor 25;
DE AltName: Full=WRKY DNA-binding protein 25;
GN Name=WRKY25; OrderedLocusNames=At2g30250; ORFNames=T9D9.6;
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; TISSUE=Flower;
RA Ulker B., Kushnir S., Somssich I.E.;
RT "Arabidopsis thaliana transcription factor WRKY25.";
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 INTERACTION WITH MKS1, AND PHOSPHORYLATION.
RX PubMed=15990873; DOI=10.1038/sj.emboj.7600737;
RA Andreasson E., Jenkins T., Brodersen P., Thorgrimsen S., Petersen N.H.T.,
RA Zhu S., Qiu J.-L., Micheelsen P., Rocher A., Petersen M., Newman M.-A.,
RA Bjoern Nielsen H., Hirt H., Somssich I.E., Mattsson O., Mundy J.;
RT "The MAP kinase substrate MKS1 is a regulator of plant defense responses.";
RL EMBO J. 24:2579-2589(2005).
RN [6]
RP FUNCTION, AND INDUCTION BY HEAT.
RX PubMed=19125253; DOI=10.1007/s00299-008-0666-y;
RA Li S., Fu Q., Huang W., Yu D.;
RT "Functional analysis of an Arabidopsis transcription factor WRKY25 in heat
RT stress.";
RL Plant Cell Rep. 28:683-693(2009).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY SALT, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18839316; DOI=10.1007/s11103-008-9408-3;
RA Jiang Y., Deyholos M.K.;
RT "Functional characterization of Arabidopsis NaCl-inducible WRKY25 and
RT WRKY33 transcription factors in abiotic stresses.";
RL Plant Mol. Biol. 69:91-105(2009).
RN [8]
RP FUNCTION.
RX PubMed=21336597; DOI=10.1007/s00425-011-1375-2;
RA Li S., Fu Q., Chen L., Huang W., Yu D.;
RT "Arabidopsis thaliana WRKY25, WRKY26, and WRKY33 coordinate induction of
RT plant thermotolerance.";
RL Planta 233:1237-1252(2011).
RN [9]
RP INTERACTION WITH SIB1.
RX PubMed=21990940; DOI=10.1105/tpc.111.090571;
RA Lai Z., Li Y., Wang F., Cheng Y., Fan B., Yu J.Q., Chen Z.;
RT "Arabidopsis sigma factor binding proteins are activators of the WRKY33
RT transcription factor in plant defense.";
RL Plant Cell 23:3824-3841(2011).
RN [10]
RP INTERACTION WITH VQ10 AND CAMBP25/VQ15.
RX PubMed=22535423; DOI=10.1104/pp.112.196816;
RA Cheng Y., Zhou Y., Yang Y., Chi Y.J., Zhou J., Chen J.Y., Wang F., Fan B.,
RA Shi K., Zhou Y.H., Yu J.Q., Chen Z.;
RT "Structural and functional analysis of VQ motif-containing proteins in
RT Arabidopsis as interacting proteins of WRKY transcription factors.";
RL Plant Physiol. 159:810-825(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 (By similarity). Functions with WRKY33 as positive
CC regulator of salt stress response and abscisic acid (ABA) signaling
CC (PubMed:18839316). Plays a partial role in heat stress tolerance
CC (PubMed:19125253). Functions with WRKY26 and WRKY33 as positive
CC regulator of plant thermotolerance by partially participating in
CC ethylene-response signal transduction pathway (PubMed:21336597).
CC {ECO:0000250|UniProtKB:Q9SI37, ECO:0000269|PubMed:18839316,
CC ECO:0000269|PubMed:19125253, ECO:0000269|PubMed:21336597}.
CC -!- SUBUNIT: Interacts with MKS1 (PubMed:15990873). Interacts with SIB1
CC (PubMed:21990940). Interacts with VQ10 and CAMBP25/VQ15
CC (PubMed:22535423). {ECO:0000269|PubMed:15990873,
CC ECO:0000269|PubMed:21990940, ECO:0000269|PubMed:22535423}.
CC -!- INTERACTION:
CC O22921; Q8LGD5: MKS1; NbExp=3; IntAct=EBI-1392386, EBI-1392198;
CC O22921; Q39024: MPK4; NbExp=2; IntAct=EBI-1392386, EBI-994375;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18839316}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots and at lower levels in
CC leaves, stems and seeds. {ECO:0000269|PubMed:18839316}.
CC -!- INDUCTION: By salt stress (PubMed:18839316). Induced by heat stress
CC (PubMed:19125253). {ECO:0000269|PubMed:18839316,
CC ECO:0000269|PubMed:19125253}.
CC -!- PTM: Phosphorylated by MPK4. {ECO:0000305|PubMed:15990873}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:18839316}.
CC -!- SIMILARITY: Belongs to the WRKY group I family. {ECO:0000305}.
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DR EMBL; AF418309; AAL13040.1; -; mRNA.
DR EMBL; AC002338; AAC16930.1; -; Genomic_DNA.
DR EMBL; AC004165; AAM14918.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08362.1; -; Genomic_DNA.
DR EMBL; AY062720; AAL32798.1; -; mRNA.
DR EMBL; AY114650; AAM47969.1; -; mRNA.
DR EMBL; AY136318; AAM96984.1; -; mRNA.
DR EMBL; AY045813; AAK76487.2; -; mRNA.
DR EMBL; BT002338; AAN86171.1; -; mRNA.
DR EMBL; BT008482; AAP37841.1; -; mRNA.
DR PIR; T00575; T00575.
DR RefSeq; NP_180584.1; NM_128578.4.
DR AlphaFoldDB; O22921; -.
DR SMR; O22921; -.
DR BioGRID; 2924; 19.
DR IntAct; O22921; 3.
DR STRING; 3702.AT2G30250.1; -.
DR PaxDb; O22921; -.
DR PRIDE; O22921; -.
DR ProteomicsDB; 234413; -.
DR EnsemblPlants; AT2G30250.1; AT2G30250.1; AT2G30250.
DR GeneID; 817575; -.
DR Gramene; AT2G30250.1; AT2G30250.1; AT2G30250.
DR KEGG; ath:AT2G30250; -.
DR Araport; AT2G30250; -.
DR TAIR; locus:2060805; AT2G30250.
DR eggNOG; ENOG502QRXJ; Eukaryota.
DR HOGENOM; CLU_012086_5_0_1; -.
DR InParanoid; O22921; -.
DR OMA; PHDQSEN; -.
DR OrthoDB; 845542at2759; -.
DR PhylomeDB; O22921; -.
DR PRO; PR:O22921; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22921; baseline and differential.
DR Genevisible; O22921; AT.
DR GO; GO:0005634; C:nucleus; IDA: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; IEA:InterPro.
DR GO; GO:0070370; P:cellular heat acclimation; IMP:TAIR.
DR GO; GO:0034605; P:cellular response to heat; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP: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 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Stress response; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..393
FT /note="Probable WRKY transcription factor 25"
FT /id="PRO_0000133667"
FT DNA_BIND 160..224
FT /note="WRKY 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT DNA_BIND 322..387
FT /note="WRKY 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT REGION 217..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
SQ SEQUENCE 393 AA; 44134 MW; 9057D65B69E12A0C CRC64;
MSSTSFTDLL GSSGVDCYED DEDLRVSGSS FGGYYPERTG SGLPKFKTAQ PPPLPISQSS
HNFTFSDYLD SPLLLSSSHS LISPTTGTFP LQGFNGTTNN HSDFPWQLQS QPSNASSALQ
ETYGVQDHEK KQEMIPNEIA TQNNNQSFGT ERQIKIPAYM VSRNSNDGYG WRKYGQKQVK
KSENPRSYFK CTYPDCVSKK IVETASDGQI TEIIYKGGHN HPKPEFTKRP SQSSLPSSVN
GRRLFNPASV VSEPHDQSEN SSISFDYSDL EQKSFKSEYG EIDEEEEQPE MKRMKREGED
EGMSIEVSKG VKEPRVVVQT ISDIDVLIDG FRWRKYGQKV VKGNTNPRSY YKCTFQGCGV
KKQVERSAAD ERAVLTTYEG RHNHDIPTAL RRS
