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 27-MAR-2024, entry version 155. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.O22921; -. DR PaxDb; 3702-AT2G30250-1; -. 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; AT2G30250; WRKY25. DR eggNOG; ENOG502QRXJ; Eukaryota. DR HOGENOM; CLU_012086_5_0_1; -. DR InParanoid; O22921; -. DR OMA; PHDQSEN; -. DR OrthoDB; 5478560at2759; -. DR PhylomeDB; O22921; -. DR PRO; PR:O22921; -. DR Proteomes; UP000006548; Chromosome 2. DR ExpressionAtlas; O22921; baseline and differential. 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; WRKY domain; 2. DR InterPro; IPR003657; WRKY_dom. DR InterPro; IPR036576; WRKY_dom_sf. DR InterPro; IPR044810; WRKY_plant. DR PANTHER; PTHR31221:SF221; WRKY TRANSCRIPTION FACTOR 25-RELATED; 1. DR PANTHER; PTHR31221; WRKY TRANSCRIPTION FACTOR PROTEIN 1-RELATED; 1. DR Pfam; PF03106; WRKY; 2. DR SMART; SM00774; WRKY; 2. DR SUPFAM; SSF118290; WRKY DNA-binding domain; 2. DR PROSITE; PS50811; WRKY; 2. DR Genevisible; O22921; AT. 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 //