WRK26_ARATH
ID WRK26_ARATH Reviewed; 309 AA.
AC Q9C5T3; Q8GYK8; Q9LYQ5;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable WRKY transcription factor 26;
DE AltName: Full=SPF1-like protein;
DE AltName: Full=WRKY DNA-binding protein 26;
GN Name=WRKY26; OrderedLocusNames=At5g07100; ORFNames=MOJ9.27, T28J14_40;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND INDUCTION BY HEAT.
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 [8]
RP INTERACTION WITH VQ10.
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 WRKY25 and WRKY33 as
CC positive regulator of plant thermotolerance by partially participating
CC in ethylene-response signal transduction pathway (PubMed:21336597).
CC {ECO:0000250|UniProtKB:Q9SI37, ECO:0000269|PubMed:21336597}.
CC -!- SUBUNIT: Interacts with VQ10. {ECO:0000269|PubMed:22535423}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9SI37}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9C5T3-1; Sequence=Displayed;
CC -!- INDUCTION: By salicylic acid (PubMed:11449049). Induced by heat stress
CC (PubMed:21336597). {ECO:0000269|PubMed:11449049,
CC ECO:0000269|PubMed:21336597}.
CC -!- SIMILARITY: Belongs to the WRKY group I family. {ECO:0000305}.
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DR EMBL; AF224699; AAK28309.1; -; mRNA.
DR EMBL; AB010697; BAB11168.1; -; Genomic_DNA.
DR EMBL; AL163652; CAB87266.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91109.1; -; Genomic_DNA.
DR EMBL; AK117545; BAC42206.1; -; mRNA.
DR EMBL; AY084692; AAM61254.1; -; mRNA.
DR PIR; T48481; T48481.
DR RefSeq; NP_196327.1; NM_120792.2. [Q9C5T3-1]
DR AlphaFoldDB; Q9C5T3; -.
DR SMR; Q9C5T3; -.
DR BioGRID; 15880; 5.
DR IntAct; Q9C5T3; 4.
DR STRING; 3702.AT5G07100.1; -.
DR PaxDb; Q9C5T3; -.
DR PRIDE; Q9C5T3; -.
DR ProteomicsDB; 234363; -. [Q9C5T3-1]
DR EnsemblPlants; AT5G07100.1; AT5G07100.1; AT5G07100. [Q9C5T3-1]
DR GeneID; 830601; -.
DR Gramene; AT5G07100.1; AT5G07100.1; AT5G07100. [Q9C5T3-1]
DR KEGG; ath:AT5G07100; -.
DR Araport; AT5G07100; -.
DR TAIR; locus:2169354; AT5G07100.
DR eggNOG; ENOG502QRXJ; Eukaryota.
DR HOGENOM; CLU_012086_5_0_1; -.
DR InParanoid; Q9C5T3; -.
DR OMA; SHFQTED; -.
DR OrthoDB; 1013914at2759; -.
DR PhylomeDB; Q9C5T3; -.
DR PRO; PR:Q9C5T3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C5T3; baseline and differential.
DR Genevisible; Q9C5T3; 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: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 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; 3.
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 Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Stress response; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..309
FT /note="Probable WRKY transcription factor 26"
FT /id="PRO_0000133668"
FT DNA_BIND 111..176
FT /note="WRKY 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT DNA_BIND 228..293
FT /note="WRKY 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 259
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 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT CONFLICT 148
FT /note="L -> P (in Ref. 5; BAC42206)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="I -> F (in Ref. 6; AAM61254)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="S -> P (in Ref. 1; AAK28309)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 34911 MW; B83AF11B93F3909E CRC64;
MGSFDRQRAV PKFKTATPSP LPLSPSPYFT MPPGLTPADF LDSPLLFTSS NILPSPTTGT
FPAQSLNYNN NGLLIDKNEI KYEDTTPPLF LPSMVTQPLP QLDLFKSEIM SSNKTSDDGY
NWRKYGQKQV KGSENPRSYF KCTYPNCLTK KKVETSLVKG QMIEIVYKGS HNHPKPQSTK
RSSSTAIAAH QNSSNGDGKD IGEDETEAKR WKREENVKEP RVVVQTTSDI DILDDGYRWR
KYGQKVVKGN PNPRSYYKCT FTGCFVRKHV ERAFQDPKSV ITTYEGKHKH QIPTPRRGPV
LRLLGKTET
