WRKY8_ARATH
ID WRKY8_ARATH Reviewed; 326 AA.
AC Q9FL26;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=WRKY transcription factor 8;
DE AltName: Full=WRKY DNA-binding protein 8;
GN Name=WRKY8; OrderedLocusNames=At5g46350; ORFNames=MPL12.15;
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.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
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 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 FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20367464; DOI=10.1094/mpmi-23-5-0558;
RA Chen L., Zhang L., Yu D.;
RT "Wounding-induced WRKY8 is involved in basal defense in Arabidopsis.";
RL Mol. Plant Microbe Interact. 23:558-565(2010).
RN [6]
RP FUNCTION, INTERACTION WITH VQ9, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP INDUCTION BY SALT, AND DISRUPTION PHENOTYPE.
RX PubMed=23451802; DOI=10.1111/tpj.12159;
RA Hu Y., Chen L., Wang H., Zhang L., Wang F., Yu D.;
RT "Arabidopsis transcription factor WRKY8 functions antagonistically with its
RT interacting partner VQ9 to modulate salinity stress tolerance.";
RL Plant J. 74:730-745(2013).
RN [7]
RP FUNCTION.
RX PubMed=23650359; DOI=10.1073/pnas.1221347110;
RA Chen L., Zhang L., Li D., Wang F., Yu D.;
RT "WRKY8 transcription factor functions in the TMV-cg defense response by
RT mediating both abscisic acid and ethylene signaling in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E1963-1971(2013).
CC -!- FUNCTION: Transcription factor. Interacts specifically with the W box
CC (5'-TTGAC[CT]-3'), a frequently occurring stress-responsive cis-acting
CC element. Functions as positive regulator of salt stress response. Binds
CC the W box of LTI78/RD29A stress-response gene and directly regulates
CC its transcription under salt stress. Functions antagonistically with
CC VQ9 to regulate sodium and potassium homeostasis under salt stress by
CC regulating the expression of downstream SOS (SALT OVERLY SENSITIVE)
CC stress-responsive genes. The DNA-binding activity of WRKY8 is decreased
CC by VQ9 (PubMed:23451802). Functions as negative regulator of basal
CC resistance to the bacterial pathogen P. syringae and as positive
CC regulator of resistance to the fungal pathogen to B. cinerea
CC (PubMed:20367464). Functions as positive regulator of defense response
CC againt tobamovirus (TMV) by regulating both the abscisic acid and
CC ethylene signaling pathways. Positively regulates ABI4 expression and
CC negatively modulates ACS6 and ERF104 expression by directly binding to
CC the W box consensus motifs within their promoters (PubMed:23650359).
CC {ECO:0000269|PubMed:20367464, ECO:0000269|PubMed:23451802,
CC ECO:0000269|PubMed:23650359}.
CC -!- SUBUNIT: Interacts with VQ9 (via N-terminus).
CC {ECO:0000269|PubMed:23451802}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20367464,
CC ECO:0000269|PubMed:23451802}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots and at lower levels in
CC rosette leaves, cauline leaves, stems, flowers and siliques.
CC {ECO:0000269|PubMed:23451802}.
CC -!- INDUCTION: By wounding, abscisic acid (ABA), salicylic acid (SA),
CC H(2)O(2), and infection with P.syringae pv. tomato DC3000 and B.cinerea
CC (PubMed:20367464). Induced by salt stress (PubMed:23451802).
CC {ECO:0000269|PubMed:20367464, ECO:0000269|PubMed:23451802}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (PubMed:20367464, PubMed:23451802). Mutant plants show
CC increased resistance to the bacterial pathogen P.syringae and enhanced
CC susceptibility to the fungal pathogen to B.cinerea (PubMed:20367464).
CC Mutant plants display increased sensitivity to salt stress
CC (PubMed:23451802). {ECO:0000269|PubMed:20367464,
CC ECO:0000269|PubMed:23451802}.
CC -!- SIMILARITY: Belongs to the WRKY group II-c family. {ECO:0000305}.
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DR EMBL; AF404855; AAK96193.1; -; mRNA.
DR EMBL; AB010698; BAB11090.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95372.1; -; Genomic_DNA.
DR EMBL; AY063916; AAL36272.1; -; mRNA.
DR EMBL; AY096426; AAM20066.1; -; mRNA.
DR RefSeq; NP_199447.1; NM_124005.5.
DR AlphaFoldDB; Q9FL26; -.
DR SMR; Q9FL26; -.
DR BioGRID; 19927; 2.
DR IntAct; Q9FL26; 1.
DR STRING; 3702.AT5G46350.1; -.
DR PaxDb; Q9FL26; -.
DR PRIDE; Q9FL26; -.
DR ProteomicsDB; 234368; -.
DR EnsemblPlants; AT5G46350.1; AT5G46350.1; AT5G46350.
DR GeneID; 834678; -.
DR Gramene; AT5G46350.1; AT5G46350.1; AT5G46350.
DR KEGG; ath:AT5G46350; -.
DR Araport; AT5G46350; -.
DR TAIR; locus:2170403; AT5G46350.
DR eggNOG; ENOG502QQYS; Eukaryota.
DR HOGENOM; CLU_033779_2_0_1; -.
DR InParanoid; Q9FL26; -.
DR OMA; NRRTAMF; -.
DR OrthoDB; 966867at2759; -.
DR PhylomeDB; Q9FL26; -.
DR PRO; PR:Q9FL26; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FL26; baseline and differential.
DR Genevisible; Q9FL26; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0051607; P:defense response to virus; IMP:CACAO.
DR GO; GO:1901002; P:positive regulation of response to salt stress; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR Gene3D; 2.20.25.80; -; 1.
DR InterPro; IPR017396; TF_WRKY_IIc.
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; 1.
DR PIRSF; PIRSF038130; TF_WRKY_IIc; 1.
DR SMART; SM00774; WRKY; 1.
DR SUPFAM; SSF118290; SSF118290; 1.
DR PROSITE; PS50811; WRKY; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Plant defense; Reference proteome; Stress response;
KW Transcription; Transcription regulation.
FT CHAIN 1..326
FT /note="WRKY transcription factor 8"
FT /id="PRO_0000133650"
FT DNA_BIND 177..242
FT /note="WRKY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT REGION 115..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 326 AA; 37294 MW; 4D2A58B4327467BC CRC64;
MSHEIKDLNN YHYTSSYNHY NINNQNMINL PYVSGPSAYN ANMISSSQVG FDLPSKNLSP
QGAFELGFEL SPSSSDFFNP SLDQENGLYN AYNYNSSQKS HEVVGDGCAT IKSEVRVSAS
PSSSEADHHP GEDSGKIRKK REVRDGGEDD QRSQKVVKTK KKEEKKKEPR VSFMTKTEVD
HLEDGYRWRK YGQKAVKNSP YPRSYYRCTT QKCNVKKRVE RSYQDPTVVI TTYESQHNHP
IPTNRRTAMF SGTTASDYNP SSSPIFSDLI INTPRSFSND DLFRVPYASV NVNPSYHQQQ
HGFHQQESEF ELLKEMFPSV FFKQEP
