WRKY6_ARATH
ID WRKY6_ARATH Reviewed; 553 AA.
AC Q9C519; O04594; Q9C5T1;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=WRKY transcription factor 6 {ECO:0000303|PubMed:11722756};
DE AltName: Full=WRKY DNA-binding protein 6 {ECO:0000303|PubMed:11722756};
DE Short=AtWRKY6 {ECO:0000303|PubMed:11722756};
GN Name=WRKY6 {ECO:0000303|PubMed:11722756};
GN OrderedLocusNames=At1g62300 {ECO:0000312|Araport:AT1G62300};
GN ORFNames=F19K23.22 {ECO:0000312|EMBL:AAB60774.1};
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 [GENOMIC DNA / MRNA], INDUCTION, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF LYS-278 AND 296-ARG-LYS-297.
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 [2]
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 [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 [MRNA] OF 316-553, 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 [5]
RP FUNCTION.
RX PubMed=12000796; DOI=10.1101/gad.222702;
RA Robatzek S., Somssich I.E.;
RT "Targets of AtWRKY6 regulation during plant senescence and pathogen
RT defense.";
RL Genes Dev. 16:1139-1149(2002).
RN [6]
RP FUNCTION.
RX PubMed=25733771; DOI=10.1104/pp.114.253799;
RA Su T., Xu Q., Zhang F.C., Chen Y., Li L.Q., Wu W.H., Chen Y.F.;
RT "WRKY42 modulates phosphate homeostasis through regulating phosphate
RT translocation and acquisition in Arabidopsis.";
RL Plant Physiol. 167:1579-1591(2015).
CC -!- FUNCTION: Transcription factor involved in the control of processes
CC related to senescence and pathogen defense (PubMed:12000796). Interacts
CC specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring
CC elicitor-responsive cis-acting element (PubMed:12000796). Activates the
CC transcription of the SIRK gene and represses its own expression and
CC that of the WRKY42 genes (PubMed:12000796). Modulates phosphate
CC homeostasis and Pi translocation by regulating PHO1 expression
CC (PubMed:25733771). {ECO:0000269|PubMed:12000796,
CC ECO:0000269|PubMed:25733771}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00223,
CC ECO:0000269|PubMed:11722756}.
CC -!- TISSUE SPECIFICITY: Roots, leaves, shoots, flowers and siliques.
CC -!- INDUCTION: By salicylic acid, ethylene, jasmonic acid, pathogens,
CC wounding and strongly during leaf senescence.
CC {ECO:0000269|PubMed:11449049, ECO:0000269|PubMed:11722756}.
CC -!- SIMILARITY: Belongs to the WRKY group II-b family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB60774.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF331713; AAK01128.1; -; Genomic_DNA.
DR EMBL; AF331712; AAK01127.1; -; mRNA.
DR EMBL; AC000375; AAB60774.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33948.1; -; Genomic_DNA.
DR EMBL; AF224702; AAK28312.1; -; mRNA.
DR PIR; F96649; F96649.
DR RefSeq; NP_564792.1; NM_104910.3.
DR AlphaFoldDB; Q9C519; -.
DR SMR; Q9C519; -.
DR BioGRID; 27748; 13.
DR IntAct; Q9C519; 9.
DR STRING; 3702.AT1G62300.1; -.
DR iPTMnet; Q9C519; -.
DR PaxDb; Q9C519; -.
DR PRIDE; Q9C519; -.
DR ProteomicsDB; 246420; -.
DR EnsemblPlants; AT1G62300.1; AT1G62300.1; AT1G62300.
DR GeneID; 842527; -.
DR Gramene; AT1G62300.1; AT1G62300.1; AT1G62300.
DR KEGG; ath:AT1G62300; -.
DR Araport; AT1G62300; -.
DR TAIR; locus:2018052; AT1G62300.
DR eggNOG; ENOG502QSY8; Eukaryota.
DR HOGENOM; CLU_021824_3_1_1; -.
DR InParanoid; Q9C519; -.
DR OMA; HMMNRRE; -.
DR OrthoDB; 885744at2759; -.
DR PhylomeDB; Q9C519; -.
DR PRO; PR:Q9C519; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C519; baseline and differential.
DR Genevisible; Q9C519; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:TAIR.
DR GO; GO:0080169; P:cellular response to boron-containing substance deprivation; IMP:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IMP:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:TAIR.
DR Gene3D; 2.20.25.80; -; 1.
DR InterPro; IPR003657; WRKY_dom.
DR InterPro; IPR036576; WRKY_dom_sf.
DR InterPro; IPR044810; WRKY_plant.
DR PANTHER; PTHR31429; PTHR31429; 2.
DR Pfam; PF03106; WRKY; 1.
DR SMART; SM00774; WRKY; 1.
DR SUPFAM; SSF118290; SSF118290; 1.
DR PROSITE; PS50811; WRKY; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Ethylene signaling pathway; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..553
FT /note="WRKY transcription factor 6"
FT /id="PRO_0000133648"
FT DNA_BIND 306..372
FT /note="WRKY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT REGION 111..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 278
FT /note="K->E: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:11722756"
FT MUTAGEN 296..297
FT /note="RK->AA: No effect on nuclear localization."
FT /evidence="ECO:0000269|PubMed:11722756"
SQ SEQUENCE 553 AA; 60593 MW; 9C75C89E4F16F297 CRC64;
MDRGWSGLTL DSSSLDLLNP NRISHKNHRR FSNPLAMSRI DEEDDQKTRI STNGSEFRFP
VSLSGIRDRE DEDFSSGVAG DNDREVPGEV DFFSDKKSRV CREDDEGFRV KKEEQDDRTD
VNTGLNLRTT GNTKSDESMI DDGESSEMED KRAKNELVKL QDELKKMTMD NQKLRELLTQ
VSNSYTSLQM HLVSLMQQQQ QQNNKVIEAA EKPEETIVPR QFIDLGPTRA VGEAEDVSNS
SSEDRTRSGG SSAAERRSNG KRLGREESPE TESNKIQKVN STTPTTFDQT AEATMRKARV
SVRARSEAPM ISDGCQWRKY GQKMAKGNPC PRAYYRCTMA TGCPVRKQVQ RCAEDRSILI
TTYEGNHNHP LPPAAVAMAS TTTAAANMLL SGSMSSHDGM MNPTNLLARA VLPCSTSMAT
ISASAPFPTV TLDLTHSPPP PNGSNPSSSA ATNNNHNSLM QRPQQQQQQM TNLPPGMLPH
VIGQALYNQS KFSGLQFSGG SPSTAAFSQS HAVADTITAL TADPNFTAAL AAVISSMING
TNHHDGEGNN KNQ