WRKY1_ARATH
ID WRKY1_ARATH Reviewed; 487 AA.
AC Q9SI37; Q058Q1; Q43388;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=WRKY transcription factor 1 {ECO:0000303|Ref.2};
DE AltName: Full=Transcription factor ZAP1 {ECO:0000303|PubMed:8972846};
DE AltName: Full=WRKY DNA-binding protein 1 {ECO:0000303|Ref.2};
DE AltName: Full=Zinc-dependent activator protein 1 {ECO:0000303|PubMed:8972846};
GN Name=WRKY1 {ECO:0000303|Ref.2}; Synonyms=ZAP1 {ECO:0000303|PubMed:8972846};
GN OrderedLocusNames=At2g04880 {ECO:0000312|Araport:AT2G04880};
GN ORFNames=F1O13.1 {ECO:0000312|EMBL:AAD25579.1},
GN F28I8.34 {ECO:0000312|EMBL:AAL35283.1};
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 [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, AND
RP DNA-BINDING.
RC STRAIN=cv. C24; TISSUE=Flower, and Silique;
RX PubMed=8972846; DOI=10.1093/nar/24.23.4624;
RA De Pater S., Greco V., Pham K., Memelink J., Kijne J.;
RT "Characterization of a zinc-dependent transcriptional activator from
RT Arabidopsis.";
RL Nucleic Acids Res. 24:4624-4631(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia; TISSUE=Flower;
RA Ulker B., Kushnir S., Somssich I.E.;
RT "Arabidopsis thaliana transcription factor WRKY1.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clone.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 293-368 IN COMPLEX WITH ZINC,
RP INDUCTION BY SALICYLIC ACID, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP 273-LYS--LYS-277; ARG-313; LYS-314; TYR-315; GLY-316; GLN-317; ARG-327;
RP TYR-330; ARG-331 AND LYS-340, AND NUCLEAR LOCALIZATION SIGNAL.
RC STRAIN=cv. Columbia;
RX PubMed=17264121; DOI=10.1093/nar/gkm001;
RA Duan M.-R., Nan J., Liang Y.-H., Mao P., Lu L., Li L., Wei C., Lai L.,
RA Li Y., Su X.-D.;
RT "DNA binding mechanism revealed by high resolution crystal structure of
RT Arabidopsis thaliana WRKY1 protein.";
RL Nucleic Acids Res. 35:1145-1154(2007).
CC -!- FUNCTION: Transcription factor. Binds to a 5'-CGTTGACCGAG-3' consensus
CC core sequence which contains a W box, a frequently occurring elicitor-
CC responsive cis-acting element. {ECO:0000269|PubMed:8972846}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17264121}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SI37-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SI37-2; Sequence=VSP_007124;
CC -!- TISSUE SPECIFICITY: Expressed to similar levels in root and flower, to
CC a somewhat lower level in stem and to low levels in leaf and siliques.
CC {ECO:0000269|PubMed:8972846}.
CC -!- INDUCTION: By salicylic acid (SA). {ECO:0000269|PubMed:17264121}.
CC -!- MISCELLANEOUS: Binding to target DNA is mediated mainly by the C-
CC terminal WRKY domain, while part of the activation domain is located
CC between positions 210 and 285. {ECO:0000269|PubMed:8972846}.
CC -!- SIMILARITY: Belongs to the WRKY group I family. {ECO:0000305}.
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DR EMBL; X92976; CAA63554.1; -; mRNA.
DR EMBL; AF442389; AAL35282.1; -; mRNA.
DR EMBL; AF442390; AAL35283.1; -; mRNA.
DR EMBL; AC006955; AAM15341.1; -; Genomic_DNA.
DR EMBL; AC007211; AAD25579.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05880.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05881.1; -; Genomic_DNA.
DR EMBL; BT029167; ABJ17102.1; -; mRNA.
DR PIR; F84462; F84462.
DR RefSeq; NP_178565.1; NM_126520.4. [Q9SI37-1]
DR RefSeq; NP_849936.1; NM_179605.3. [Q9SI37-2]
DR PDB; 2AYD; X-ray; 1.60 A; A=293-368.
DR PDB; 6J4E; X-ray; 3.13 A; B=101-170.
DR PDB; 7D11; NMR; -; A=92-170.
DR PDBsum; 2AYD; -.
DR PDBsum; 6J4E; -.
DR PDBsum; 7D11; -.
DR AlphaFoldDB; Q9SI37; -.
DR SMR; Q9SI37; -.
DR BioGRID; 436; 1.
DR STRING; 3702.AT2G04880.1; -.
DR iPTMnet; Q9SI37; -.
DR PaxDb; Q9SI37; -.
DR PRIDE; Q9SI37; -.
DR ProteomicsDB; 234394; -. [Q9SI37-1]
DR EnsemblPlants; AT2G04880.1; AT2G04880.1; AT2G04880. [Q9SI37-1]
DR EnsemblPlants; AT2G04880.2; AT2G04880.2; AT2G04880. [Q9SI37-2]
DR GeneID; 815035; -.
DR Gramene; AT2G04880.1; AT2G04880.1; AT2G04880. [Q9SI37-1]
DR Gramene; AT2G04880.2; AT2G04880.2; AT2G04880. [Q9SI37-2]
DR KEGG; ath:AT2G04880; -.
DR Araport; AT2G04880; -.
DR TAIR; locus:2045049; AT2G04880.
DR eggNOG; ENOG502QV11; Eukaryota.
DR InParanoid; Q9SI37; -.
DR OMA; PMNQDRR; -.
DR OrthoDB; 646737at2759; -.
DR PhylomeDB; Q9SI37; -.
DR EvolutionaryTrace; Q9SI37; -.
DR PRO; PR:Q9SI37; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SI37; baseline and differential.
DR Genevisible; Q9SI37; AT.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IMP:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IDA:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR GO; GO:0009863; P:salicylic acid mediated signaling pathway; IEP: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 3D-structure; Activator; Alternative splicing; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..487
FT /note="WRKY transcription factor 1"
FT /id="PRO_0000133644"
FT DNA_BIND 105..169
FT /note="WRKY 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT DNA_BIND 301..366
FT /note="WRKY 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT REGION 69..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 273..277
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:17264121"
FT COMPBIAS 82..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:17264121,
FT ECO:0007744|PDB:2AYD"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:17264121,
FT ECO:0007744|PDB:2AYD"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:17264121,
FT ECO:0007744|PDB:2AYD"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:17264121,
FT ECO:0007744|PDB:2AYD"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17264121,
FT ECO:0007744|PDB:2AYD"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17264121,
FT ECO:0007744|PDB:2AYD"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17264121,
FT ECO:0007744|PDB:2AYD"
FT BINDING 363
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17264121,
FT ECO:0007744|PDB:2AYD"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 191..214
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8972846, ECO:0000303|Ref.5"
FT /id="VSP_007124"
FT MUTAGEN 273..277
FT /note="Missing: Impaired nuclear localization."
FT /evidence="ECO:0000269|PubMed:17264121"
FT MUTAGEN 313
FT /note="R->E: Reduced DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:17264121"
FT MUTAGEN 314
FT /note="K->A: Impaired DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:17264121"
FT MUTAGEN 314
FT /note="K->R: Reduced DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:17264121"
FT MUTAGEN 315
FT /note="Y->F: Reduced DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:17264121"
FT MUTAGEN 315
FT /note="Y->R: Impaired DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:17264121"
FT MUTAGEN 316
FT /note="G->F: Impaired DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:17264121"
FT MUTAGEN 317
FT /note="Q->A: Normal DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:17264121"
FT MUTAGEN 317
FT /note="Q->K: Reduced DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:17264121"
FT MUTAGEN 327
FT /note="R->A,E: Impaired DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:17264121"
FT MUTAGEN 330
FT /note="Y->F: Normal DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:17264121"
FT MUTAGEN 331
FT /note="R->A: Impaired DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:17264121"
FT MUTAGEN 331
FT /note="R->K: Normal DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:17264121"
FT MUTAGEN 340
FT /note="K->A: Normal DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:17264121"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:7D11"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:7D11"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:7D11"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:6J4E"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:6J4E"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:6J4E"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:6J4E"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:6J4E"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:2AYD"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:2AYD"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:2AYD"
FT STRAND 327..332
FT /evidence="ECO:0007829|PDB:2AYD"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:2AYD"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:2AYD"
FT STRAND 352..359
FT /evidence="ECO:0007829|PDB:2AYD"
SQ SEQUENCE 487 AA; 54010 MW; 61721DB016897C38 CRC64;
MAEVGKVLAS DMELDHSNET KAVDDVVATT DKAEVIPVAV TRTETVVESL ESTDCKELEK
LVPHTVASQS EVDVASPVSE KAPKVSESSG ALSLQSGSEG NSPFIREKVM EDGYNWRKYG
QKLVKGNEFV RSYYRCTHPN CKAKKQLERS AGGQVVDTVY FGEHDHPKPL AGAVPINQDK
RSDVFTAVSK GEQRIDIVSL IYKLCIVSYD IMFVEKTSGS SVQTLRQTEP PKIHGGLHVS
VIPPADDVKT DISQSSRITG DNTHKDYNSP TAKRRKKGGN IELSPVERST NDSRIVVHTQ
TLFDIVNDGY RWRKYGQKSV KGSPYPRSYY RCSSPGCPVK KHVERSSHDT KLLITTYEGK
HDHDMPPGRV VTHNNMLDSE VDDKEGDANK TPQSSTLQSI TKDQHVEDHL RKKTKTNGFE
KSLDQGPVLD EKLKEEIKER SDANKDHAAN HAKPEAKSDD KTTVCQEKAV GTLESEEQKP
KTEPAQS
