WRK33_ARATH
ID WRK33_ARATH Reviewed; 519 AA.
AC Q8S8P5; Q0WWP2;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Probable WRKY transcription factor 33;
DE AltName: Full=WRKY DNA-binding protein 33;
GN Name=WRKY33; OrderedLocusNames=At2g38470; ORFNames=T19C21.4;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-519.
RC STRAIN=cv. Columbia; TISSUE=Flower;
RA Lippok B., Somssich I.E.;
RT "Arabidopsis thaliana transcription factor WRKY33.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17059405; DOI=10.1111/j.1365-313x.2006.02901.x;
RA Zheng Z., Qamar S.A., Chen Z., Mengiste T.;
RT "Arabidopsis WRKY33 transcription factor is required for resistance to
RT necrotrophic fungal pathogens.";
RL Plant J. 48:592-605(2006).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY SALT.
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 FUNCTION, INDUCTION, AND PHOSPHORYLATION.
RX PubMed=21498677; DOI=10.1105/tpc.111.084996;
RA Mao G., Meng X., Liu Y., Zheng Z., Chen Z., Zhang S.;
RT "Phosphorylation of a WRKY transcription factor by two pathogen-responsive
RT MAPKs drives phytoalexin biosynthesis in Arabidopsis.";
RL Plant Cell 23:1639-1653(2011).
RN [10]
RP FUNCTION, INTERACTION WITH SIB1 AND SIB2, SUBCELLULAR LOCATION, INDUCTION,
RP AND DISRUPTION PHENOTYPE.
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 [11]
RP INTERACTION WITH ATG18A.
RX PubMed=21395886; DOI=10.1111/j.1365-313x.2011.04553.x;
RA Lai Z., Wang F., Zheng Z., Fan B., Chen Z.;
RT "A critical role of autophagy in plant resistance to necrotrophic fungal
RT pathogens.";
RL Plant J. 66:953-968(2011).
RN [12]
RP FUNCTION.
RX PubMed=22392279; DOI=10.1104/pp.111.192641;
RA Birkenbihl R.P., Diezel C., Somssich I.E.;
RT "Arabidopsis WRKY33 is a key transcriptional regulator of hormonal and
RT metabolic responses toward Botrytis cinerea infection.";
RL Plant Physiol. 159:266-285(2012).
RN [13]
RP INTERACTION WITH VQ1 AND VQ10, AND MUTAGENESIS OF ASP-359; ASP-362 AND
RP ARG-366.
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'-TTGAC[CT]-3'), a frequently occurring elicitor-responsive cis-
CC acting element. Involved in defense responses. Required for resistance
CC to the necrotrophic fungal pathogen B.cinerea (PubMed:17059405,
CC PubMed:21990940). Regulates the antagonistic relationship between
CC defense pathways mediating responses to the bacterial pathogen P.
CC syringae and the necrotrophic pathogen B.cinerea (PubMed:17059405).
CC Required for the phytoalexin camalexin synthesis following infection
CC with B.cinerea. Acts as positive regulator of the camalexin
CC biosynthetic genes PAD3 (CYP71B15) and CYP71A13 by binding to their
CC promoters (PubMed:21498677, PubMed:22392279). Acts downstream of MPK3
CC and MPK6 in reprogramming the expression of camalexin biosynthetic
CC genes, which drives the metabolic flow to camalexin production
CC (PubMed:21498677). Functions with WRKY25 as positive regulator of salt
CC stress response and abscisic acid (ABA) signaling (PubMed:18839316).
CC Functions with WRKY25 and WRKY26 as positive regulator of plant
CC thermotolerance by partially participating in ethylene-response signal
CC transduction pathway (PubMed:21336597). The DNA-binding activity of
CC WRKY33 is increased by SIB1 and SIB2 (PubMed:21990940).
CC {ECO:0000269|PubMed:18839316, ECO:0000269|PubMed:21336597,
CC ECO:0000269|PubMed:21498677, ECO:0000269|PubMed:21990940,
CC ECO:0000269|PubMed:22392279}.
CC -!- SUBUNIT: Interacts with MKS1 (PubMed:15990873). Interacts with ATG18A
CC (PubMed:21395886). Interacts with SIB1 and SIB2 (PubMed:21990940).
CC Interacts with VQ1 and VQ10 (PubMed:22535423).
CC {ECO:0000269|PubMed:15990873, ECO:0000269|PubMed:21395886,
CC ECO:0000269|PubMed:21990940, ECO:0000269|PubMed:22535423}.
CC -!- INTERACTION:
CC Q8S8P5; Q93VB2: ATG18A; NbExp=3; IntAct=EBI-1392374, EBI-6510711;
CC Q8S8P5; Q8LGD5: MKS1; NbExp=5; IntAct=EBI-1392374, EBI-1392198;
CC Q8S8P5; Q39024: MPK4; NbExp=2; IntAct=EBI-1392374, EBI-994375;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17059405,
CC ECO:0000269|PubMed:18839316, ECO:0000269|PubMed:21990940}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots, leaves and flowers, and
CC at lower levels in stems, siliques and seeds.
CC {ECO:0000269|PubMed:18839316}.
CC -!- INDUCTION: By salt stress (PubMed:18839316). Induced by infection with
CC the necrotrophic fungal pathogen B.cinerea (PubMed:17059405,
CC PubMed:21498677, PubMed:21990940). Induced by infection with the
CC bacterial pathogen P.syringae pv. tomato DC3000 (PubMed:17059405).
CC {ECO:0000269|PubMed:17059405, ECO:0000269|PubMed:18839316,
CC ECO:0000269|PubMed:21498677, ECO:0000269|PubMed:21990940}.
CC -!- PTM: Phosphorylated by MPK4 (PubMed:15990873). Phosphorylated on serine
CC residues by MPK3 and MPK6 following infection with the necrotrophic
CC fungal pathogen B.cinerea (PubMed:21498677).
CC {ECO:0000269|PubMed:21498677, ECO:0000305|PubMed:15990873}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants are extremely susceptible to the
CC necrotrophic fungal pathogen B.cinerea. {ECO:0000269|PubMed:17059405,
CC ECO:0000269|PubMed:21990940}.
CC -!- SIMILARITY: Belongs to the WRKY group I family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM14994.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC004683; AAM14994.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC09541.1; -; Genomic_DNA.
DR EMBL; AK226301; BAE98456.1; -; mRNA.
DR EMBL; AF509499; AAM34736.1; -; mRNA.
DR PIR; T02498; T02498.
DR RefSeq; NP_181381.2; NM_129404.4.
DR PDB; 6J4G; X-ray; 3.00 A; B=178-242.
DR PDBsum; 6J4G; -.
DR AlphaFoldDB; Q8S8P5; -.
DR SMR; Q8S8P5; -.
DR BioGRID; 3771; 28.
DR IntAct; Q8S8P5; 5.
DR MINT; Q8S8P5; -.
DR STRING; 3702.AT2G38470.1; -.
DR iPTMnet; Q8S8P5; -.
DR PaxDb; Q8S8P5; -.
DR PRIDE; Q8S8P5; -.
DR ProteomicsDB; 234271; -.
DR EnsemblPlants; AT2G38470.1; AT2G38470.1; AT2G38470.
DR GeneID; 818429; -.
DR Gramene; AT2G38470.1; AT2G38470.1; AT2G38470.
DR KEGG; ath:AT2G38470; -.
DR Araport; AT2G38470; -.
DR TAIR; locus:2057212; AT2G38470.
DR eggNOG; ENOG502QRXJ; Eukaryota.
DR HOGENOM; CLU_012086_5_1_1; -.
DR InParanoid; Q8S8P5; -.
DR OMA; KDETIAC; -.
DR OrthoDB; 782615at2759; -.
DR PhylomeDB; Q8S8P5; -.
DR PRO; PR:Q8S8P5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8S8P5; baseline and differential.
DR Genevisible; Q8S8P5; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0010120; P:camalexin biosynthetic process; IMP:TAIR.
DR GO; GO:0070370; P:cellular heat acclimation; IMP:TAIR.
DR GO; GO:0034605; P:cellular response to heat; IMP: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:0010508; P:positive regulation of autophagy; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0009408; P:response to heat; 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 GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR GO; GO:0009627; P:systemic acquired resistance; 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; 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; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Plant defense; Reference proteome; Repeat; Stress response; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..519
FT /note="Probable WRKY transcription factor 33"
FT /id="PRO_0000133675"
FT DNA_BIND 178..242
FT /note="WRKY 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT DNA_BIND 356..421
FT /note="WRKY 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 214
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 237
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 239
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 387
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT MUTAGEN 359
FT /note="D->A: Weak interaction with VQ10 protein."
FT /evidence="ECO:0000269|PubMed:22535423"
FT MUTAGEN 362
FT /note="D->A: Loss of interaction with VQ10 protein."
FT /evidence="ECO:0000269|PubMed:22535423"
FT MUTAGEN 366
FT /note="R->Q: No effect on the interaction with VQ10
FT protein."
FT /evidence="ECO:0000269|PubMed:22535423"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:6J4G"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:6J4G"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:6J4G"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:6J4G"
SQ SEQUENCE 519 AA; 57179 MW; A90A6A8A2DF56DB1 CRC64;
MAASFLTMDN SRTRQNMNGS ANWSQQSGRT STSSLEDLEI PKFRSFAPSS ISISPSLVSP
STCFSPSLFL DSPAFVSSSA NVLASPTTGA LITNVTNQKG INEGDKSNNN NFNLFDFSFH
TQSSGVSAPT TTTTTTTTTT TTNSSIFQSQ EQQKKNQSEQ WSQTETRPNN QAVSYNGREQ
RKGEDGYNWR KYGQKQVKGS ENPRSYYKCT FPNCPTKKKV ERSLEGQITE IVYKGSHNHP
KPQSTRRSSS SSSTFHSAVY NASLDHNRQA SSDQPNSNNS FHQSDSFGMQ QEDNTTSDSV
GDDEFEQGSS IVSRDEEDCG SEPEAKRWKG DNETNGGNGG GSKTVREPRI VVQTTSDIDI
LDDGYRWRKY GQKVVKGNPN PRSYYKCTTI GCPVRKHVER ASHDMRAVIT TYEGKHNHDV
PAARGSGYAT NRAPQDSSSV PIRPAAIAGH SNYTTSSQAP YTLQMLHNNN TNTGPFGYAM
NNNNNNSNLQ TQQNFVGGGF SRAKEEPNEE TSFFDSFMP
