WRKY2_ARATH
ID WRKY2_ARATH Reviewed; 687 AA.
AC Q9FG77;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable WRKY transcription factor 2 {ECO:0000303|Ref.1};
DE AltName: Full=WRKY DNA-binding protein 2 {ECO:0000303|Ref.1};
GN Name=WRKY2 {ECO:0000303|Ref.1};
GN OrderedLocusNames=At5g56270 {ECO:0000312|Araport:AT5G56270};
GN ORFNames=K24C1.9, MXK23.1 {ECO:0000312|EMBL:BAB08871.1};
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].
RC STRAIN=cv. Columbia; TISSUE=Flower;
RA Ulker B., Kushnir S., Somssich I.E.;
RT "Arabidopsis thaliana transcription factor WRKY2.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 TISSUE SPECIFICITY.
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21316593; DOI=10.1016/j.devcel.2011.01.009;
RA Ueda M., Zhang Z., Laux T.;
RT "Transcriptional activation of Arabidopsis axis patterning genes WOX8/9
RT links zygote polarity to embryo development.";
RL Dev. Cell 20:264-270(2011).
CC -!- FUNCTION: Transcription factor. Regulates WOX8 and WOX9 expression and
CC basal cell division patterns during early embryogenesis. Interacts
CC specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring
CC elicitor-responsive cis-acting element. Required to repolarize the
CC zygote from a transient symmetric state. {ECO:0000269|PubMed:21316593}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9SI37}.
CC -!- TISSUE SPECIFICITY: Low expression in senescent leaves
CC (PubMed:11722756). Expressed in both the unfertilized egg cell and the
CC pollen tube (PubMed:21316593). {ECO:0000269|PubMed:11722756,
CC ECO:0000269|PubMed:21316593}.
CC -!- DISRUPTION PHENOTYPE: Strong defects in embryo development.
CC {ECO:0000269|PubMed:21316593}.
CC -!- SIMILARITY: Belongs to the WRKY group I family. {ECO:0000305}.
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DR EMBL; AF418308; AAL13039.1; -; mRNA.
DR EMBL; AB026656; BAB08871.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96743.1; -; Genomic_DNA.
DR EMBL; AY096493; AAM20132.1; -; mRNA.
DR EMBL; AY123006; AAM67539.1; -; mRNA.
DR RefSeq; NP_200438.1; NM_125010.3.
DR PDB; 6J4F; X-ray; 2.40 A; B/F=259-331.
DR PDBsum; 6J4F; -.
DR AlphaFoldDB; Q9FG77; -.
DR SMR; Q9FG77; -.
DR BioGRID; 20970; 2.
DR IntAct; Q9FG77; 2.
DR STRING; 3702.AT5G56270.1; -.
DR iPTMnet; Q9FG77; -.
DR PaxDb; Q9FG77; -.
DR PRIDE; Q9FG77; -.
DR ProteomicsDB; 246482; -.
DR EnsemblPlants; AT5G56270.1; AT5G56270.1; AT5G56270.
DR GeneID; 835726; -.
DR Gramene; AT5G56270.1; AT5G56270.1; AT5G56270.
DR KEGG; ath:AT5G56270; -.
DR Araport; AT5G56270; -.
DR TAIR; locus:2177596; AT5G56270.
DR eggNOG; ENOG502QU86; Eukaryota.
DR HOGENOM; CLU_012086_3_0_1; -.
DR InParanoid; Q9FG77; -.
DR OMA; WKHENLE; -.
DR OrthoDB; 478624at2759; -.
DR PhylomeDB; Q9FG77; -.
DR PRO; PR:Q9FG77; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FG77; baseline and differential.
DR Genevisible; Q9FG77; 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:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:TAIR.
DR GO; GO:0009942; P:longitudinal axis specification; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..687
FT /note="Probable WRKY transcription factor 2"
FT /id="PRO_0000133645"
FT DNA_BIND 267..331
FT /note="WRKY 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT DNA_BIND 481..546
FT /note="WRKY 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT REGION 197..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 512
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 517
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 541
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 543
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:6J4F"
FT TURN 287..290
FT /evidence="ECO:0007829|PDB:6J4F"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:6J4F"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:6J4F"
FT STRAND 317..324
FT /evidence="ECO:0007829|PDB:6J4F"
SQ SEQUENCE 687 AA; 74561 MW; D47EAB1FB0C6335F CRC64;
MAGFDENVAV MGEWVPRSPS PGTLFSSAIG EEKSSKRVLE RELSLNHGQV IGLEEDTSSN
HNKDSSQSNV FRGGLSERIA ARAGFNAPRL NTENIRTNTD FSIDSNLRSP CLTISSPGLS
PATLLESPVF LSNPLAQPSP TTGKFPFLPG VNGNALSSEK AKDEFFDDIG ASFSFHPVSR
SSSSFFQGTT EMMSVDYGNY NNRSSSHQSA EEVKPGSENI ESSNLYGIET DNQNGQNKTS
DVTTNTSLET VDHQEEEEEQ RRGDSMAGGA PAEDGYNWRK YGQKLVKGSE YPRSYYKCTN
PNCQVKKKVE RSREGHITEI IYKGAHNHLK PPPNRRSGMQ VDGTEQVEQQ QQQRDSAATW
VSCNNTQQQG GSNENNVEEG STRFEYGNQS GSIQAQTGGQ YESGDPVVVV DASSTFSNDE
DEDDRGTHGS VSLGYDGGGG GGGGEGDESE SKRRKLEAFA AEMSGSTRAI REPRVVVQTT
SDVDILDDGY RWRKYGQKVV KGNPNPRSYY KCTAPGCTVR KHVERASHDL KSVITTYEGK
HNHDVPAARN SSHGGGGDSG NGNSGGSAAV SHHYHNGHHS EPPRGRFDRQ VTTNNQSPFS
RPFSFQPHLG PPSGFSFGLG QTGLVNLSMP GLAYGQGKMP GLPHPYMTQP VGMSEAMMQR
GMEPKVEPVS DSGQSVYNQI MSRLPQI
