WRK45_ARATH
ID WRK45_ARATH Reviewed; 147 AA.
AC Q9S763; Q8LET6; Q96308;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable WRKY transcription factor 45;
DE AltName: Full=AT.I.24-4;
DE AltName: Full=WRKY DNA-binding protein 45;
GN Name=WRKY45; OrderedLocusNames=At3g01970; ORFNames=F1C9.25, F28J7.30;
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 Kushnir S., Ulker B., Somssich I.E.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE OF 68-121.
RC STRAIN=cv. Columbia;
RX PubMed=2615757; DOI=10.1007/bf00261164;
RA Axelos M., Bardet C., Liboz T., Le van Thai A., Curie C., Lescure B.;
RT "The gene family encoding the Arabidopsis thaliana translation elongation
RT factor EF-1 alpha: molecular cloning, characterization and expression.";
RL Mol. Gen. Genet. 219:106-112(1989).
CC -!- FUNCTION: Transcription factor. Interacts specifically with the W box
CC (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-
CC acting element. {ECO:0000250|UniProtKB:Q9SI37}.
CC -!- INTERACTION:
CC Q9S763; Q8VZI9: At3g11100; NbExp=4; IntAct=EBI-15195723, EBI-1998580;
CC Q9S763; A0A178VL61: AXX17_At2g18500; NbExp=3; IntAct=EBI-15195723, EBI-25517681;
CC Q9S763; Q8GXL7: GATA24; NbExp=6; IntAct=EBI-15195723, EBI-4426127;
CC Q9S763; Q9LQF0: TCP23; NbExp=6; IntAct=EBI-15195723, EBI-15192297;
CC Q9S763; Q8LPR5: TCP4; NbExp=3; IntAct=EBI-15195723, EBI-15192325;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9SI37}.
CC -!- SIMILARITY: Belongs to the WRKY group I family. {ECO:0000305}.
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DR EMBL; AF426251; AAL29428.1; -; mRNA.
DR EMBL; AC010797; AAF03448.1; -; Genomic_DNA.
DR EMBL; AC011664; AAF14838.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73742.1; -; Genomic_DNA.
DR EMBL; AK118457; BAC43065.1; -; mRNA.
DR EMBL; AY085246; AAM62478.1; -; mRNA.
DR EMBL; U63815; AAB07876.1; -; Genomic_DNA.
DR RefSeq; NP_186846.1; NM_111063.4.
DR AlphaFoldDB; Q9S763; -.
DR SMR; Q9S763; -.
DR BioGRID; 6603; 29.
DR IntAct; Q9S763; 24.
DR STRING; 3702.AT3G01970.1; -.
DR PaxDb; Q9S763; -.
DR PRIDE; Q9S763; -.
DR ProteomicsDB; 246439; -.
DR EnsemblPlants; AT3G01970.1; AT3G01970.1; AT3G01970.
DR GeneID; 821270; -.
DR Gramene; AT3G01970.1; AT3G01970.1; AT3G01970.
DR KEGG; ath:AT3G01970; -.
DR Araport; AT3G01970; -.
DR TAIR; locus:2078703; AT3G01970.
DR eggNOG; ENOG502RZAJ; Eukaryota.
DR HOGENOM; CLU_073202_4_0_1; -.
DR InParanoid; Q9S763; -.
DR OMA; EARYAFQ; -.
DR OrthoDB; 847761at2759; -.
DR PhylomeDB; Q9S763; -.
DR PRO; PR:Q9S763; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S763; baseline and differential.
DR Genevisible; Q9S763; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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:0006817; P:phosphate ion transport; 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; PTHR31221; PTHR31221; 1.
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 DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..147
FT /note="Probable WRKY transcription factor 45"
FT /id="PRO_0000133686"
FT DNA_BIND 59..124
FT /note="WRKY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT REGION 21..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT CONFLICT 30
FT /note="A -> S (in Ref. 5; AAM62478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 17225 MW; CD8C6C70BCF3E87D CRC64;
MEDRRCDVLF PCSSSVDPRL TEFHGVDNSA QPTTSSEEKP RSKKKKKERE ARYAFQTRSQ
VDILDDGYRW RKYGQKAVKN NPFPRSYYKC TEEGCRVKKQ VQRQWGDEGV VVTTYQGVHT
HAVDKPSDNF HHILTQMHIF PPFCLKE
