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WRK42_ARATH
ID   WRK42_ARATH             Reviewed;         528 AA.
AC   Q9XEC3;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=WRKY transcription factor 42 {ECO:0000303|Ref.1};
DE   AltName: Full=WRKY DNA-binding protein 42 {ECO:0000303|Ref.1};
GN   Name=WRKY42 {ECO:0000303|Ref.1};
GN   OrderedLocusNames=At4g04450 {ECO:0000312|Araport:AT4G04450};
GN   ORFNames=T26N6.6 {ECO:0000312|EMBL:AAD29757.1};
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 WRKY42.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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   FUNCTION, AND DEGRADATION.
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. Interacts specifically with the W box
CC       (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-
CC       acting element (By similarity). Modulates phosphate homeostasis and Pi
CC       translocation by regulating PHO1 expression (PubMed:25733771).
CC       {ECO:0000250, ECO:0000269|PubMed:25733771}.
CC   -!- INTERACTION:
CC       Q9XEC3; Q9ZSI7: WRKY47; NbExp=3; IntAct=EBI-15196907, EBI-2367993;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00223}.
CC   -!- PTM: Degraded through the 26S proteasome pathway during Pi starvation
CC       (PubMed:25733771). {ECO:0000269|PubMed:25733771}.
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DR   EMBL; AY052650; AAL11011.1; -; mRNA.
DR   EMBL; AF076243; AAD29757.1; -; Genomic_DNA.
DR   EMBL; AL161500; CAB77913.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE82389.1; -; Genomic_DNA.
DR   PIR; C85056; C85056.
DR   RefSeq; NP_192354.1; NM_116683.3.
DR   AlphaFoldDB; Q9XEC3; -.
DR   SMR; Q9XEC3; -.
DR   BioGRID; 11086; 13.
DR   IntAct; Q9XEC3; 12.
DR   STRING; 3702.AT4G04450.1; -.
DR   PaxDb; Q9XEC3; -.
DR   PRIDE; Q9XEC3; -.
DR   ProteomicsDB; 234365; -.
DR   EnsemblPlants; AT4G04450.1; AT4G04450.1; AT4G04450.
DR   GeneID; 825775; -.
DR   Gramene; AT4G04450.1; AT4G04450.1; AT4G04450.
DR   KEGG; ath:AT4G04450; -.
DR   Araport; AT4G04450; -.
DR   TAIR; locus:2137179; AT4G04450.
DR   eggNOG; ENOG502QSY8; Eukaryota.
DR   HOGENOM; CLU_021824_3_1_1; -.
DR   InParanoid; Q9XEC3; -.
DR   OMA; TDHINIG; -.
DR   OrthoDB; 885744at2759; -.
DR   PhylomeDB; Q9XEC3; -.
DR   PRO; PR:Q9XEC3; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9XEC3; baseline and differential.
DR   Genevisible; Q9XEC3; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
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; 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; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..528
FT                   /note="WRKY transcription factor 42"
FT                   /id="PRO_0000133683"
FT   DNA_BIND        286..352
FT                   /note="WRKY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        200..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   528 AA;  58071 MW;  763AABB88203A2B9 CRC64;
     MFRFPVSLGG GPRENLKPSD EQHQRAVVNE VDFFRSAEKR DRVSREEQNI IADETHRVHV
     KRENSRVDDH DDRSTDHINI GLNLLTANTG SDESMVDDGL SVDMEEKRTK CENAQLREEL
     KKASEDNQRL KQMLSQTTNN FNSLQMQLVA VMRQQEDHHH LATTENNDNV KNRHEVPEMV
     PRQFIDLGPH SDEVSSEERT TVRSGSPPSL LEKSSSRQNG KRVLVREESP ETESNGWRNP
     NKVPKHHASS SICGGNGSEN ASSKVIEQAA AEATMRKARV SVRARSEAPM LSDGCQWRKY
     GQKMAKGNPC PRAYYRCTMA VGCPVRKQVQ RCAEDRTILI TTYEGNHNHP LPPAAMNMAS
     TTTAAASMLL SGSTMSNQDG LMNPTNLLAR TILPCSSSMA TISASAPFPT ITLDLTESPN
     GNNPTNNPLM QFSQRSGLVE LNQSVLPHMM GQALYYNQQS KFSGLHMPSQ PLNAGESVSA
     ATAAIASNPN FAAALAAAIT SIINGSNNQQ NGNNNNSNVT TSNVDNRQ
 
 
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