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WRK71_ORYSI
ID   WRK71_ORYSI             Reviewed;         348 AA.
AC   Q6IEL0;
DT   07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 124.
DE   RecName: Full=WRKY transcription factor WRKY71 {ECO:0000303|PubMed:15047897};
DE            Short=OsWRKY71 {ECO:0000303|PubMed:15047897};
GN   Name=WRKY71 {ECO:0000303|PubMed:15047897};
GN   ORFNames=OsI_06106 {ECO:0000312|EMBL:EAY84736.1};
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, AND REGULATION BY GIBBERELLIC ACID.
RX   PubMed=15047897; DOI=10.1104/pp.103.034967;
RA   Zhang Z.-L., Xie Z., Zou X., Casaretto J., Ho T.-H.D., Shen Q.J.;
RT   "A rice WRKY gene encodes a transcriptional repressor of the gibberellin
RT   signaling pathway in aleurone cells.";
RL   Plant Physiol. 134:1500-1513(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY DEFENSE SIGNALING
RP   MOLECULES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Guang-Lu-Ai No.4; TISSUE=Leaf;
RX   PubMed=16919842; DOI=10.1016/j.jplph.2006.07.006;
RA   Liu X., Bai X., Wang X., Chu C.;
RT   "OsWRKY71, a rice transcription factor, is involved in rice defense
RT   response.";
RL   J. Plant Physiol. 164:969-979(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15618416; DOI=10.1104/pp.104.054312;
RA   Xie Z., Zhang Z.-L., Zou X., Huang J., Ruas P., Thompson D., Shen Q.J.;
RT   "Annotations and functional analyses of the rice WRKY gene superfamily
RT   reveal positive and negative regulators of abscisic acid signaling in
RT   aleurone cells.";
RL   Plant Physiol. 137:176-189(2005).
RN   [5]
RP   INDUCTION BY ABA.
RC   STRAIN=cv. IR29, and cv. Pokkali;
RX   PubMed=25110688; DOI=10.1155/2014/706890;
RA   Basu S., Roychoudhury A.;
RT   "Expression profiling of abiotic stress-inducible genes in response to
RT   multiple stresses in rice (Oryza sativa L.) varieties with contrasting
RT   level of stress tolerance.";
RL   Biomed. Res. Int. 2014:706890-706890(2014).
CC   -!- FUNCTION: Transcription repressor. Interacts specifically with the W
CC       box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive
CC       cis-acting element. Represses specifically gibberellic acid (GA)-
CC       induced promoters in aleurone cells, probably by interfering with GAM1
CC       (PubMed:15047897). Regulates, probably indirectly, the activation of
CC       defense-related genes such as GF14E during defense response (By
CC       similarity). Modulates plant innate immunity against X.oryzae pv.
CC       oryzae (Xoo) (By similarity). Confers resistance to the virulent
CC       bacterial pathogen X.oryzae pv. oryzae (Xoo) 13751, probably via the
CC       regulation of NPR1 and PR1b defense signaling pathways
CC       (PubMed:16919842). {ECO:0000250|UniProtKB:Q6QHD1,
CC       ECO:0000269|PubMed:15047897, ECO:0000269|PubMed:16919842}.
CC   -!- SUBUNIT: Interacts with WRKY51; this interaction promotes W box binding
CC       of the complex WRKY51/WRKY71 in a zinc ion-dependent manner.
CC       {ECO:0000250|UniProtKB:Q6QHD1}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00223,
CC       ECO:0000269|PubMed:15047897}. Note=Localized in nuclei of aleurone
CC       cells. {ECO:0000269|PubMed:15047897}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in aleurone cells
CC       (PubMed:15047897). In seeds, predominantly present in the plumule,
CC       radicle and scutellum of the embryo. Expressed in roots, stems, young
CC       leaves and spikelets (PubMed:16919842). {ECO:0000269|PubMed:15047897,
CC       ECO:0000269|PubMed:16919842}.
CC   -!- INDUCTION: Induced by biotic elicitors (e.g. fungal chitin
CC       oligosaccharide and fungal cerebroside elicitors) and pathogen
CC       infection (e.g. the compatible pathogenic fungus M.grisea race 007,
CC       M.grisea crabgrass BR29). Accumulates in response to M.oryzae (By
CC       similarity). Triggered by defense signaling molecules, such as
CC       salicylic acid (SA), methyl jasmonate (MeJA), 1-aminocyclo-propane-1-
CC       carboxylic acid (ACC), wounding and pathogen infection (e.g. X.oryzae)
CC       (PubMed:16919842). Repressed by gibberellic acid (GA) (at protein
CC       level) (PubMed:15047897). Induced by abscisic acid (ABA) in aleurone
CC       cells, roots and leaves (PubMed:25110688). Accumulates in response to
CC       uniconazole, a GA biosynthesis inhibitor. Triggered strongly by cold in
CC       leaves, stems and developing spikes, but moderately by drought and salt
CC       stresses (By similarity). {ECO:0000250|UniProtKB:Q6QHD1,
CC       ECO:0000269|PubMed:15047897, ECO:0000269|PubMed:16919842,
CC       ECO:0000269|PubMed:25110688}.
CC   -!- DOMAIN: The WRKY domain (213-266) is required to bind DNA.
CC       {ECO:0000250|UniProtKB:Q6QHD1}.
CC   -!- DOMAIN: The C-terminal region (267-348) is required for the repressing
CC       activity on gibberellic acid (GA)-induced promoters.
CC       {ECO:0000250|UniProtKB:Q6QHD1}.
CC   -!- SIMILARITY: Belongs to the WRKY group II-a family. {ECO:0000305}.
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DR   EMBL; BK005074; DAA05136.1; -; Genomic_DNA.
DR   EMBL; AY676927; AAT84158.1; -; mRNA.
DR   EMBL; CM000127; EAY84736.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6IEL0; -.
DR   SMR; Q6IEL0; -.
DR   STRING; 39946.Q6IEL0; -.
DR   EnsemblPlants; BGIOSGA007670-TA; BGIOSGA007670-PA; BGIOSGA007670.
DR   Gramene; BGIOSGA007670-TA; BGIOSGA007670-PA; BGIOSGA007670.
DR   HOGENOM; CLU_047067_0_0_1; -.
DR   OMA; DPWISTQ; -.
DR   Proteomes; UP000007015; Chromosome 2.
DR   GO; GO:0005634; C:nucleus; IDA:Gramene.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:Gramene.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0006952; P:defense response; IMP:Gramene.
DR   GO; GO:0050832; P:defense response to fungus; IEA:EnsemblPlants.
DR   GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0009685; P:gibberellin metabolic process; IEP:Gramene.
DR   GO; GO:0009938; P:negative regulation of gibberellic acid mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:EnsemblPlants.
DR   GO; GO:0031347; P:regulation of defense response; IMP:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:Gramene.
DR   GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR   GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR   GO; GO:0010200; P:response to chitin; ISS:UniProtKB.
DR   GO; GO:0009409; P:response to cold; IEA:EnsemblPlants.
DR   GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR   GO; GO:0009739; P:response to gibberellin; IDA:UniProtKB.
DR   GO; GO:0009753; P:response to jasmonic acid; IEP:UniProtKB.
DR   GO; GO:0002237; P:response to molecule of bacterial origin; IEA:EnsemblPlants.
DR   GO; GO:0002238; P:response to molecule of fungal origin; IEA:EnsemblPlants.
DR   GO; GO:0009751; P:response to salicylic acid; IEP:UniProtKB.
DR   GO; GO:0009651; P:response to salt stress; IEA:EnsemblPlants.
DR   GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
DR   GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
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   Coiled coil; DNA-binding; Gibberellin signaling pathway; Nucleus;
KW   Plant defense; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..348
FT                   /note="WRKY transcription factor WRKY71"
FT                   /id="PRO_0000436959"
FT   DNA_BIND        187..253
FT                   /note="WRKY"
FT                   /evidence="ECO:0000250|UniProtKB:Q6QHD1,
FT                   ECO:0000255|PROSITE-ProRule:PRU00223"
FT   REGION          91..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          267..348
FT                   /note="Transcription repression of gibberellic acid (GA)-
FT                   induced promoters"
FT                   /evidence="ECO:0000250|UniProtKB:Q6QHD1"
FT   COILED          50..84
FT                   /evidence="ECO:0000255"
FT   MOTIF           116..122
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        91..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..139
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   348 AA;  37258 MW;  BA7BC1EDF6C1E28C CRC64;
     MDPWISTQPS LSLDLRVGLP ATAAVAMVKP KVLVEEDFFH QQPLKKDPEV AALEAELKRM
     GAENRQLSEM LAAVAAKYEA LQSQFSDMVT ASANNGGGGG NNQSSTSEGG SVSPSRKRKS
     ESLDDSPPPP PPPHPHAAPH HMHVMPGAAA AGYADQTECT SGEPCKRIRE ECKPKISKLY
     VHADPSDLSL VVKDGYQWRK YGQKVTKDNP CPRAYFRCSF APACPVKKKV QRSAEDNTIL
     VATYEGEHNH GQPPPPLQSA AQNSDGSGKS AGKPPHAPAA APPAPVVPHR QHEPVVVNGE
     QQAAAASEMI RRNLAEQMAM TLTRDPSFKA ALVTALSGRI LELSPTKD
 
 
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