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WRK10_ARATH
ID   WRK10_ARATH             Reviewed;         485 AA.
AC   Q9LG05; Q1PFK1; Q8VWQ3;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Probable WRKY transcription factor 10;
DE   AltName: Full=Protein MINISEED 3;
DE   AltName: Full=WRKY DNA-binding protein 10;
GN   Name=WRKY10; Synonyms=MINI3; OrderedLocusNames=At1g55600; ORFNames=F20N2.3;
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 WRKY10.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND MUTAGENESIS OF GLU-344.
RX   PubMed=16293693; DOI=10.1073/pnas.0508418102;
RA   Luo M., Dennis E.S., Berger F., Peacock W.J., Chaudhury A.;
RT   "MINISEED3 (MINI3), a WRKY family gene, and HAIKU2 (IKU2), a leucine-rich
RT   repeat (LRR) KINASE gene, are regulators of seed size in Arabidopsis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:17531-17536(2005).
RN   [6]
RP   INTERACTION WITH IKU1.
RX   PubMed=20545893; DOI=10.1111/j.1365-313x.2010.04271.x;
RA   Wang A., Garcia D., Zhang H., Feng K., Chaudhury A., Berger F.,
RA   Peacock W.J., Dennis E.S., Luo M.;
RT   "The VQ motif protein IKU1 regulates endosperm growth and seed size in
RT   Arabidopsis.";
RL   Plant J. 63:670-679(2010).
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 seed size by negatively
CC       regulating the cellularization of syncytial endosperm
CC       (PubMed:16293693). {ECO:0000250|UniProtKB:Q9SI37,
CC       ECO:0000269|PubMed:16293693}.
CC   -!- SUBUNIT: Interacts with IKU1. {ECO:0000269|PubMed:20545893}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00223,
CC       ECO:0000269|PubMed:16293693}.
CC   -!- TISSUE SPECIFICITY: Expressed in male gametophytes (pollen) and in the
CC       endosperm of fertilized ovules. {ECO:0000269|PubMed:16293693}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the endosperm of embryo from the two
CC       nuclei stage to the late globular embryo stage, including the endosperm
CC       cellularization time. {ECO:0000269|PubMed:16293693}.
CC   -!- SIMILARITY: Belongs to the WRKY group I family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF79511.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY071851; AAL61861.1; -; mRNA.
DR   EMBL; AC002328; AAF79511.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE33270.1; -; Genomic_DNA.
DR   EMBL; DQ446362; ABE65713.1; -; mRNA.
DR   RefSeq; NP_175956.1; NM_104436.2.
DR   AlphaFoldDB; Q9LG05; -.
DR   SMR; Q9LG05; -.
DR   BioGRID; 27234; 1.
DR   STRING; 3702.AT1G55600.1; -.
DR   PaxDb; Q9LG05; -.
DR   PRIDE; Q9LG05; -.
DR   ProteomicsDB; 232452; -.
DR   EnsemblPlants; AT1G55600.1; AT1G55600.1; AT1G55600.
DR   GeneID; 842009; -.
DR   Gramene; AT1G55600.1; AT1G55600.1; AT1G55600.
DR   KEGG; ath:AT1G55600; -.
DR   Araport; AT1G55600; -.
DR   TAIR; locus:2020467; AT1G55600.
DR   eggNOG; ENOG502QU86; Eukaryota.
DR   HOGENOM; CLU_027756_0_0_1; -.
DR   InParanoid; Q9LG05; -.
DR   OMA; DYATTTI; -.
DR   OrthoDB; 847761at2759; -.
DR   PhylomeDB; Q9LG05; -.
DR   PRO; PR:Q9LG05; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LG05; baseline and differential.
DR   Genevisible; Q9LG05; AT.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0009960; P:endosperm development; 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..485
FT                   /note="Probable WRKY transcription factor 10"
FT                   /id="PRO_0000133652"
FT   DNA_BIND        301..366
FT                   /note="WRKY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00223"
FT   REGION          43..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          215..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          358..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..263
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..414
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         332
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT   BINDING         337
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT   BINDING         361
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT   BINDING         363
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SI37"
FT   MUTAGEN         344
FT                   /note="E->K: In mini3-1; reduced seed size and earlier
FT                   endosperm cellularization."
FT                   /evidence="ECO:0000269|PubMed:16293693"
SQ   SEQUENCE   485 AA;  54552 MW;  3D96CE29CC9BFAC0 CRC64;
     MSDFDENFIE MTSYWAPPSS PSPRTILAML EQTDNGLNPI SEIFPQESLP RDHTDQSGQR
     SGLRERLAAR VGFNLPTLNT EENMSPLDAF FRSSNVPNSP VVAISPGFSP SALLHTPNMV
     SDSSQIIPPS SATNYGPLEM VETSGEDNAA MMMFNNDLPY QPYNVDLPSL EVFDDIATEE
     SFYIPSYEPH VDPIGTPLVT SFESELVDDA HTDIISIEDS ESEDGNKDDD DEDFQYEDED
     EDQYDQDQDV DEDEEEEKDE DNVALDDPQP PPPKRRRYEV SNMIGATRTS KTQRIILQME
     SDEDNPNDGY RWRKYGQKVV KGNPNPRSYF KCTNIECRVK KHVERGADNI KLVVTTYDGI
     HNHPSPPARR SNSSSRNRSA GATIPQNQND RTSRLGRAPP TPTPPTPPPS SYTPEEMRPF
     SSLATEIDLT EVYMTGISML PNIPVYENSG FMYQNDEPTM NAMPDGSDVY DGIMERLYFK
     FGVDM
 
 
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