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TI11A_ARATH
ID   TI11A_ARATH             Reviewed;         274 AA.
AC   Q9LDU5; Q8LAR9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Protein TIFY 11A {ECO:0000303|PubMed:17499004};
DE   AltName: Full=Jasmonate ZIM domain-containing protein 5 {ECO:0000303|PubMed:17637675, ECO:0000303|PubMed:19151223};
GN   Name=TIFY11A {ECO:0000303|PubMed:17499004};
GN   Synonyms=JAZ5 {ECO:0000303|PubMed:17637675, ECO:0000303|PubMed:19151223};
GN   OrderedLocusNames=At1g17380 {ECO:0000312|Araport:AT1G17380};
GN   ORFNames=F1L3.3 {ECO:0000312|EMBL:AAF79491.1},
GN   F28G4.16 {ECO:0000312|EMBL:AAF97303.1};
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 [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   [2]
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   [3]
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   [4]
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   [5]
RP   INDUCTION BY JASMONATE.
RX   PubMed=17637677; DOI=10.1038/nature05960;
RA   Thines B., Katsir L., Melotto M., Niu Y., Mandaokar A., Liu G., Nomura K.,
RA   He S.Y., Howe G.A., Browse J.;
RT   "JAZ repressor proteins are targets of the SCF(COI1) complex during
RT   jasmonate signalling.";
RL   Nature 448:661-665(2007).
RN   [6]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17637675; DOI=10.1038/nature06006;
RA   Chini A., Fonseca S., Fernandez G., Adie B., Chico J.M., Lorenzo O.,
RA   Garcia-Casado G., Lopez-Vidriero I., Lozano F.M., Ponce M.R., Micol J.L.,
RA   Solano R.;
RT   "The JAZ family of repressors is the missing link in jasmonate
RT   signalling.";
RL   Nature 448:666-671(2007).
RN   [7]
RP   DOMAIN.
RX   PubMed=17675405; DOI=10.1105/tpc.107.050708;
RA   Yan Y., Stolz S., Chetelat A., Reymond P., Pagni M., Dubugnon L.,
RA   Farmer E.E.;
RT   "A downstream mediator in the growth repression limb of the jasmonate
RT   pathway.";
RL   Plant Cell 19:2470-2483(2007).
RN   [8]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=17499004; DOI=10.1016/j.tplants.2007.04.004;
RA   Vanholme B., Grunewald W., Bateman A., Kohchi T., Gheysen G.;
RT   "The tify family previously known as ZIM.";
RL   Trends Plant Sci. 12:239-244(2007).
RN   [9]
RP   INDUCTION BY WOUNDING AND HERBIVORY.
RX   PubMed=18223147; DOI=10.1104/pp.107.115691;
RA   Chung H.S., Koo A.J., Gao X., Jayanty S., Thines B., Jones A.D., Howe G.A.;
RT   "Regulation and function of Arabidopsis JASMONATE ZIM-domain genes in
RT   response to wounding and herbivory.";
RL   Plant Physiol. 146:952-964(2008).
RN   [10]
RP   FUNCTION, INTERACTION WITH TIFY10A/JAZ1; TIFY10B/JAZ2; TIFY11B/JAZ6;
RP   TIFY5A/JAZ8 AND TIFY3B/JAZ12, AND SUBUNIT.
RX   PubMed=19151223; DOI=10.1105/tpc.108.064097;
RA   Chung H.S., Howe G.A.;
RT   "A critical role for the TIFY motif in repression of jasmonate signaling by
RT   a stabilized splice variant of the JASMONATE ZIM-domain protein JAZ10 in
RT   Arabidopsis.";
RL   Plant Cell 21:131-145(2009).
RN   [11]
RP   INTERACTION WITH MYC2.
RX   PubMed=19309455; DOI=10.1111/j.1365-313x.2009.03852.x;
RA   Chini A., Fonseca S., Chico J.M., Fernandez-Calvo P., Solano R.;
RT   "The ZIM domain mediates homo- and heteromeric interactions between
RT   Arabidopsis JAZ proteins.";
RL   Plant J. 59:77-87(2009).
RN   [12]
RP   INTERACTION WITH AFPH2/NINJA.
RX   PubMed=20360743; DOI=10.1038/nature08854;
RA   Pauwels L., Barbero G.F., Geerinck J., Tilleman S., Grunewald W.,
RA   Perez A.C., Chico J.M., Bossche R.V., Sewell J., Gil E., Garcia-Casado G.,
RA   Witters E., Inze D., Long J.A., De Jaeger G., Solano R., Goossens A.;
RT   "NINJA connects the co-repressor TOPLESS to jasmonate signalling.";
RL   Nature 464:788-791(2010).
RN   [13]
RP   FUNCTION, INTERACTION WITH MYC2; MYC3; MYC4; TIFY10B/JAZ2; TIFY3B/JAZ12 AND
RP   AFPH2/NINJA, AND SUBUNIT.
RX   PubMed=21335373; DOI=10.1105/tpc.110.080788;
RA   Fernandez-Calvo P., Chini A., Fernandez-Barbero G., Chico J.M.,
RA   Gimenez-Ibanez S., Geerinck J., Eeckhout D., Schweizer F., Godoy M.,
RA   Franco-Zorrilla J.M., Pauwels L., Witters E., Puga M.I., Paz-Ares J.,
RA   Goossens A., Reymond P., De Jaeger G., Solano R.;
RT   "The Arabidopsis bHLH transcription factors MYC3 and MYC4 are targets of
RT   JAZ repressors and act additively with MYC2 in the activation of jasmonate
RT   responses.";
RL   Plant Cell 23:701-715(2011).
RN   [14]
RP   INTERACTION WITH PSEUDOMONAS SYRINGAE HOPZ1A (MICROBIAL INFECTION).
RC   STRAIN=cv. Columbia;
RX   PubMed=24204266; DOI=10.1371/journal.ppat.1003715;
RA   Jiang S., Yao J., Ma K.-W., Zhou H., Song J., He S.Y., Ma W.;
RT   "Bacterial effector activates jasmonate signaling by directly targeting JAZ
RT   transcriptional repressors.";
RL   PLoS Pathog. 9:e1003715-e1003715(2013).
CC   -!- FUNCTION: Repressor of jasmonate responses.
CC       {ECO:0000269|PubMed:19151223, ECO:0000269|PubMed:21335373}.
CC   -!- SUBUNIT: Homo- and heterodimer. Interacts with MYC2, MYC3, MYC4,
CC       AFPH2/NINJA, TIFY10A/JAZ1, TIFY10B/JAZ2, TIFY11B/JAZ6, TIFY5A/JAZ8 and
CC       TIFY3B/JAZ12. {ECO:0000269|PubMed:19151223,
CC       ECO:0000269|PubMed:19309455, ECO:0000269|PubMed:20360743,
CC       ECO:0000269|PubMed:21335373}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with the pathogenic
CC       Pseudomonas syringae HopZ1a protein. {ECO:0000269|PubMed:24204266}.
CC   -!- INTERACTION:
CC       Q9LDU5; Q9SV55: AFPH2; NbExp=10; IntAct=EBI-2312095, EBI-1787005;
CC       Q9LDU5; Q9ZNV8: AHP2; NbExp=3; IntAct=EBI-2312095, EBI-1100687;
CC       Q9LDU5; Q9LNJ5: BHLH13; NbExp=6; IntAct=EBI-2312095, EBI-4434261;
CC       Q9LDU5; Q42290: MPPbeta; NbExp=3; IntAct=EBI-2312095, EBI-1777952;
CC       Q9LDU5; Q39204: MYC2; NbExp=9; IntAct=EBI-2312095, EBI-1792336;
CC       Q9LDU5; O49687: MYC4; NbExp=3; IntAct=EBI-2312095, EBI-15406909;
CC       Q9LDU5; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-2312095, EBI-4426144;
CC       Q9LDU5; Q83YM6: avrPphE; Xeno; NbExp=3; IntAct=EBI-2312095, EBI-16093655;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC   -!- INDUCTION: (Microbial infection) Triggered to degradation by the
CC       pathogenic Pseudomonas syringae HopZ1a protein in a COI1-dependent
CC       manner, thereby activating host jasmonate signaling.
CC       {ECO:0000250|UniProtKB:Q9LMA8}.
CC   -!- INDUCTION: Up-regulated by jasmonate, wounding and herbivory.
CC       {ECO:0000269|PubMed:17637677, ECO:0000269|PubMed:18223147}.
CC   -!- DOMAIN: The jas domain (182-206) is required for interaction with COI1
CC       and Pseudomonas syringae HopZ1a. {ECO:0000250|UniProtKB:Q7XPM8,
CC       ECO:0000250|UniProtKB:Q9C9E3}.
CC   -!- PTM: (Microbial infection) Acetylated by Pseudomonas syringae HopZ1a.
CC       {ECO:0000250|UniProtKB:Q9C9E3}.
CC   -!- PTM: Ubiquitinated. Targeted for degradation by the SCF(COI1) E3
CC       ubiquitin ligase-proteasome pathway during jasmonate signaling.
CC       {ECO:0000250|UniProtKB:Q7XPM8}.
CC   -!- SIMILARITY: Belongs to the TIFY/JAZ family. {ECO:0000305}.
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DR   EMBL; AC007843; AAF97303.1; -; Genomic_DNA.
DR   EMBL; AC022492; AAF79491.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29581.1; -; Genomic_DNA.
DR   EMBL; BT000430; AAN17407.1; -; mRNA.
DR   EMBL; BT002543; AAO00903.1; -; mRNA.
DR   EMBL; AY087653; AAM65191.1; -; mRNA.
DR   RefSeq; NP_564019.1; NM_101599.3.
DR   AlphaFoldDB; Q9LDU5; -.
DR   SMR; Q9LDU5; -.
DR   BioGRID; 23550; 26.
DR   DIP; DIP-53275N; -.
DR   ELM; Q9LDU5; -.
DR   IntAct; Q9LDU5; 15.
DR   STRING; 3702.AT1G17380.1; -.
DR   PaxDb; Q9LDU5; -.
DR   PRIDE; Q9LDU5; -.
DR   EnsemblPlants; AT1G17380.1; AT1G17380.1; AT1G17380.
DR   GeneID; 838310; -.
DR   Gramene; AT1G17380.1; AT1G17380.1; AT1G17380.
DR   KEGG; ath:AT1G17380; -.
DR   Araport; AT1G17380; -.
DR   TAIR; locus:2018804; AT1G17380.
DR   eggNOG; ENOG502S4J6; Eukaryota.
DR   HOGENOM; CLU_051749_1_0_1; -.
DR   InParanoid; Q9LDU5; -.
DR   OMA; YNEFPAD; -.
DR   OrthoDB; 1280219at2759; -.
DR   PhylomeDB; Q9LDU5; -.
DR   PRO; PR:Q9LDU5; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LDU5; baseline and differential.
DR   Genevisible; Q9LDU5; AT.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0031347; P:regulation of defense response; IBA:GO_Central.
DR   GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR   GO; GO:0009611; P:response to wounding; IBA:GO_Central.
DR   InterPro; IPR018467; CCT_CS.
DR   InterPro; IPR040390; TIFY/JAZ.
DR   InterPro; IPR010399; Tify_dom.
DR   PANTHER; PTHR33077; PTHR33077; 1.
DR   Pfam; PF09425; Jas_motif; 1.
DR   Pfam; PF06200; tify; 1.
DR   SMART; SM00979; TIFY; 1.
DR   PROSITE; PS51320; TIFY; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Jasmonic acid signaling pathway; Nucleus;
KW   Plant defense; Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..274
FT                   /note="Protein TIFY 11A"
FT                   /id="PRO_0000300654"
FT   DOMAIN          92..127
FT                   /note="Tify"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00650"
FT   REGION          49..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          206..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          161..185
FT                   /evidence="ECO:0000255"
FT   MOTIF           182..206
FT                   /note="Jas"
FT                   /evidence="ECO:0000255"
FT   MOTIF           183..190
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        227..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..274
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        97
FT                   /note="S -> L (in Ref. 4; AAM65191)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165
FT                   /note="L -> P (in Ref. 4; AAM65191)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   274 AA;  30343 MW;  54A55E02C18E5BAF CRC64;
     MSSSNENAKA QAPEKSDFTR RCSLLSRYLK EKGSFGNIDL GLYRKPDSSL ALPGKFDPPG
     KQNAMHKAGH SKGEPSTSSG GKVKDVADLS ESQPGSSQLT IFFGGKVLVY NEFPVDKAKE
     IMEVAKQAKP VTEINIQTPI NDENNNNKSS MVLPDLNEPT DNNHLTKEQQ QQQEQNQIVE
     RIARRASLHR FFAKRKDRAV ARAPYQVNQN AGHHRYPPKP EIVTGQPLEA GQSSQRPPDN
     AIGQTMAHIK SDGDKDDIMK IEEGQSSKDL DLRL
 
 
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