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TI10A_ARATH
ID   TI10A_ARATH             Reviewed;         253 AA.
AC   Q9LMA8; Q8LAG5; Q93Z09;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Protein TIFY 10A {ECO:0000303|PubMed:17499004};
DE   AltName: Full=Jasmonate ZIM domain-containing protein 1 {ECO:0000303|PubMed:17637675, ECO:0000303|PubMed:19151223};
GN   Name=TIFY10A {ECO:0000303|PubMed:17499004};
GN   Synonyms=JAZ1 {ECO:0000303|PubMed:17637675, ECO:0000303|PubMed:19151223};
GN   OrderedLocusNames=At1g19180 {ECO:0000312|Araport:AT1G19180};
GN   ORFNames=T29M8.5 {ECO:0000312|EMBL:AAF82229.1};
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   FUNCTION, MUTAGENESIS OF 202-PRO--LEU-228, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND 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   FUNCTION, INTERACTION WITH COI1 AND MYC2, 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   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, 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   INTERACTION WITH COI1 AND MYC2, DOMAIN, AND MUTAGENESIS OF 205-ARG-ARG-206.
RX   PubMed=18547396; DOI=10.1111/j.1365-313x.2008.03566.x;
RA   Melotto M., Mecey C., Niu Y., Chung H.S., Katsir L., Yao J., Zeng W.,
RA   Thines B., Staswick P., Browse J., Howe G.A., He S.Y.;
RT   "A critical role of two positively charged amino acids in the Jas motif of
RT   Arabidopsis JAZ proteins in mediating coronatine- and jasmonoyl isoleucine-
RT   dependent interactions with the COI1 F-box protein.";
RL   Plant J. 55:979-988(2008).
RN   [10]
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   [11]
RP   FUNCTION, INTERACTION WITH TIFY10B/JAZ2; TIFY6B/JAZ3; TIFY6A/JAZ4;
RP   TIFY11A/JAZ5; TIFY11B/JAZ6; TIFY5A/JAZ8; TIFY7/JAZ9; TIFY9/JAZ10;
RP   TIFY3A/JAZ11 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   [12]
RP   INTERACTION WITH MYC2, AND SUBUNIT.
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   [13]
RP   INTERACTION WITH TIFY3B/JAZ12; ATR2/MYC3; COI1 AND 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   [14]
RP   INTERACTION WITH MYC2; MYC3; MYC4 AND AFPH2.
RX   PubMed=21321051; DOI=10.1093/jxb/erq408;
RA   Niu Y., Figueroa P., Browse J.;
RT   "Characterization of JAZ-interacting bHLH transcription factors that
RT   regulate jasmonate responses in Arabidopsis.";
RL   J. Exp. Bot. 62:2143-2154(2011).
RN   [15]
RP   INTERACTION WITH MYB21 AND MYB24.
RX   PubMed=21447791; DOI=10.1105/tpc.111.083089;
RA   Song S., Qi T., Huang H., Ren Q., Wu D., Chang C., Peng W., Liu Y.,
RA   Peng J., Xie D.;
RT   "The Jasmonate-ZIM domain proteins interact with the R2R3-MYB transcription
RT   factors MYB21 and MYB24 to affect Jasmonate-regulated stamen development in
RT   Arabidopsis.";
RL   Plant Cell 23:1000-1013(2011).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 200-226 IN COMPLEX WITH
RP   JASMONOYL-ISOLEUCINE AND CORONATINE, AND INTERACTION WITH COI1.
RX   PubMed=20927106; DOI=10.1038/nature09430;
RA   Sheard L.B., Tan X., Mao H., Withers J., Ben-Nissan G., Hinds T.R.,
RA   Kobayashi Y., Hsu F.F., Sharon M., Browse J., He S.Y., Rizo J., Howe G.A.,
RA   Zheng N.;
RT   "Jasmonate perception by inositol-phosphate-potentiated COI1-JAZ co-
RT   receptor.";
RL   Nature 468:400-405(2010).
RN   [17]
RP   REPRESSION BY 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. Jasmonoyl-isoleucine (JA-
CC       Ile) specifically promotes COI1-TIFY10A/JAZ1 interaction. Interacts
CC       with COI1 and inositol pentakisphosphate to form a high-affinity
CC       jasmonates coreceptor. {ECO:0000269|PubMed:17637675,
CC       ECO:0000269|PubMed:17637677, ECO:0000269|PubMed:19151223}.
CC   -!- SUBUNIT: Homo- and heterodimer. Interacts with TIFY10B/JAZ2,
CC       TIFY6B/JAZ3, TIFY6A/JAZ4, TIFY11A/JAZ5, TIFY11B/JAZ6, TIFY5A/JAZ8,
CC       TIFY7/JAZ9, TIFY9/JAZ10, TIFY3A/JAZ11 and TIFY3B/JAZ12. Interacts with
CC       COI1, MYC2, MYC3, MYC4, MYB21 and MYB24. Interacts (via tify domain)
CC       with AFPH2/NINJA. {ECO:0000269|PubMed:17637675,
CC       ECO:0000269|PubMed:18547396, ECO:0000269|PubMed:19151223,
CC       ECO:0000269|PubMed:19309455, ECO:0000269|PubMed:20360743,
CC       ECO:0000269|PubMed:20927106, ECO:0000269|PubMed:21321051,
CC       ECO:0000269|PubMed:21447791}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with the pathogenic
CC       Pseudomonas syringae HopZ1a protein. {ECO:0000250|UniProtKB:Q9C9E3}.
CC   -!- INTERACTION:
CC       Q9LMA8; P49597: ABI1; NbExp=3; IntAct=EBI-1388539, EBI-782526;
CC       Q9LMA8; Q9SV55: AFPH2; NbExp=9; IntAct=EBI-1388539, EBI-1787005;
CC       Q9LMA8; Q9ZNV8: AHP2; NbExp=3; IntAct=EBI-1388539, EBI-1100687;
CC       Q9LMA8; Q9FIW5: ANAC094; NbExp=3; IntAct=EBI-1388539, EBI-25522986;
CC       Q9LMA8; Q9LNJ5: BHLH13; NbExp=9; IntAct=EBI-1388539, EBI-4434261;
CC       Q9LMA8; O04197: COI1; NbExp=10; IntAct=EBI-1388539, EBI-401159;
CC       Q9LMA8; O24606: EIN3; NbExp=4; IntAct=EBI-1388539, EBI-593576;
CC       Q9LMA8; Q9ZVC9: FRS3; NbExp=7; IntAct=EBI-1388539, EBI-4448729;
CC       Q9LMA8; Q9LQT8: GAI; NbExp=5; IntAct=EBI-1388539, EBI-963606;
CC       Q9LMA8; Q9FN69: GL3; NbExp=3; IntAct=EBI-1388539, EBI-533348;
CC       Q9LMA8; Q9FML2: HDA6; NbExp=4; IntAct=EBI-1388539, EBI-639608;
CC       Q9LMA8; Q39204: MYC2; NbExp=13; IntAct=EBI-1388539, EBI-1792336;
CC       Q9LMA8; Q9FIP9: MYC3; NbExp=3; IntAct=EBI-1388539, EBI-15845995;
CC       Q9LMA8; O49687: MYC4; NbExp=3; IntAct=EBI-1388539, EBI-15406909;
CC       Q9LMA8; O80920: PYL4; NbExp=3; IntAct=EBI-1388539, EBI-2349683;
CC       Q9LMA8; Q8GXW1: RGL2; NbExp=3; IntAct=EBI-1388539, EBI-963665;
CC       Q9LMA8; Q9FHZ1: SCL23; NbExp=4; IntAct=EBI-1388539, EBI-1238460;
CC       Q9LMA8; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-1388539, EBI-4426144;
CC       Q9LMA8; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-1388539, EBI-25522447;
CC       Q9LMA8; Q9LMA8: TIFY10A; NbExp=7; IntAct=EBI-1388539, EBI-1388539;
CC       Q9LMA8; Q9S7M2: TIFY10B; NbExp=5; IntAct=EBI-1388539, EBI-1792563;
CC       Q9LMA8; Q8LBM2: TIFY5A; NbExp=12; IntAct=EBI-1388539, EBI-2312143;
CC       Q9LMA8; Q9LVI4: TIFY6B; NbExp=2; IntAct=EBI-1388539, EBI-1792431;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC       ECO:0000269|PubMed:17499004, ECO:0000269|PubMed:17637677}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9C9E3,
CC       ECO:0000255|PROSITE-ProRule:PRU00768}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q9C9E3}. Note=(Microbial infection) Interacts
CC       with Pseudomonas syringae HopZ1a at the plasma membrane and in the
CC       nucleus. {ECO:0000250|UniProtKB:Q9C9E3}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9LMA8-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Srtongly expressed in root tips.
CC       {ECO:0000269|PubMed:17499004, ECO:0000269|PubMed:17637677}.
CC   -!- INDUCTION: Up-regulated by jasmonate, wounding and herbivory.
CC       {ECO:0000269|PubMed:17637677, ECO:0000269|PubMed:18223147}.
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:0000269|PubMed:24204266}.
CC   -!- DOMAIN: The jas domain (202-227) is necessary and sufficient for
CC       interaction with COI1 and is required for TIFY 10A/JAI1 instability in
CC       response to jasmonate (PubMed:17675405, PubMed:18547396). The jas
CC       domain (202-227) is required for interaction with Pseudomonas syringae
CC       HopZ1a (By similarity). {ECO:0000250|UniProtKB:Q9C9E3,
CC       ECO:0000269|PubMed:17675405, ECO:0000269|PubMed:18547396}.
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; AC069143; AAF82229.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29814.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60136.1; -; Genomic_DNA.
DR   EMBL; AF332421; AAG48784.1; -; mRNA.
DR   EMBL; AY039894; AAK63998.1; -; mRNA.
DR   EMBL; AY065146; AAL38322.1; -; mRNA.
DR   EMBL; AY081738; AAL87391.1; -; mRNA.
DR   EMBL; AY081633; AAM10195.1; -; mRNA.
DR   EMBL; AY058863; AAL24250.1; -; mRNA.
DR   EMBL; AY087830; AAM65383.1; -; mRNA.
DR   PIR; C86325; C86325.
DR   RefSeq; NP_001319041.1; NM_001332386.1. [Q9LMA8-1]
DR   RefSeq; NP_564075.1; NM_101776.3. [Q9LMA8-1]
DR   PDB; 3OGK; X-ray; 2.80 A; Q/R/S/U/V/W/X=205-226.
DR   PDB; 3OGL; X-ray; 3.18 A; Q/R/S/U/V/W/X=200-220.
DR   PDB; 3OGM; X-ray; 3.34 A; Q/R/S/U/V/W/X=200-220.
DR   PDB; 4YZ6; X-ray; 1.95 A; B=200-221.
DR   PDBsum; 3OGK; -.
DR   PDBsum; 3OGL; -.
DR   PDBsum; 3OGM; -.
DR   PDBsum; 4YZ6; -.
DR   AlphaFoldDB; Q9LMA8; -.
DR   SMR; Q9LMA8; -.
DR   BioGRID; 23740; 49.
DR   DIP; DIP-39129N; -.
DR   ELM; Q9LMA8; -.
DR   IntAct; Q9LMA8; 41.
DR   STRING; 3702.AT1G19180.1; -.
DR   PaxDb; Q9LMA8; -.
DR   PRIDE; Q9LMA8; -.
DR   ProteomicsDB; 234300; -. [Q9LMA8-1]
DR   EnsemblPlants; AT1G19180.1; AT1G19180.1; AT1G19180. [Q9LMA8-1]
DR   EnsemblPlants; AT1G19180.3; AT1G19180.3; AT1G19180. [Q9LMA8-1]
DR   GeneID; 838501; -.
DR   Gramene; AT1G19180.1; AT1G19180.1; AT1G19180. [Q9LMA8-1]
DR   Gramene; AT1G19180.3; AT1G19180.3; AT1G19180. [Q9LMA8-1]
DR   KEGG; ath:AT1G19180; -.
DR   Araport; AT1G19180; -.
DR   TAIR; locus:2202180; AT1G19180.
DR   eggNOG; ENOG502RIU4; Eukaryota.
DR   HOGENOM; CLU_051749_1_0_1; -.
DR   InParanoid; Q9LMA8; -.
DR   OMA; RNDRITA; -.
DR   PhylomeDB; Q9LMA8; -.
DR   EvolutionaryTrace; Q9LMA8; -.
DR   PRO; PR:Q9LMA8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LMA8; baseline and differential.
DR   Genevisible; Q9LMA8; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR   GO; GO:0009908; P:flower development; IMP:TAIR.
DR   GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR   GO; GO:0009555; P:pollen development; IMP:TAIR.
DR   GO; GO:1900067; P:regulation of cellular response to alkaline pH; IMP:CACAO.
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   3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW   Jasmonic acid signaling pathway; Membrane; Nucleus; Plant defense;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..253
FT                   /note="Protein TIFY 10A"
FT                   /id="PRO_0000300652"
FT   DOMAIN          120..155
FT                   /note="Tify"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00650"
FT   MOTIF           202..227
FT                   /note="Jas"
FT                   /evidence="ECO:0000255"
FT   MOTIF           204..211
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   BINDING         204
FT                   /ligand="jasmonate"
FT                   /ligand_id="ChEBI:CHEBI:58431"
FT   MUTAGEN         202..228
FT                   /note="Missing: In jaz1delta3A; dominant mutation that
FT                   confers jasmonate insensitivity."
FT                   /evidence="ECO:0000269|PubMed:17637677"
FT   MUTAGEN         205..206
FT                   /note="RR->AA: Loss of binding to COI1 and jasmonate
FT                   insensitivity. No effect on MYC2 binding."
FT                   /evidence="ECO:0000269|PubMed:18547396"
FT   MUTAGEN         205
FT                   /note="R->A: Loss of binding to COI1 but no effect on MYC2
FT                   binding."
FT   MUTAGEN         206
FT                   /note="R->A: Loss of binding to COI1but no effect on MYC2
FT                   binding."
FT   CONFLICT        19
FT                   /note="K -> N (in Ref. 4; AAM65383)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        31
FT                   /note="S -> G (in Ref. 4; AAM65383)"
FT                   /evidence="ECO:0000305"
FT   HELIX           203..216
FT                   /evidence="ECO:0007829|PDB:4YZ6"
SQ   SEQUENCE   253 AA;  27608 MW;  EF2DAAC0CEF2DBBB CRC64;
     MSSSMECSEF VGSRRFTGKK PSFSQTCSRL SQYLKENGSF GDLSLGMACK PDVNGTLGNS
     RQPTTTMSLF PCEASNMDSM VQDVKPTNLF PRQPSFSSSS SSLPKEDVLK MTQTTRSVKP
     ESQTAPLTIF YAGQVIVFND FSAEKAKEVI NLASKGTANS LAKNQTDIRS NIATIANQVP
     HPRKTTTQEP IQSSPTPLTE LPIARRASLH RFLEKRKDRV TSKAPYQLCD PAKASSNPQT
     TGNMSWLGLA AEI
 
 
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