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TIF6B_ARATH
ID   TIF6B_ARATH             Reviewed;         352 AA.
AC   Q9LVI4; Q56W78; Q8LF26;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Protein TIFY 6B;
DE   AltName: Full=Jasmonate ZIM domain-containing protein 3;
DE   AltName: Full=Protein JASMONATE INSENSITIVE 3;
GN   Name=TIFY6B; Synonyms=JAI3, JAZ3; OrderedLocusNames=At3g17860;
GN   ORFNames=MEB5.8;
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=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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].
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-352.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, 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   [7]
RP   FUNCTION, MUTAGENESIS OF 299-VAL--THR-312, INTERACTION WITH COI1 AND MYC2,
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   [8]
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   [9]
RP   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   [10]
RP   INTERACTION WITH COI1, DOMAIN, AND SUBUNIT.
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   [11]
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   [12]
RP   FUNCTION, INTERACTION WITH TIFY10A/JAZ1; TIFY10B/JAZ2; TIFY6A/JAZ4;
RP   TIFY5A/JAZ8; TIFY7/JAZ9; TIFY9/JAZ10 AND TIFY3A/JAZ11, SUBUNIT, SUBCELLULAR
RP   LOCATION, DOMAIN, AND MUTAGENESIS OF THR-180; ILE-181; PHE-182; TYR-183 AND
RP   GLY-185.
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   [13]
RP   INTERACTION WITH COI1 AND MYC2, DOMAIN, 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   [14]
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   [15]
RP   INTERACTION WITH MYC2; MYC3 AND MYC4.
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   [16]
RP   FUNCTION, INTERACTION WITH MYC2; MYC3; MYC4 AND 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).
CC   -!- FUNCTION: Repressor of jasmonate responses. Jasmonoyl-isoleucine (JA-
CC       Ile) specifically promotes COI1-TIFY6B/JAZ3 interaction. Acts as a
CC       negative regulator of MYC2 function. Feed-back regulated by MYC2.
CC       {ECO:0000269|PubMed:17637675, ECO:0000269|PubMed:17637677,
CC       ECO:0000269|PubMed:19151223, ECO:0000269|PubMed:21335373}.
CC   -!- SUBUNIT: Homo- and heterodimer. Interacts with COI1, MYC2, MYC3, MYC4,
CC       TIFY10A/JAZ1, TIFY10B/JAZ2, TIFY6A/JAZ4, TIFY5A/JAZ8, TIFY7/JAZ9,
CC       TIFY9/JAZ10 and TIFY3A/JAZ11. Interacts (via TIFY domain) with
CC       AFPH2/NINJA. {ECO:0000269|PubMed:17637675, ECO:0000269|PubMed:18547396,
CC       ECO:0000269|PubMed:19151223, ECO:0000269|PubMed:19309455,
CC       ECO:0000269|PubMed:20360743, ECO:0000269|PubMed:21321051,
CC       ECO:0000269|PubMed:21335373}.
CC   -!- INTERACTION:
CC       Q9LVI4; Q9SV55: AFPH2; NbExp=3; IntAct=EBI-1792431, EBI-1787005;
CC       Q9LVI4; Q9LNJ5: BHLH13; NbExp=5; IntAct=EBI-1792431, EBI-4434261;
CC       Q9LVI4; O04197: COI1; NbExp=6; IntAct=EBI-1792431, EBI-401159;
CC       Q9LVI4; Q9ZVC9: FRS3; NbExp=4; IntAct=EBI-1792431, EBI-4448729;
CC       Q9LVI4; Q9LQT8: GAI; NbExp=3; IntAct=EBI-1792431, EBI-963606;
CC       Q9LVI4; Q39204: MYC2; NbExp=7; IntAct=EBI-1792431, EBI-1792336;
CC       Q9LVI4; O49687: MYC4; NbExp=3; IntAct=EBI-1792431, EBI-15406909;
CC       Q9LVI4; A4FVP6: NAC016; NbExp=3; IntAct=EBI-1792431, EBI-25522702;
CC       Q9LVI4; Q9M126: NAC69; NbExp=3; IntAct=EBI-1792431, EBI-15191931;
CC       Q9LVI4; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-1792431, EBI-4426144;
CC       Q9LVI4; Q9MAH8: TCP3; NbExp=3; IntAct=EBI-1792431, EBI-25522447;
CC       Q9LVI4; Q9LMA8: TIFY10A; NbExp=2; IntAct=EBI-1792431, EBI-1388539;
CC       Q9LVI4; Q8GY55: TIFY4B; NbExp=3; IntAct=EBI-1792431, EBI-15206004;
CC       Q9LVI4; Q58G47: TIFY6A; NbExp=3; IntAct=EBI-1792431, EBI-2312053;
CC       Q9LVI4; Q9LVI4: TIFY6B; NbExp=8; IntAct=EBI-1792431, EBI-1792431;
CC       Q9LVI4; Q8W4J8: TIFY7; NbExp=4; IntAct=EBI-1792431, EBI-1792583;
CC       Q9LVI4; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-1792431, EBI-4426557;
CC       Q9LVI4; O22152: YAB1; NbExp=3; IntAct=EBI-1792431, EBI-1113627;
CC       Q9LVI4; Q9LDT3: YAB4; NbExp=5; IntAct=EBI-1792431, EBI-1115523;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC       ECO:0000269|PubMed:19151223}.
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=Q9LVI4-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Srtongly expressed in root tips.
CC       {ECO:0000269|PubMed:17499004}.
CC   -!- INDUCTION: Up-regulated by jasmonate, wounding and herbivory.
CC       {ECO:0000269|PubMed:17637677, ECO:0000269|PubMed:18223147}.
CC   -!- DOMAIN: The tify domain is required for homo- and heterodimerization
CC       and for the interaction with other TIFY proteins.
CC       {ECO:0000269|PubMed:19151223}.
CC   -!- DOMAIN: The jas domain (302-326) is necessary and sufficient for the
CC       hormone dependent interaction with COI1 and the hormone independent
CC       interaction with MYC2. {ECO:0000269|PubMed:19309455}.
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}.
CC   -!- CAUTION: PubMed:17637675 showed that COI1 interacts with the N-terminal
CC       part of the protein (1-208), but not with its C terminus.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD95285.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB019230; BAB02709.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76016.1; -; Genomic_DNA.
DR   EMBL; AY085082; AAM67301.1; -; mRNA.
DR   EMBL; AF372907; AAK49623.1; -; mRNA.
DR   EMBL; BT003044; AAO23609.1; -; mRNA.
DR   EMBL; AK222169; BAD95285.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001078174.1; NM_001084705.3.
DR   RefSeq; NP_001327107.1; NM_001338310.1.
DR   RefSeq; NP_566590.1; NM_112667.4. [Q9LVI4-1]
DR   AlphaFoldDB; Q9LVI4; -.
DR   SMR; Q9LVI4; -.
DR   BioGRID; 6388; 56.
DR   DIP; DIP-40532N; -.
DR   ELM; Q9LVI4; -.
DR   IntAct; Q9LVI4; 56.
DR   STRING; 3702.AT3G17860.1; -.
DR   PaxDb; Q9LVI4; -.
DR   PRIDE; Q9LVI4; -.
DR   ProteomicsDB; 234278; -. [Q9LVI4-1]
DR   EnsemblPlants; AT3G17860.1; AT3G17860.1; AT3G17860. [Q9LVI4-1]
DR   GeneID; 821055; -.
DR   Gramene; AT3G17860.1; AT3G17860.1; AT3G17860. [Q9LVI4-1]
DR   KEGG; ath:AT3G17860; -.
DR   Araport; AT3G17860; -.
DR   TAIR; locus:2088530; AT3G17860.
DR   eggNOG; ENOG502QWAG; Eukaryota.
DR   HOGENOM; CLU_062327_0_0_1; -.
DR   InParanoid; Q9LVI4; -.
DR   OMA; MERDFIG; -.
DR   OrthoDB; 1055787at2759; -.
DR   PhylomeDB; Q9LVI4; -.
DR   PRO; PR:Q9LVI4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LVI4; baseline and differential.
DR   Genevisible; Q9LVI4; AT.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR   GO; GO:0031347; P:regulation of defense response; IMP:TAIR.
DR   GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IBA:GO_Central.
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   Alternative splicing; Jasmonic acid signaling pathway; Nucleus;
KW   Plant defense; Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..352
FT                   /note="Protein TIFY 6B"
FT                   /id="PRO_0000300648"
FT   DOMAIN          172..207
FT                   /note="Tify"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00650"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           302..326
FT                   /note="Jas"
FT                   /evidence="ECO:0000255"
FT   MOTIF           304..311
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        27..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         180
FT                   /note="T->A: No effect on dimerization."
FT                   /evidence="ECO:0000269|PubMed:19151223"
FT   MUTAGEN         181
FT                   /note="I->A: No effect on dimerization, but loss of
FT                   interaction with TIFY9/JAZ10."
FT                   /evidence="ECO:0000269|PubMed:19151223"
FT   MUTAGEN         182
FT                   /note="F->A: No effect on dimerization."
FT                   /evidence="ECO:0000269|PubMed:19151223"
FT   MUTAGEN         183
FT                   /note="Y->A: No effect on dimerization."
FT                   /evidence="ECO:0000269|PubMed:19151223"
FT   MUTAGEN         185
FT                   /note="G->A: Loss of dimerization and loss of interaction
FT                   with TIFY9/JAZ10."
FT                   /evidence="ECO:0000269|PubMed:19151223"
FT   MUTAGEN         299..312
FT                   /note="VALPLARKASLARF->GKKQSQRPDTTFAI: In jai3-1; dominant
FT                   mutation that confers jasmonate insensitivity."
FT                   /evidence="ECO:0000269|PubMed:17637675"
FT   MUTAGEN         313..352
FT                   /note="Missing: In jai3-1; dominant mutation that confers
FT                   jasmonate insensitivity."
FT   CONFLICT        22
FT                   /note="S -> R (in Ref. 3; AAM67301)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   352 AA;  37746 MW;  D65DEEA2F04C58E4 CRC64;
     MERDFLGLGS KNSPITVKEE TSESSRDSAP NRGMNWSFSN KVSASSSQFL SFRPTQEDRH
     RKSGNYHLPH SGSFMPSSVA DVYDSTRKAP YSSVQGVRMF PNSNQHEETN AVSMSMPGFQ
     SHHYAPGGRS FMNNNNNSQP LVGVPIMAPP ISILPPPGSI VGTTDIRSSS KPIGSPAQLT
     IFYAGSVCVY DDISPEKAKA IMLLAGNGSS MPQVFSPPQT HQQVVHHTRA SVDSSAMPPS
     FMPTISYLSP EAGSSTNGLG ATKATRGLTS TYHNNQANGS NINCPVPVSC STNVMAPTVA
     LPLARKASLA RFLEKRKERV TSVSPYCLDK KSSTDCRRSM SECISSSLSS AT
 
 
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