MYC2_ARATH
ID MYC2_ARATH Reviewed; 623 AA.
AC Q39204; O48644; Q5K1L7; Q8W2F4; Q9LPJ8;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 2.
DT 25-MAY-2022, entry version 172.
DE RecName: Full=Transcription factor MYC2;
DE Short=AtMYC2;
DE AltName: Full=Basic helix-loop-helix protein 6;
DE Short=AtbHLH6;
DE Short=bHLH 6;
DE AltName: Full=Protein JASMONATE INSENSITIVE 1;
DE AltName: Full=R-homologous Arabidopsis protein 1;
DE Short=RAP-1;
DE AltName: Full=Transcription factor EN 38;
DE AltName: Full=Z-box binding factor 1 protein;
DE AltName: Full=bHLH transcription factor bHLH006;
DE AltName: Full=rd22BP1;
GN Name=MYC2; Synonyms=BHLH6, EN38, JAI1, JIN1, RAP1, RD22BP1, ZBF1;
GN OrderedLocusNames=At1g32640; ORFNames=F6N18.4;
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. C24;
RX PubMed=9177323; DOI=10.1023/a:1005898823105;
RA de Pater S., Pham K., Memelink J., Kijne J.;
RT "RAP-1 is an Arabidopsis MYC-like R protein homologue, that binds to G-box
RT sequence motifs.";
RL Plant Mol. Biol. 34:169-174(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=9368419; DOI=10.2307/3870530;
RA Abe H., Yamaguchi-Shinozaki K., Urao T., Iwasaki T., Hosokawa D.,
RA Shinozaki K.;
RT "Role of Arabidopsis MYC and MYB homologs in drought- and abscisic acid-
RT regulated gene expression.";
RL Plant Cell 9:1859-1868(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15923349; DOI=10.1105/tpc.105.032060;
RA Yadav V., Mallappa C., Gangappa S.N., Bhatia S., Chattopadhyay S.;
RT "A basic helix-loop-helix transcription factor in Arabidopsis, MYC2, acts
RT as a repressor of blue light-mediated photomorphogenic growth.";
RL Plant Cell 17:1953-1966(2005).
RN [4]
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-458, TISSUE SPECIFICITY, INDUCTION BY UV
RP LIGHT, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=12679534; DOI=10.1093/molbev/msg088;
RA Heim M.A., Jakoby M., Werber M., Martin C., Weisshaar B., Bailey P.C.;
RT "The basic helix-loop-helix transcription factor family in plants: a
RT genome-wide study of protein structure and functional diversity.";
RL Mol. Biol. Evol. 20:735-747(2003).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12509522; DOI=10.1105/tpc.006130;
RA Abe H., Urao T., Ito T., Seki M., Shinozaki K., Yamaguchi-Shinozaki K.;
RT "Arabidopsis AtMYC2 (bHLH) and AtMYB2 (MYB) function as transcriptional
RT activators in abscisic acid signaling.";
RL Plant Cell 15:63-78(2003).
RN [9]
RP GENE FAMILY.
RX PubMed=12897250; DOI=10.1105/tpc.013839;
RA Toledo-Ortiz G., Huq E., Quail P.H.;
RT "The Arabidopsis basic/helix-loop-helix transcription factor family.";
RL Plant Cell 15:1749-1770(2003).
RN [10]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=14600211; DOI=10.1105/tpc.151140;
RA Bailey P.C., Martin C., Toledo-Ortiz G., Quail P.H., Huq E., Heim M.A.,
RA Jakoby M., Werber M., Weisshaar B.;
RT "Update on the basic helix-loop-helix transcription factor gene family in
RT Arabidopsis thaliana.";
RL Plant Cell 15:2497-2502(2003).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INDUCTION BY
RP ABSCISIC ACID AND JASMONIC ACID.
RX PubMed=15208388; DOI=10.1105/tpc.022319;
RA Lorenzo O., Chico J.M., Sanchez-Serrano J.J., Solano R.;
RT "JASMONATE-INSENSITIVE1 encodes a MYC transcription factor essential to
RT discriminate between different jasmonate-regulated defense responses in
RT Arabidopsis.";
RL Plant Cell 16:1938-1950(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [13]
RP INTERACTION WITH TIFY10A/JAZ1; TIFY10B/JAZ2; TIFY6B/JAZ3; TIFY6A/JAZ4;
RP TIFY11A/JAZ5; TIFY11B/JAZ6; TIFY5A/JAZ8; TIFY7/JAZ9; TIFY9/JAZ10;
RP TIFY3A/JAZ11 AND TIFY3B/JAZ12.
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 FUNCTION, AND INTERACTION WITH TIFY10A/JAZ1; TIFY6B/JAZ3 AND TIFY7/JAZ9.
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 FUNCTION, INTERACTION WITH TIFY10A/JAZ1; TIFY10B/JAZ2; TIFY6B/JAZ3;
RP TIFY11A/JAZ5; TIFY11B/JAZ6; TIFY5A/JAZ8; TIFY7/JAZ9; TIFY9/JAZ10;
RP TIFY3A/JAZ11; TIFY3B/JAZ12; MYC3 AND AFPH2/NINJA, SUBUNIT, DOMAIN,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [16]
RP FUNCTION.
RX PubMed=21954460; DOI=10.1105/tpc.111.089870;
RA Chen Q., Sun J., Zhai Q., Zhou W., Qi L., Xu L., Wang B., Chen R.,
RA Jiang H., Qi J., Li X., Palme K., Li C.;
RT "The basic helix-loop-helix transcription factor MYC2 directly represses
RT PLETHORA expression during jasmonate-mediated modulation of the root stem
RT cell niche in Arabidopsis.";
RL Plant Cell 23:3335-3352(2011).
RN [17]
RP INTERACTION WITH TIC.
RX PubMed=22693280; DOI=10.1105/tpc.111.095430;
RA Shin J., Heidrich K., Sanchez-Villarreal A., Parker J.E., Davis S.J.;
RT "TIME FOR COFFEE represses accumulation of the MYC2 transcription factor to
RT provide time-of-day regulation of jasmonate signaling in Arabidopsis.";
RL Plant Cell 24:2470-2482(2012).
RN [18]
RP INTERACTION WITH MED25.
RX PubMed=22822206; DOI=10.1105/tpc.112.098277;
RA Chen R., Jiang H., Li L., Zhai Q., Qi L., Zhou W., Liu X., Li H., Zheng W.,
RA Sun J., Li C.;
RT "The Arabidopsis mediator subunit MED25 differentially regulates jasmonate
RT and abscisic acid signaling through interacting with the MYC2 and ABI5
RT transcription factors.";
RL Plant Cell 24:2898-2916(2012).
RN [19]
RP FUNCTION, AND INTERACTION WITH RGA.
RX PubMed=22669881; DOI=10.1105/tpc.112.098749;
RA Hong G.J., Xue X.Y., Mao Y.B., Wang L.J., Chen X.Y.;
RT "Arabidopsis MYC2 interacts with DELLA proteins in regulating sesquiterpene
RT synthase gene expression.";
RL Plant Cell 24:2635-2648(2012).
RN [20]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=23169619; DOI=10.1073/pnas.1210054109;
RA Withers J., Yao J., Mecey C., Howe G.A., Melotto M., He S.Y.;
RT "Transcription factor-dependent nuclear localization of a transcriptional
RT repressor in jasmonate hormone signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:20148-20153(2012).
RN [21]
RP FUNCTION, AND REVIEW.
RX PubMed=23142764; DOI=10.1093/mp/sss128;
RA Kazan K., Manners J.M.;
RT "MYC2: the master in action.";
RL Mol. Plant 6:686-703(2013).
RN [22]
RP FUNCTION, INDUCTION BY METHYL JASMONATE, PHOSPHORYLATION AT THR-328,
RP DOMAIN, AND MUTAGENESIS OF THR-328; SER-330; SER-334 AND THR-336.
RX PubMed=23593022; DOI=10.1371/journal.pgen.1003422;
RA Zhai Q., Yan L., Tan D., Chen R., Sun J., Gao L., Dong M.Q., Wang Y.,
RA Li C.;
RT "Phosphorylation-coupled proteolysis of the transcription factor MYC2 is
RT important for jasmonate-signaled plant immunity.";
RL PLoS Genet. 9:E1003422-E1003422(2013).
RN [23]
RP FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, INTERACTION WITH MYB28; MYB29;
RP MYB34; MYB51; MYB76 AND MYB122, AND INDUCTION BY HERBIVORY.
RX PubMed=23943862; DOI=10.1105/tpc.113.115139;
RA Schweizer F., Fernandez-Calvo P., Zander M., Diez-Diaz M., Fonseca S.,
RA Glauser G., Lewsey M.G., Ecker J.R., Solano R., Reymond P.;
RT "Arabidopsis basic helix-loop-helix transcription factors MYC2, MYC3, and
RT MYC4 regulate glucosinolate biosynthesis, insect performance, and feeding
RT behavior.";
RL Plant Cell 25:3117-3132(2013).
RN [24]
RP INTERACTION WITH KIN10, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-563,
RP MUTAGENESIS OF SER-563, AND ACTIVITY REGULATION.
RX PubMed=24890857; DOI=10.1111/pce.12375;
RA Im J.H., Cho Y.H., Kim G.D., Kang G.H., Hong J.W., Yoo S.D.;
RT "Inverse modulation of the energy sensor Snf1-related protein kinase 1 on
RT hypoxia adaptation and salt stress tolerance in Arabidopsis thaliana.";
RL Plant Cell Environ. 37:2303-2312(2014).
RN [25]
RP INTERACTION WITH JAZ13.
RX PubMed=25846245; DOI=10.1111/tpj.12841;
RA Thireault C., Shyu C., Yoshida Y., St Aubin B., Campos M.L., Howe G.A.;
RT "Repression of jasmonate signaling by a non-TIFY JAZ protein in
RT Arabidopsis.";
RL Plant J. 82:669-679(2015).
RN [26]
RP INTERACTION WITH PYL6, AND SUBCELLULAR LOCATION.
RX PubMed=27357749; DOI=10.1038/srep28941;
RA Aleman F., Yazaki J., Lee M., Takahashi Y., Kim A.Y., Li Z., Kinoshita T.,
RA Ecker J.R., Schroeder J.I.;
RT "An ABA-increased interaction of the PYL6 ABA receptor with MYC2
RT Transcription Factor: A putative link of ABA and JA signaling.";
RL Sci. Rep. 6:28941-28941(2016).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 446-525 IN COMPLEX WITH DNA, AND
RP HOMOTETRAMERIZATION.
RX PubMed=28514654; DOI=10.1016/j.celrep.2017.04.057;
RA Lian T.F., Xu Y.P., Li L.F., Su X.D.;
RT "Crystal structure of tetrameric Arabidopsis MYC2 reveals the mechanism of
RT enhanced interaction with DNA.";
RL Cell Rep. 19:1334-1342(2017).
CC -!- FUNCTION: Transcriptional activator. Common transcription factor of
CC light, abscisic acid (ABA), and jasmonic acid (JA) signaling pathways.
CC With MYC3 and MYC4, controls additively subsets of JA-dependent
CC responses. In cooperation with MYB2 is involved in the regulation of
CC ABA-inducible genes under drought stress conditions. Can form complexes
CC with all known glucosinolate-related MYBs to regulate glucosinolate
CC biosynthesis. Binds to the MYC recognition site (5'-CACATG-3'), and to
CC the G-box (5'-CACNTG-3') and Z-box (5'-ATACGTGT-3') of promoters. Binds
CC directly to the promoters of the transcription factors PLETHORA1 (PLT1)
CC and PLT2 and represses their expression. Negative regulator of blue
CC light-mediated photomorphogenic growth and blue- and far-red-light
CC regulated gene expression. Activates multiple TIFY/JAZ promoters.
CC Positive regulator of lateral root formation. Regulates sesquiterpene
CC biosynthesis. Subjected to proteasome-dependent proteolysis. The
CC presence of the destruction element (DE) involved in turnover is
CC required for the function to regulate gene transcription.
CC {ECO:0000269|PubMed:12509522, ECO:0000269|PubMed:15208388,
CC ECO:0000269|PubMed:15923349, ECO:0000269|PubMed:21321051,
CC ECO:0000269|PubMed:21335373, ECO:0000269|PubMed:21954460,
CC ECO:0000269|PubMed:22669881, ECO:0000269|PubMed:23142764,
CC ECO:0000269|PubMed:23593022, ECO:0000269|PubMed:23943862,
CC ECO:0000269|PubMed:9368419}.
CC -!- ACTIVITY REGULATION: Down-regulated by KIN10 that controls its protein
CC stability under a phosphorylation-dependent manner.
CC {ECO:0000269|PubMed:24890857}.
CC -!- SUBUNIT: Homotetramer. Tetramerization enhances DNA binding affinity
CC (PubMed:28514654). Interacts (via N-terminus) with RGA, (via TAD
CC domain) with the mediator subunit MED25, with TIC, MYC3, AFPH2/NINJA
CC and the JAZ repressors TIFY10A/JAZ1, TIFY10B/JAZ2, TIFY6B/JAZ3,
CC TIFY6A/JAZ4, TIFY11A/JAZ5, TIFY11B/JAZ6, TIFY5A/JAZ8, TIFY7/JAZ9,
CC TIFY9/JAZ10, TIFY3A/JAZ11 and TIFY3B/JAZ12. Interacts with JAZ13 (via
CC jas motif) (PubMed:25846245). Interacts with MYB28, MYB29, MYB34,
CC MYB51, MYB76, MYB122 and mybe MYB2. Interacts with PYL6 in the nucleus.
CC Interaction with PYL6 is increased in the presence of abscisic acid
CC (PubMed:27357749). Interacts with KIN10 (PubMed:24890857).
CC {ECO:0000250, ECO:0000269|PubMed:19309455, ECO:0000269|PubMed:21321051,
CC ECO:0000269|PubMed:21335373, ECO:0000269|PubMed:22669881,
CC ECO:0000269|PubMed:22693280, ECO:0000269|PubMed:22822206,
CC ECO:0000269|PubMed:23943862, ECO:0000269|PubMed:24890857,
CC ECO:0000269|PubMed:25846245, ECO:0000269|PubMed:27357749,
CC ECO:0000269|PubMed:28514654}.
CC -!- INTERACTION:
CC Q39204; Q9ZNV8: AHP2; NbExp=4; IntAct=EBI-1792336, EBI-1100687;
CC Q39204; Q9LZW4: CIPK14; NbExp=5; IntAct=EBI-1792336, EBI-307576;
CC Q39204; Q8W4D8: DDL; NbExp=6; IntAct=EBI-1792336, EBI-2015534;
CC Q39204; Q9LMA8: TIFY10A; NbExp=13; IntAct=EBI-1792336, EBI-1388539;
CC Q39204; Q9S7M2: TIFY10B; NbExp=5; IntAct=EBI-1792336, EBI-1792563;
CC Q39204; Q9LDU5: TIFY11A; NbExp=9; IntAct=EBI-1792336, EBI-2312095;
CC Q39204; Q9C9E3: TIFY11B; NbExp=7; IntAct=EBI-1792336, EBI-2312120;
CC Q39204; Q9M246: TIFY3A; NbExp=5; IntAct=EBI-1792336, EBI-2312209;
CC Q39204; Q9C5K8: TIFY3B; NbExp=7; IntAct=EBI-1792336, EBI-2312231;
CC Q39204; Q8LBM2: TIFY5A; NbExp=7; IntAct=EBI-1792336, EBI-2312143;
CC Q39204; Q9LVI4: TIFY6B; NbExp=7; IntAct=EBI-1792336, EBI-1792431;
CC Q39204; Q8W4J8: TIFY7; NbExp=19; IntAct=EBI-1792336, EBI-1792583;
CC Q39204; Q93ZM9: TIFY9; NbExp=2; IntAct=EBI-1792336, EBI-2312172;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:15208388, ECO:0000269|PubMed:21335373,
CC ECO:0000269|PubMed:23169619, ECO:0000269|PubMed:24890857,
CC ECO:0000269|PubMed:27357749}.
CC -!- TISSUE SPECIFICITY: Widely expressed in the whole plant with the
CC highest expression in stem. Constitutively expressed in dark- and
CC light-grown seedlings. {ECO:0000269|PubMed:12679534,
CC ECO:0000269|PubMed:15923349}.
CC -!- INDUCTION: Detected early after abscisic acid (ABA) treatment or after
CC dehydration and high-salt stresses. Induced by UV treatment. Up-
CC regulated by methyl jasmonate and herbivory.
CC {ECO:0000269|PubMed:12679534, ECO:0000269|PubMed:15208388,
CC ECO:0000269|PubMed:23593022, ECO:0000269|PubMed:23943862,
CC ECO:0000269|PubMed:9368419}.
CC -!- DOMAIN: The transcriptional activation domain (TAD) (149-188) overlaps
CC with the destruction element (DE) (154-165).
CC {ECO:0000269|PubMed:23593022}.
CC -!- DOMAIN: The JAZ-interaction domain (JID) (93-160) is sufficient for
CC interaction with MYB proteins and most of the TIFY/JAZ proteins
CC (PubMed:21335373 and PubMed:23943862).
CC -!- DOMAIN: The C-terminal half contains an active nuclear localization
CC signal (NLS). {ECO:0000269|PubMed:23169619}.
CC -!- PTM: The phosphorylation at Thr-328 is increased by methyl jasmonate
CC treatment, facilitates the proteolysis of the protein and is coupled to
CC transcriptional activity (PubMed:23593022). The phosphorylation at Ser-
CC 563 by KIN10 represses its activity in the regulation of ABA-inducible
CC genes (PubMed:24890857). {ECO:0000269|PubMed:23593022,
CC ECO:0000269|PubMed:24890857}.
CC -!- DISRUPTION PHENOTYPE: Minor effect on jasmonic acid response and no
CC effect on glucosinolate biosynthesis, but decreased abscisic acid
CC sensitivity. Myc2 and myc3 double mutant has an increased insensitivity
CC to jasmonic acid. Myc2 and myc4 double mutant has an increased
CC insensitivity to jasmonic acid. Myc2, myc3 and myc4 triple mutant has
CC no jasmonate-related defense response, is devoid of glucosinolates and
CC is extremely susceptible to generalist herbivores.
CC {ECO:0000269|PubMed:12509522, ECO:0000269|PubMed:15208388,
CC ECO:0000269|PubMed:21335373, ECO:0000269|PubMed:23943862}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25078.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X99548; CAA67885.2; -; mRNA.
DR EMBL; AB000875; BAA25078.1; ALT_FRAME; mRNA.
DR EMBL; AJ843256; CAH58735.1; -; mRNA.
DR EMBL; AC017118; AAF25980.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31513.1; -; Genomic_DNA.
DR EMBL; AY037203; AAK59788.1; -; mRNA.
DR EMBL; BT003042; AAO23607.1; -; mRNA.
DR EMBL; AF251691; AAL55713.1; -; mRNA.
DR PIR; T52293; T52293.
DR RefSeq; NP_174541.1; NM_102998.4.
DR PDB; 5GNJ; X-ray; 2.70 A; A/B/E/F/G/I/M/N=446-525.
DR PDBsum; 5GNJ; -.
DR AlphaFoldDB; Q39204; -.
DR SMR; Q39204; -.
DR BioGRID; 25392; 56.
DR DIP; DIP-40533N; -.
DR IntAct; Q39204; 23.
DR STRING; 3702.AT1G32640.1; -.
DR iPTMnet; Q39204; -.
DR PaxDb; Q39204; -.
DR PRIDE; Q39204; -.
DR ProteomicsDB; 251217; -.
DR EnsemblPlants; AT1G32640.1; AT1G32640.1; AT1G32640.
DR GeneID; 840158; -.
DR Gramene; AT1G32640.1; AT1G32640.1; AT1G32640.
DR KEGG; ath:AT1G32640; -.
DR Araport; AT1G32640; -.
DR TAIR; locus:2035609; AT1G32640.
DR eggNOG; ENOG502QUFW; Eukaryota.
DR HOGENOM; CLU_021132_0_1_1; -.
DR InParanoid; Q39204; -.
DR OMA; SGLNWNL; -.
DR OrthoDB; 371763at2759; -.
DR PhylomeDB; Q39204; -.
DR PRO; PR:Q39204; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39204; differential.
DR Genevisible; Q39204; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0009738; P:abscisic acid-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0106167; P:extracellular ATP signaling; IMP:TAIR.
DR GO; GO:0009759; P:indole glucosinolate biosynthetic process; IMP:TAIR.
DR GO; GO:0009963; P:positive regulation of flavonoid biosynthetic process; IEP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:2000068; P:regulation of defense response to insect; IMP:TAIR.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; IMP:TAIR.
DR GO; GO:2000652; P:regulation of secondary cell wall biogenesis; IMP:TAIR.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0090357; P:regulation of tryptophan metabolic process; IMP:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009269; P:response to desiccation; IEP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IMP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR GO; GO:0010374; P:stomatal complex development; IGI:TAIR.
DR GO; GO:0006568; P:tryptophan metabolic process; IEP:TAIR.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR045084; AIB/MYC-like.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR025610; MYC/MYB_N.
DR PANTHER; PTHR11514; PTHR11514; 1.
DR Pfam; PF14215; bHLH-MYC_N; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Abscisic acid signaling pathway; Activator; DNA-binding;
KW Jasmonic acid signaling pathway; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..623
FT /note="Transcription factor MYC2"
FT /id="PRO_0000127427"
FT DOMAIN 448..497
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 93..160
FT /note="JAZ-interaction domain"
FT REGION 111..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 434..442
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 284..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:23593022"
FT MOD_RES 563
FT /note="Phosphoserine; by KIN10"
FT /evidence="ECO:0000269|PubMed:24890857"
FT MUTAGEN 328
FT /note="T->A: Jasmonate-insensitive phenotype and increased
FT stability of the protein."
FT /evidence="ECO:0000269|PubMed:23593022"
FT MUTAGEN 330
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:23593022"
FT MUTAGEN 334
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:23593022"
FT MUTAGEN 336
FT /note="T->A: No effect."
FT /evidence="ECO:0000269|PubMed:23593022"
FT MUTAGEN 563
FT /note="S->D: Abolishes its activity in the regulation of
FT ABA-inducible genes."
FT /evidence="ECO:0000269|PubMed:24890857"
FT CONFLICT 258
FT /note="A -> D (in Ref. 2; BAA25078)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="K -> R (in Ref. 4; AAL55713)"
FT /evidence="ECO:0000305"
FT CONFLICT 529
FT /note="A -> P (in Ref. 2; BAA25078)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="E -> D (in Ref. 2; BAA25078)"
FT /evidence="ECO:0000305"
FT HELIX 454..472
FT /evidence="ECO:0007829|PDB:5GNJ"
FT HELIX 483..522
FT /evidence="ECO:0007829|PDB:5GNJ"
SQ SEQUENCE 623 AA; 67950 MW; 4A8D4DE34C5928F6 CRC64;
MTDYRLQPTM NLWTTDDNAS MMEAFMSSSD ISTLWPPAST TTTTATTETT PTPAMEIPAQ
AGFNQETLQQ RLQALIEGTH EGWTYAIFWQ PSYDFSGASV LGWGDGYYKG EEDKANPRRR
SSSPPFSTPA DQEYRKKVLR ELNSLISGGV APSDDAVDEE VTDTEWFFLV SMTQSFACGA
GLAGKAFATG NAVWVSGSDQ LSGSGCERAK QGGVFGMHTI ACIPSANGVV EVGSTEPIRQ
SSDLINKVRI LFNFDGGAGD LSGLNWNLDP DQGENDPSMW INDPIGTPGS NEPGNGAPSS
SSQLFSKSIQ FENGSSSTIT ENPNLDPTPS PVHSQTQNPK FNNTFSRELN FSTSSSTLVK
PRSGEILNFG DEGKRSSGNP DPSSYSGQTQ FENKRKRSMV LNEDKVLSFG DKTAGESDHS
DLEASVVKEV AVEKRPKKRG RKPANGREEP LNHVEAERQR REKLNQRFYA LRAVVPNVSK
MDKASLLGDA IAYINELKSK VVKTESEKLQ IKNQLEEVKL ELAGRKASAS GGDMSSSCSS
IKPVGMEIEV KIIGWDAMIR VESSKRNHPA ARLMSALMDL ELEVNHASMS VVNDLMIQQA
TVKMGFRIYT QEQLRASLIS KIG
