MYC3_ARATH
ID MYC3_ARATH Reviewed; 592 AA.
AC Q9FIP9; Q8W2F5;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=Transcription factor MYC3;
DE AltName: Full=Basic helix-loop-helix protein 5;
DE Short=AtbHLH5;
DE Short=bHLH 5;
DE AltName: Full=Protein ALTERED TRYPTOPHAN REGULATION 2;
DE AltName: Full=Transcription factor ATR2;
DE AltName: Full=Transcription factor EN 36;
DE AltName: Full=bHLH transcription factor bHLH005;
GN Name=MYC3; Synonyms=ATR2, BHLH5, EN36; OrderedLocusNames=At5g46760;
GN ORFNames=MZA15.18;
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], TISSUE SPECIFICITY, GENE FAMILY, AND
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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 FUNCTION, MUTAGENESIS OF ASP-94, AND TISSUE SPECIFICITY.
RX PubMed=12136026; DOI=10.1093/genetics/161.3.1235;
RA Smolen G.A., Pawlowski L., Wilensky S.E., Bender J.;
RT "Dominant alleles of the basic helix-loop-helix transcription factor ATR2
RT activate stress-responsive genes in Arabidopsis.";
RL Genetics 161:1235-1246(2002).
RN [5]
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 [6]
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 [7]
RP INTERACTION WITH TIFY10A/JAZ1.
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 [8]
RP FUNCTION, INTERACTION WITH TIFY10A/JAZ1; TIFY6B/JAZ3 AND TIFY7/JAZ9,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
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 [9]
RP FUNCTION, INTERACTION WITH TIFY10A/JAZ1; TIFY10B/JAZ2; TIFY11A/JAZ5;
RP TIFY11B/JAZ6; TIFY5A/JAZ8; TIFY7/JAZ9; TIFY9/JAZ10 AND TIFY3A/JAZ11,
RP DOMAIN, SUBCELLULAR LOCATION, AND INDUCTION BY JASMONIC ACID.
RX PubMed=21242320; DOI=10.1093/mp/ssq073;
RA Cheng Z., Sun L., Qi T., Zhang B., Peng W., Liu Y., Xie D.;
RT "The bHLH transcription factor MYC3 interacts with the Jasmonate ZIM-domain
RT proteins to mediate jasmonate response in Arabidopsis.";
RL Mol. Plant 4:279-288(2011).
RN [10]
RP FUNCTION, INTERACTION WITH TIFY10A/JAZ1; TIFY10B/JAZ2; TIFY6B/JAZ3;
RP TIFY11A/JAZ5; TIFY11B/JAZ6; TIFY5B/JAZ7; TIFY5A/JAZ8; TIFY7/JAZ9;
RP TIFY9/JAZ10; TIFY3A/JAZ11; TIFY3B/JAZ12; MYC2; MYC4 AND AFPH2/NINJA,
RP SUBUNIT, DOMAIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY
RP JASMONIC ACID, 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 [11]
RP FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, AND INTERACTION WITH MYB28; MYB29;
RP MYB34; MYB51; MYB76 AND MYB122.
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).
CC -!- FUNCTION: Transcription factor involved in tryptophan, jasmonic acid
CC (JA) and other stress-responsive gene regulation. With MYC2 and MYC4,
CC controls additively subsets of JA-dependent responses. Can form
CC complexes with all known glucosinolate-related MYBs to regulate
CC glucosinolate biosynthesis. Binds to the G-box (5'-CACGTG-3') of
CC promoters. Activates multiple TIFY/JAZ promoters.
CC {ECO:0000269|PubMed:12136026, ECO:0000269|PubMed:21242320,
CC ECO:0000269|PubMed:21321051, ECO:0000269|PubMed:21335373,
CC ECO:0000269|PubMed:23943862}.
CC -!- SUBUNIT: Homo- and heterodimer. Interacts with MYB28, MYB29, MYB34,
CC MYB51, MYB76, MYB122, MYC2, MYC4, AFPH2/NINJA and the JAZ repressors
CC TIFY10A/JAZ1, TIFY10B/JAZ2, TIFY6B/JAZ3, TIFY11A/JAZ5, TIFY11B/JAZ6,
CC TIFY5B/JAZ7, TIFY5A/JAZ8, TIFY7/JAZ9, TIFY9/JAZ10, TIFY3A/JAZ11 and
CC TIFY3B/JAZ12. {ECO:0000269|PubMed:20360743,
CC ECO:0000269|PubMed:21242320, ECO:0000269|PubMed:21321051,
CC ECO:0000269|PubMed:21335373, ECO:0000269|PubMed:23943862}.
CC -!- INTERACTION:
CC Q9FIP9; Q7XYY2-1: MED25; NbExp=2; IntAct=EBI-15845995, EBI-15924435;
CC Q9FIP9; Q9LMA8: TIFY10A; NbExp=3; IntAct=EBI-15845995, EBI-1388539;
CC Q9FIP9; Q9C5K8: TIFY3B; NbExp=2; IntAct=EBI-15845995, EBI-2312231;
CC Q9FIP9; Q8LBM2: TIFY5A; NbExp=2; IntAct=EBI-15845995, EBI-2312143;
CC Q9FIP9; Q8W4J8: TIFY7; NbExp=5; IntAct=EBI-15845995, EBI-1792583;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:21242320, ECO:0000269|PubMed:21321051,
CC ECO:0000269|PubMed:21335373}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in roots, stems, leaves,
CC flowers, and seedlings. {ECO:0000269|PubMed:12136026,
CC ECO:0000269|PubMed:12679534, ECO:0000269|PubMed:21335373}.
CC -!- INDUCTION: Barely up-regulated by jasmonic acid.
CC {ECO:0000269|PubMed:21242320, ECO:0000269|PubMed:21335373}.
CC -!- DOMAIN: The JAZ-interaction domain (JID) (82-141) is sufficient for
CC interaction with MYB proteins and most of the TIFY/JAZ proteins
CC (PubMed:21335373 and PubMed:23943862). {ECO:0000269|PubMed:21242320,
CC ECO:0000269|PubMed:21335373, ECO:0000269|PubMed:23943862}.
CC -!- DISRUPTION PHENOTYPE: Minor effect on jasmonic acid response and no
CC effect on glucosinolate biosynthesis. Myc2 and myc3 double mutant has
CC an increased insensitivity to jasmonic acid. Myc2, myc3 and myc4 triple
CC mutant has no jasmonate-related defense response, is devoid of
CC glucosinolates and is extremely susceptible to generalist herbivores.
CC {ECO:0000269|PubMed:21321051, ECO:0000269|PubMed:21335373,
CC ECO:0000269|PubMed:23943862}.
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DR EMBL; AF251690; AAL55712.1; -; mRNA.
DR EMBL; AB016882; BAB08920.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95422.1; -; Genomic_DNA.
DR RefSeq; NP_199488.1; NM_124046.2.
DR PDB; 4RQW; X-ray; 2.20 A; A/B=44-238.
DR PDB; 4RRU; X-ray; 2.10 A; A=5-242.
DR PDB; 4RS9; X-ray; 1.95 A; A=44-238.
DR PDB; 4YWC; X-ray; 2.40 A; A/B=5-242.
DR PDB; 4YZ6; X-ray; 1.95 A; A=44-238.
DR PDB; 5T0F; X-ray; 2.40 A; A=44-242.
DR PDB; 5T0Q; X-ray; 2.15 A; A=44-242.
DR PDBsum; 4RQW; -.
DR PDBsum; 4RRU; -.
DR PDBsum; 4RS9; -.
DR PDBsum; 4YWC; -.
DR PDBsum; 4YZ6; -.
DR PDBsum; 5T0F; -.
DR PDBsum; 5T0Q; -.
DR AlphaFoldDB; Q9FIP9; -.
DR SMR; Q9FIP9; -.
DR BioGRID; 19967; 28.
DR DIP; DIP-58585N; -.
DR IntAct; Q9FIP9; 13.
DR STRING; 3702.AT5G46760.1; -.
DR iPTMnet; Q9FIP9; -.
DR PaxDb; Q9FIP9; -.
DR PRIDE; Q9FIP9; -.
DR ProteomicsDB; 251260; -.
DR EnsemblPlants; AT5G46760.1; AT5G46760.1; AT5G46760.
DR GeneID; 834719; -.
DR Gramene; AT5G46760.1; AT5G46760.1; AT5G46760.
DR KEGG; ath:AT5G46760; -.
DR Araport; AT5G46760; -.
DR TAIR; locus:2178555; AT5G46760.
DR eggNOG; ENOG502QUFW; Eukaryota.
DR HOGENOM; CLU_021132_0_1_1; -.
DR OMA; GCERAGQ; -.
DR OrthoDB; 371763at2759; -.
DR PhylomeDB; Q9FIP9; -.
DR PRO; PR:Q9FIP9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIP9; baseline and differential.
DR Genevisible; Q9FIP9; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0043425; F:bHLH transcription factor binding; IPI:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IMP:TAIR.
DR GO; GO:0006952; P:defense response; IMP:TAIR.
DR GO; GO:0106167; P:extracellular ATP signaling; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009753; P:response to jasmonic acid; IMP:TAIR.
DR GO; GO:0010374; P:stomatal complex development; IGI: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; DNA-binding; Nucleus; Plant defense; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..592
FT /note="Transcription factor MYC3"
FT /id="PRO_0000358723"
FT DOMAIN 411..460
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 82..141
FT /note="JAZ-interaction domain"
FT REGION 261..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 94
FT /note="D->A,Q,S: Exhibits an atr2D-like phenotype; dominant
FT resistance to 5-methyl-tryptophan (5MT), a toxic tryptophan
FT analog."
FT /evidence="ECO:0000269|PubMed:12136026"
FT MUTAGEN 94
FT /note="D->E: No effect, normal sensitivity to 5MT."
FT /evidence="ECO:0000269|PubMed:12136026"
FT MUTAGEN 94
FT /note="D->N: In atr2D; dominant resistance to 5MT."
FT /evidence="ECO:0000269|PubMed:12136026"
FT CONFLICT 2
FT /note="N -> D (in Ref. 1; AAL55712)"
FT /evidence="ECO:0000305"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:4RRU"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:4RRU"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:4RRU"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:4RS9"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:4RS9"
FT STRAND 69..79
FT /evidence="ECO:0007829|PDB:4RS9"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:4RS9"
FT STRAND 86..97
FT /evidence="ECO:0007829|PDB:4RS9"
FT HELIX 112..127
FT /evidence="ECO:0007829|PDB:4RS9"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:4RS9"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4RS9"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:4RS9"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:4RS9"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:4RS9"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:4RS9"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:4RS9"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:4RS9"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:4RS9"
SQ SEQUENCE 592 AA; 64992 MW; 3E29BA18971E4F26 CRC64;
MNGTTSSINF LTSDDDASAA AMEAFIGTNH HSSLFPPPPQ QPPQPQFNED TLQQRLQALI
ESAGENWTYA IFWQISHDFD SSTGDNTVIL GWGDGYYKGE EDKEKKKNNT NTAEQEHRKR
VIRELNSLIS GGIGVSDESN DEEVTDTEWF FLVSMTQSFV NGVGLPGESF LNSRVIWLSG
SGALTGSGCE RAGQGQIYGL KTMVCIATQN GVVELGSSEV ISQSSDLMHK VNNLFNFNNG
GGNNGVEASS WGFNLNPDQG ENDPALWISE PTNTGIESPA RVNNGNNSNS NSKSDSHQIS
KLEKNDISSV ENQNRQSSCL VEKDLTFQGG LLKSNETLSF CGNESSKKRT SVSKGSNNDE
GMLSFSTVVR SAANDSDHSD LEASVVKEAI VVEPPEKKPR KRGRKPANGR EEPLNHVEAE
RQRREKLNQR FYSLRAVVPN VSKMDKASLL GDAISYINEL KSKLQQAESD KEEIQKKLDG
MSKEGNNGKG CGSRAKERKS SNQDSTASSI EMEIDVKIIG WDVMIRVQCG KKDHPGARFM
EALKELDLEV NHASLSVVND LMIQQATVKM GSQFFNHDQL KVALMTKVGE NY
