MYC4_ARATH
ID MYC4_ARATH Reviewed; 589 AA.
AC O49687; Q8W2F6;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Transcription factor MYC4;
DE Short=AtMYC4;
DE AltName: Full=Basic helix-loop-helix protein 4;
DE Short=AtbHLH4;
DE Short=bHLH 4;
DE AltName: Full=Transcription factor EN 37;
DE AltName: Full=bHLH transcription factor bHLH004;
GN Name=MYC4; Synonyms=BHLH4, EN37; OrderedLocusNames=At4g17880;
GN ORFNames=T6K21.60;
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], INDUCTION BY UV LIGHT, 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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP TISSUE SPECIFICITY.
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 [6]
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 [7]
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 [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; TIFY6B/JAZ3;
RP TIFY6A/JAZ4; TIFY11A/JAZ5; TIFY11B/JAZ6; TIFY5B/JAZ7; TIFY5A/JAZ8;
RP TIFY7/JAZ9; TIFY9/JAZ10; TIFY3A/JAZ11; TIFY3B/JAZ12; MYC3 AND AFPH2/NINJA,
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY JASMONIC
RP 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 [10]
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 jasmonic acid (JA) gene
CC regulation. With MYC2 and MYC3, controls additively subsets of JA-
CC dependent responses. Can form complexes with all known glucosinolate-
CC related MYBs to regulate glucosinolate biosynthesis. Binds to the G-box
CC (5'-CACGTG-3') of promoters. Activates multiple TIFY/JAZ promoters.
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, MYC3, AFPH2/NINJA and the JAZ repressors
CC TIFY10A/JAZ1, TIFY10B/JAZ2, TIFY6B/JAZ3, TIFY6A/JAZ4, TIFY11A/JAZ5,
CC TIFY11B/JAZ6, TIFY5B/JAZ7, TIFY5A/JAZ8, TIFY7/JAZ9, TIFY9/JAZ10,
CC TIFY3A/JAZ11 and TIFY3B/JAZ12. {ECO:0000269|PubMed:21321051,
CC ECO:0000269|PubMed:21335373, ECO:0000269|PubMed:23943862}.
CC -!- INTERACTION:
CC O49687; Q9LUA3: NIMIN-2; NbExp=3; IntAct=EBI-15406909, EBI-541107;
CC O49687; O64687: TIFY 5B; NbExp=3; IntAct=EBI-15406909, EBI-15403807;
CC O49687; Q9LMA8: TIFY10A; NbExp=3; IntAct=EBI-15406909, EBI-1388539;
CC O49687; Q9S7M2: TIFY10B; NbExp=3; IntAct=EBI-15406909, EBI-1792563;
CC O49687; Q9LDU5: TIFY11A; NbExp=3; IntAct=EBI-15406909, EBI-2312095;
CC O49687; Q9C9E3: TIFY11B; NbExp=3; IntAct=EBI-15406909, EBI-2312120;
CC O49687; Q9C5K8: TIFY3B; NbExp=4; IntAct=EBI-15406909, EBI-2312231;
CC O49687; Q8LBM2: TIFY5A; NbExp=4; IntAct=EBI-15406909, EBI-2312143;
CC O49687; Q9LVI4: TIFY6B; NbExp=3; IntAct=EBI-15406909, EBI-1792431;
CC O49687; Q8W4J8: TIFY7; NbExp=8; IntAct=EBI-15406909, EBI-1792583;
CC O49687; Q93ZM9: TIFY9; NbExp=3; IntAct=EBI-15406909, EBI-2312172;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:21321051, ECO:0000269|PubMed:21335373}.
CC -!- TISSUE SPECIFICITY: Expressed constitutively at low levels.
CC Preferentially expressed in vascular tissues.
CC {ECO:0000269|PubMed:12509522, ECO:0000269|PubMed:21335373}.
CC -!- INDUCTION: By UV treatment. Not induced by jasmonic acid.
CC {ECO:0000269|PubMed:12679534, ECO:0000269|PubMed:21335373}.
CC -!- DOMAIN: The JAZ-interaction domain (JID) (99-150) is sufficient for
CC interaction with MYB proteins and most of the TIFY/JAZ proteins.
CC {ECO:0000269|PubMed:23943862}.
CC -!- DISRUPTION PHENOTYPE: Minor effect on jasmonic acid response and no
CC effect on glucosinolate biosynthesis. Myc2 and myc4 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; AF251689; AAL55711.1; -; mRNA.
DR EMBL; AL021889; CAA17131.1; -; Genomic_DNA.
DR EMBL; AL161547; CAB78790.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83960.1; -; Genomic_DNA.
DR EMBL; AK221507; BAD94748.1; -; mRNA.
DR PIR; T05074; T05074.
DR RefSeq; NP_193522.1; NM_117897.4.
DR AlphaFoldDB; O49687; -.
DR SMR; O49687; -.
DR BioGRID; 12804; 29.
DR DIP; DIP-61779N; -.
DR IntAct; O49687; 12.
DR STRING; 3702.AT4G17880.1; -.
DR PaxDb; O49687; -.
DR PRIDE; O49687; -.
DR ProteomicsDB; 248917; -.
DR EnsemblPlants; AT4G17880.1; AT4G17880.1; AT4G17880.
DR GeneID; 827511; -.
DR Gramene; AT4G17880.1; AT4G17880.1; AT4G17880.
DR KEGG; ath:AT4G17880; -.
DR Araport; AT4G17880; -.
DR TAIR; locus:2141055; AT4G17880.
DR eggNOG; ENOG502QUFW; Eukaryota.
DR HOGENOM; CLU_021132_0_1_1; -.
DR InParanoid; O49687; -.
DR OMA; ASKESCW; -.
DR OrthoDB; 371763at2759; -.
DR PhylomeDB; O49687; -.
DR PRO; PR:O49687; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49687; baseline and differential.
DR Genevisible; O49687; 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:2000652; P:regulation of secondary cell wall biogenesis; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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 DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..589
FT /note="Transcription factor MYC4"
FT /id="PRO_0000358725"
FT DOMAIN 412..461
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 99..150
FT /note="JAZ-interaction domain"
FT REGION 114..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 2
FT /note="S -> A (in Ref. 1; AAL55711)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 64589 MW; C962E83290DF9CCC CRC64;
MSPTNVQVTD YHLNQSKTDT TNLWSTDDDA SVMEAFIGGG SDHSSLFPPL PPPPLPQVNE
DNLQQRLQAL IEGANENWTY AVFWQSSHGF AGEDNNNNNT VLLGWGDGYY KGEEEKSRKK
KSNPASAAEQ EHRKRVIREL NSLISGGVGG GDEAGDEEVT DTEWFFLVSM TQSFVKGTGL
PGQAFSNSDT IWLSGSNALA GSSCERARQG QIYGLQTMVC VATENGVVEL GSSEIIHQSS
DLVDKVDTFF NFNNGGGEFG SWAFNLNPDQ GENDPGLWIS EPNGVDSGLV AAPVMNNGGN
DSTSNSDSQP ISKLCNGSSV ENPNPKVLKS CEMVNFKNGI ENGQEEDSSN KKRSPVSNNE
EGMLSFTSVL PCDSNHSDLE ASVAKEAESN RVVVEPEKKP RKRGRKPANG REEPLNHVEA
ERQRREKLNQ RFYSLRAVVP NVSKMDKASL LGDAISYISE LKSKLQKAES DKEELQKQID
VMNKEAGNAK SSVKDRKCLN QESSVLIEME VDVKIIGWDA MIRIQCSKRN HPGAKFMEAL
KELDLEVNHA SLSVVNDLMI QQATVKMGNQ FFTQDQLKVA LTEKVGECP
