BH012_ARATH
ID BH012_ARATH Reviewed; 526 AA.
AC Q8W2F1; O65257; P93651;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Transcription factor MYC1;
DE Short=AtMYC1;
DE AltName: Full=Basic helix-loop-helix protein 12;
DE Short=AtbHLH12;
DE Short=bHLH 12;
DE AltName: Full=Transcription factor EN 58;
DE AltName: Full=bHLH transcription factor bHLH012;
GN Name=BHLH12; Synonyms=EN58, MYC1; OrderedLocusNames=At4g00480;
GN ORFNames=F6N23.22;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=8980509; DOI=10.1007/bf00019112;
RA Urao T., Yamaguchi-Shinozaki K., Mitsukawa N., Shibata D., Shinozaki K.;
RT "Molecular cloning and characterization of a gene that encodes a MYC-
RT related protein in Arabidopsis.";
RL Plant Mol. Biol. 32:571-576(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, 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 [3]
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 [4]
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 [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 FUNCTION, AND INTERACTION WITH MYB75/PAP1; MYB90/PAP2; MYB4; MYB5; MYB6;
RP MYB23; MYB82; MYB113; MYB114; TT2; MYB0/GL1 AND MYB66/WER.
RX PubMed=15361138; DOI=10.1111/j.1365-313x.2004.02183.x;
RA Zimmermann I.M., Heim M.A., Weisshaar B., Uhrig J.F.;
RT "Comprehensive identification of Arabidopsis thaliana MYB transcription
RT factors interacting with R/B-like BHLH proteins.";
RL Plant J. 40:22-34(2004).
CC -!- FUNCTION: Trancsription activator, when associated with MYB75/PAP1 or
CC MYB90/PAP2. {ECO:0000269|PubMed:15361138}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with MYB75/PAP1, MYB90/PAP2,
CC MYB4, MYB5, MYB6, MYB23, MYB82, MYB113, MYB114, TT2, MYB0/GL1, and
CC MYB66/WER. {ECO:0000269|PubMed:15361138, ECO:0000305}.
CC -!- INTERACTION:
CC Q8W2F1; Q9FE25: MYB75; NbExp=3; IntAct=EBI-1546379, EBI-1545177;
CC Q8W2F1; Q9ZTC3: MYB90; NbExp=2; IntAct=EBI-1546379, EBI-1545203;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
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=Q8W2F1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Mostly expressed in developing seeds. Also detected
CC in stems and leaves. {ECO:0000269|PubMed:12679534,
CC ECO:0000269|PubMed:8980509}.
CC -!- INDUCTION: By cold, UV, flagellin, jasmonic acid (JA), and salicylic
CC acid (SA) treatments. {ECO:0000269|PubMed:12679534}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC13623.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80857.1; Type=Erroneous gene model prediction; 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; D83511; BAA11933.1; -; Genomic_DNA.
DR EMBL; AF251697; AAL55719.1; -; mRNA.
DR EMBL; AF058919; AAC13623.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161472; CAB80857.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81887.1; -; Genomic_DNA.
DR PIR; T01212; T01212.
DR RefSeq; NP_191957.2; NM_116272.4. [Q8W2F1-1]
DR AlphaFoldDB; Q8W2F1; -.
DR SMR; Q8W2F1; -.
DR BioGRID; 13256; 14.
DR DIP; DIP-38469N; -.
DR IntAct; Q8W2F1; 14.
DR STRING; 3702.AT4G00480.2; -.
DR PaxDb; Q8W2F1; -.
DR PRIDE; Q8W2F1; -.
DR EnsemblPlants; AT4G00480.1; AT4G00480.1; AT4G00480. [Q8W2F1-1]
DR GeneID; 827965; -.
DR Gramene; AT4G00480.1; AT4G00480.1; AT4G00480. [Q8W2F1-1]
DR KEGG; ath:AT4G00480; -.
DR Araport; AT4G00480; -.
DR eggNOG; ENOG502QT7W; Eukaryota.
DR HOGENOM; CLU_023211_1_1_1; -.
DR InParanoid; Q8W2F1; -.
DR OMA; AEWYYLL; -.
DR PhylomeDB; Q8W2F1; -.
DR PRO; PR:Q8W2F1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8W2F1; baseline and differential.
DR Genevisible; Q8W2F1; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd18918; bHLH_AtMYC1_like; 1.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR025610; MYC/MYB_N.
DR InterPro; IPR045896; MYC1-like_bHLH.
DR Pfam; PF14215; bHLH-MYC_N; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..526
FT /note="Transcription factor MYC1"
FT /id="PRO_0000358729"
FT DOMAIN 333..382
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 330..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 272..273
FT /note="ND -> TA (in Ref. 1; BAA11933)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 59988 MW; 1E090B0EB5A107F3 CRC64;
MSLTMADGVE AAAGRSKRQN SLLRKQLALA VRSVQWSYAI FWSSSLTQPG VLEWGEGCYN
GDMKKRKKSY ESHYKYGLQK SKELRKLYLS MLEGDSGTTV STTHDNLNDD DDNCHSTSMM
LSPDDLSDEE WYYLVSMSYV FSPSQCLPGR ASATGETIWL CNAQYAENKL FSRSLLARSA
SIQTVVCFPY LGGVIELGVT ELISEDHNLL RNIKSCLMEI SAHQDNDDEK KMEIKISEEK
HQLPLGISDE DLHYKRTIST VLNYSADRSG KNDKNIRHRQ PNIVTSEPGS SFLRWKQCEQ
QVSGFVQKKK SQNVLRKILH DVPLMHTKRM FPSQNSGLNQ DDPSDRRKEN EKFSVLRTMV
PTVNEVDKES ILNNTIKYLQ ELEARVEELE SCMGSVNFVE RQRKTTENLN DSVLIEETSG
NYDDSTKIDD NSGETEQVTV FRDKTHLRVK LKETEVVIEV RCSYRDYIVA DIMETLSNLH
MDAFSVRSHT LNKFLTLNLK AKFRGAAVAS VGMIKRELRR VIGDLF
