EGL1_ARATH
ID EGL1_ARATH Reviewed; 596 AA.
AC Q9CAD0; O22418;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Transcription factor EGL1;
DE AltName: Full=Basic helix-loop-helix protein 2;
DE Short=AtMYC146;
DE Short=AtbHLH2;
DE Short=bHLH 2;
DE AltName: Full=Protein ENHANCER OF GLABRA 3;
DE AltName: Full=Transcription factor EN 30;
DE AltName: Full=bHLH transcription factor bHLH002;
GN Name=BHLH2; Synonyms=EGL1, EGL3, EN30, MYC146; OrderedLocusNames=At1g63650;
GN ORFNames=F24D7.16;
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 [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Bate N.J., Rothstein S.J.;
RT "An Arabidopsis Myc-like gene (MYC-146) with homology to the anthocyanin
RT regulatory gene Delila.";
RL (er) Plant Gene Register PGR97-140(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Lloyd A.M., Zhang F.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
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 FUNCTION, DEVELOPMENTAL STAGE, HOMODIMERIZATION, AND INTERACTION WITH CPC;
RP GL3; MYB0; MYB75; MYB90; TRY AND TTG1.
RX PubMed=12917293; DOI=10.1242/dev.00681;
RA Zhang F., Gonzalez A., Zhao M., Payne C.T., Lloyd A.M.;
RT "A network of redundant bHLH proteins functions in all TTG1-dependent
RT pathways of Arabidopsis.";
RL Development 130:4859-4869(2003).
RN [7]
RP FUNCTION, INTERACTION WITH CPC AND MYB66, AND TISSUE SPECIFICITY.
RX PubMed=14627722; DOI=10.1242/dev.00880;
RA Bernhardt C., Lee M.M., Gonzalez A., Zhang F., Lloyd A.M., Schiefelbein J.;
RT "The bHLH genes GLABRA3 (GL3) and ENHANCER OF GLABRA3 (EGL3) specify
RT epidermal cell fate in the Arabidopsis root.";
RL Development 130:6431-6439(2003).
RN [8]
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 [9]
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 [10]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12956536; DOI=10.1023/a:1024852021124;
RA Ramsay N.A., Walker A.R., Mooney M., Gray J.C.;
RT "Two basic-helix-loop-helix genes (MYC-146 and GL3) from Arabidopsis can
RT activate anthocyanin biosynthesis in a white-flowered Matthiola incana
RT mutant.";
RL Plant Mol. Biol. 52:679-688(2003).
RN [11]
RP FUNCTION, AND INTERACTION WITH MYB75; MYB90; MYB5; MYB23; MYB113; MYB114;
RP 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).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15590742; DOI=10.1242/dev.01565;
RA Bernhardt C., Zhao M., Gonzalez A., Lloyd A., Schiefelbein J.;
RT "The bHLH genes GL3 and EGL3 participate in an intercellular regulatory
RT circuit that controls cell patterning in the Arabidopsis root epidermis.";
RL Development 132:291-298(2005).
CC -!- FUNCTION: Transcription activator, when associated with MYB75/PAP1,
CC MYB90/PAP2 or TT2. Involved in epidermal cell fate specification.
CC Regulates negatively stomata formation but promotes trichome formation.
CC Together with MYB66/WER, promotes the formation of non-hair cells in
CC root epidermis cells in the N position. Whereas together with CPC,
CC promotes the formation of hair cells in root epidermis cells in the H
CC position by inhibiting non-hair cell formation. Seems also to play a
CC role in the activation of anthocyanin biosynthesis, probably together
CC with MYB75/PAP1. Involved in seed mucilage production. Activates the
CC transcription of GL2. {ECO:0000269|PubMed:12917293,
CC ECO:0000269|PubMed:12956536, ECO:0000269|PubMed:14627722,
CC ECO:0000269|PubMed:15361138, ECO:0000269|PubMed:15590742}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein (By similarity). Homodimer and heterodimer with GL3. Interacts
CC with CPC, MYB0/GL1, MYB5, MYB23, MYB113, MYB114, MYB75/PAP1,
CC MYB90/PAP2, TT2, TRY, TTG1 and MYB66/WER. {ECO:0000250,
CC ECO:0000269|PubMed:12917293, ECO:0000269|PubMed:14627722,
CC ECO:0000269|PubMed:15361138}.
CC -!- INTERACTION:
CC Q9CAD0; O22059: CPC; NbExp=3; IntAct=EBI-533398, EBI-533386;
CC Q9CAD0; Q9FE25: MYB75; NbExp=5; IntAct=EBI-533398, EBI-1545177;
CC Q9CAD0; Q9ZTC3: MYB90; NbExp=3; IntAct=EBI-533398, EBI-1545203;
CC Q9CAD0; Q9SEI0: WER; NbExp=4; IntAct=EBI-533398, EBI-533373;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Note=Moves from developing
CC hair cells (trichoblasts) to developing non-hair cells (atrichoblasts).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous with higher levels in buds and flowers.
CC Specifically localized in developing root hair cells. Expressed in
CC epidermal root hair cells (trichoblasts) and moves to root hairless
CC cells (atrichoblasts) by a cell-to-cell movement through plasmodesmata
CC (at protein level). {ECO:0000269|PubMed:12956536,
CC ECO:0000269|PubMed:14627722, ECO:0000269|PubMed:15590742}.
CC -!- DEVELOPMENTAL STAGE: Localized in trichome developing region of leaves,
CC prior to trichome initiation. Levels increase in initiating and young
CC trichome cells, but dropped in the pavement cells between trichomes.
CC Disappears in mature trichomes. {ECO:0000269|PubMed:12917293}.
CC -!- INDUCTION: By UV treatment. Negatively regulated by MYB66/WER, GL3 and
CC BHLH2 in the developing non-hair cells, and positively regulated by CPC
CC and TRY in the developing hair cells. {ECO:0000269|PubMed:12679534,
CC ECO:0000269|PubMed:15590742}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB72192.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF251687; AAL55709.1; -; mRNA.
DR EMBL; AF013465; AAB72192.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF027732; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC011622; AAG52418.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34124.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34125.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34126.1; -; Genomic_DNA.
DR PIR; D96661; D96661.
DR RefSeq; NP_001185302.1; NM_001198373.2.
DR RefSeq; NP_176552.1; NM_105042.5.
DR RefSeq; NP_974080.1; NM_202351.2.
DR AlphaFoldDB; Q9CAD0; -.
DR SMR; Q9CAD0; -.
DR BioGRID; 27890; 21.
DR IntAct; Q9CAD0; 18.
DR STRING; 3702.AT1G63650.3; -.
DR iPTMnet; Q9CAD0; -.
DR PaxDb; Q9CAD0; -.
DR PRIDE; Q9CAD0; -.
DR EnsemblPlants; AT1G63650.1; AT1G63650.1; AT1G63650.
DR EnsemblPlants; AT1G63650.2; AT1G63650.2; AT1G63650.
DR EnsemblPlants; AT1G63650.3; AT1G63650.3; AT1G63650.
DR GeneID; 842669; -.
DR Gramene; AT1G63650.1; AT1G63650.1; AT1G63650.
DR Gramene; AT1G63650.2; AT1G63650.2; AT1G63650.
DR Gramene; AT1G63650.3; AT1G63650.3; AT1G63650.
DR KEGG; ath:AT1G63650; -.
DR Araport; AT1G63650; -.
DR TAIR; locus:2026629; AT1G63650.
DR eggNOG; ENOG502QT7W; Eukaryota.
DR HOGENOM; CLU_023211_1_1_1; -.
DR InParanoid; Q9CAD0; -.
DR OMA; ELNNCVH; -.
DR OrthoDB; 287853at2759; -.
DR PhylomeDB; Q9CAD0; -.
DR PRO; PR:Q9CAD0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAD0; baseline and differential.
DR Genevisible; Q9CAD0; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0009957; P:epidermal cell fate specification; IMP:TAIR.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0010026; P:trichome differentiation; IMP:TAIR.
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 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 Activator; Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..596
FT /note="Transcription factor EGL1"
FT /id="PRO_0000127426"
FT DOMAIN 401..450
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT CONFLICT 248
FT /note="Q -> Y (in Ref. 2; AAB72192)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 66620 MW; 6B934DFBE82AA102 CRC64;
MATGENRTVP DNLKKQLAVS VRNIQWSYGI FWSVSASQPG VLEWGDGYYN GDIKTRKTIQ
AAEVKIDQLG LERSEQLREL YESLSLAESS ASGSSQVTRR ASAAALSPED LTDTEWYYLV
CMSFVFNIGE GIPGGALSNG EPIWLCNAET ADSKVFTRSL LAKSASLQTV VCFPFLGGVL
EIGTTEHIKE DMNVIQSVKT LFLEAPPYTT ISTRSDYQEI FDPLSDDKYT PVFITEAFPT
TSTSGFEQEP EDHDSFINDG GASQVQSWQF VGEEISNCIH QSLNSSDCVS QTFVGTTGRL
ACDPRKSRIQ RLGQIQEQSN HVNMDDDVHY QGVISTIFKT THQLILGPQF QNFDKRSSFT
RWKRSSSVKT LGEKSQKMIK KILFEVPLMN KKEELLPDTP EETGNHALSE KKRREKLNER
FMTLRSIIPS ISKIDKVSIL DDTIEYLQDL QKRVQELESC RESADTETRI TMMKRKKPDD
EEERASANCM NSKRKGSDVN VGEDEPADIG YAGLTDNLRI SSLGNEVVIE LRCAWREGIL
LEIMDVISDL NLDSHSVQSS TGDGLLCLTV NCKHKGTKIA TTGMIQEALQ RVAWIC
