ID GL3_ARATH Reviewed; 637 AA.
AC Q9FN69;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 137.
DE RecName: Full=Transcription factor GLABRA 3;
DE AltName: Full=Basic helix-loop-helix protein 1;
DE Short=AtMYC6;
DE Short=AtbHLH1;
DE Short=bHLH 1;
DE AltName: Full=Protein SHAPESHIFTER;
DE AltName: Full=Transcription factor EN 31;
DE AltName: Full=bHLH transcription factor bHLH001;
GN Name=GL3; Synonyms=BHLH1, EN31, MYC6, SST; OrderedLocusNames=At5g41315;
GN ORFNames=MYC6.2;
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, TISSUE SPECIFICITY, GENE
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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, INTERACTION WITH MYB0 AND TTG1, AND DISRUPTION PHENOTYPE.
RX PubMed=11063707; DOI=10.1093/genetics/156.3.1349;
RA Payne C.T., Zhang F., Lloyd A.M.;
RT "GL3 encodes a bHLH protein that regulates trichome development in
RT arabidopsis through interaction with GL1 and TTG1.";
RL Genetics 156:1349-1362(2000).
RN [5]
RP FUNCTION, DEVELOPMENTAL STAGE, AND INTERACTION WITH BHLH2.
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MYB0; TTG1 AND TRY, AND
RP MUTAGENESIS OF LEU-78.
RX PubMed=14561633; DOI=10.1242/dev.00812;
RA Esch J.J., Chen M., Sanders M., Hillestad M., Ndkium S., Idelkope B.,
RA Neizer J., Marks M.D.;
RT "A contradictory GLABRA3 allele helps define gene interactions controlling
RT trichome development in Arabidopsis.";
RL Development 130:5885-5894(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.
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 AND TT2.
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, INDUCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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).
RN [13]
RP INTERACTION WITH MYB23; TTG1 AND MYB0.
RX PubMed=15728674; DOI=10.1242/dev.01708;
RA Kirik V., Lee M.M., Wester K., Herrmann U., Zheng Z., Oppenheimer D.,
RA Schiefelbein J., Hulskamp M.;
RT "Functional diversification of MYB23 and GL1 genes in trichome
RT morphogenesis and initiation.";
RL Development 132:1477-1485(2005).
RN [14]
RP INDUCTION BY NITROGEN DEFICIENCY.
RX PubMed=17053893; DOI=10.1007/s00425-006-0414-x;
RA Lea U.S., Slimestad R., Smedvig P., Lillo C.;
RT "Nitrogen deficiency enhances expression of specific MYB and bHLH
RT transcription factors and accumulation of end products in the flavonoid
RT pathway.";
RL Planta 225:1245-1253(2007).
RN [15]
RP INTERACTION WITH MYB82.
RC STRAIN=cv. Columbia;
RX PubMed=24803498; DOI=10.1093/jxb/eru179;
RA Liang G., He H., Li Y., Ai Q., Yu D.;
RT "MYB82 functions in regulation of trichome development in Arabidopsis.";
RL J. Exp. Bot. 65:3215-3223(2014).
CC -!- FUNCTION: Transcription activator, when associated with MYB75/PAP1,
CC MYB90/PAP2 or TT2. Involved in epidermal cell fate specification.
CC Negatively regulates stomata formation, but, in association with TTG1
CC and MYB0/GL1, promotes trichome formation, branching and
CC endoreplication. Also regulates trichome cell wall maturation. Together
CC with MYB66/WER, promotes the formation of non-hair cells in root
CC epidermis cells in the N position. Whereas together with CPC, promotes
CC the formation of hair cells in root epidermis cells in the H position
CC by inhibiting non-hair cell formation. Seems also to play a role in the
CC activation of anthocyanin biosynthesis, probably together with
CC MYB75/PAP1. Activates the transcription of GL2.
CC {ECO:0000269|PubMed:11063707, ECO:0000269|PubMed:12917293,
CC ECO:0000269|PubMed:12956536, ECO:0000269|PubMed:14561633,
CC ECO:0000269|PubMed:14627722, ECO:0000269|PubMed:15361138,
CC ECO:0000269|PubMed:15590742}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein (By similarity). Homodimer and heterodimer with BHLH2.
CC Interacts directly with TTG1 and MYB0/GL1 to form a complex. Its
CC interaction with TRY prevents MYB0/GL1 binding. Interacts with
CC MYB75/PAP1, MYB90/PAP2, TT2, CPC, MYB23 and MYB66/WER. Interacts with
CC MYB82 (PubMed:24803498). {ECO:0000250, ECO:0000269|PubMed:11063707,
CC ECO:0000269|PubMed:12917293, ECO:0000269|PubMed:14561633,
CC ECO:0000269|PubMed:14627722, ECO:0000269|PubMed:15361138,
CC ECO:0000269|PubMed:15728674, ECO:0000269|PubMed:24803498}.
CC -!- INTERACTION:
CC Q9FN69; P27900: GL1; NbExp=5; IntAct=EBI-533348, EBI-1543742;
CC Q9FN69; Q9FE25: MYB75; NbExp=2; IntAct=EBI-533348, EBI-1545177;
CC Q9FN69; Q9ZTC3: MYB90; NbExp=2; IntAct=EBI-533348, EBI-1545203;
CC Q9FN69; Q9FNZ5: NIMIN-1; NbExp=3; IntAct=EBI-533348, EBI-541099;
CC Q9FN69; Q9LMA8: TIFY10A; NbExp=3; IntAct=EBI-533348, EBI-1388539;
CC Q9FN69; Q9XGN1: TTG1; NbExp=3; IntAct=EBI-533348, EBI-395803;
CC Q9FN69; Q9SEI0: WER; NbExp=3; IntAct=EBI-533348, EBI-533373;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:14561633, ECO:0000269|PubMed:15590742}. Note=Moves
CC from developing hair cells (trichoblasts) to developing non-hair cells
CC (atrichoblasts). Also detected in trichome nucleus.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots and flowers. Also present
CC in stems and leaves, and, to a lower extent, in hypocotyls. Expressed
CC in 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:12679534,
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 nitrogen deficiency and UV light. Negatively regulated by
CC MYB66/WER, GL3 and BHLH2 in the developing non-hair cells, and
CC positively regulated by CPC and TRY in the developing hair cells.
CC {ECO:0000269|PubMed:12679534, ECO:0000269|PubMed:15590742,
CC ECO:0000269|PubMed:17053893}.
CC -!- DISRUPTION PHENOTYPE: Plants exhibit two-branched trichomes instead of
CC three-branched trichomes. {ECO:0000269|PubMed:11063707}.
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DR EMBL; AF246291; AAL36964.1; -; mRNA.
DR EMBL; AB006707; BAB08503.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94664.1; -; Genomic_DNA.
DR RefSeq; NP_680372.1; NM_148067.4.
DR AlphaFoldDB; Q9FN69; -.
DR SMR; Q9FN69; -.
DR BioGRID; 19384; 21.
DR IntAct; Q9FN69; 11.
DR STRING; 3702.Q9FN69; -.
DR PaxDb; 3702-AT5G41315-1; -.
DR ProteomicsDB; 228796; -.
DR EnsemblPlants; AT5G41315.1; AT5G41315.1; AT5G41315.
DR GeneID; 834133; -.
DR Gramene; AT5G41315.1; AT5G41315.1; AT5G41315.
DR KEGG; ath:AT5G41315; -.
DR Araport; AT5G41315; -.
DR TAIR; AT5G41315; GL3.
DR eggNOG; ENOG502QT7W; Eukaryota.
DR HOGENOM; CLU_023211_1_1_1; -.
DR InParanoid; Q9FN69; -.
DR PhylomeDB; Q9FN69; -.
DR PRO; PR:Q9FN69; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FN69; baseline and differential.
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:0001708; P:cell fate specification; IMP:TAIR.
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:0031542; P:positive regulation of anthocyanin biosynthetic process; IMP:TAIR.
DR GO; GO:0010091; P:trichome branching; IMP:TAIR.
DR GO; GO:0010026; P:trichome differentiation; IMP:TAIR.
DR CDD; cd11451; bHLH_AtTT8_like; 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR025610; MYC/MYB_N.
DR PANTHER; PTHR46266:SF3; TRANSCRIPTION FACTOR GLABRA 3; 1.
DR PANTHER; PTHR46266; TRANSCRIPTION FACTOR TT8; 1.
DR Pfam; PF14215; bHLH-MYC_N; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 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..637
FT /note="Transcription factor GLABRA 3"
FT /id="PRO_0000285268"
FT DOMAIN 437..486
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 497..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..637
FT /note="Binding with MYB0/GL1 and MYB23"
FT COMPBIAS 497..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 78
FT /note="L->F: In gl3-sst; oddly shaped trichomes with more
FT endoreplication, disturbed cell wall development and
FT abnormal nuclear shape. Reduced interactions with MYB0/GL1
FT and TTG1."
FT /evidence="ECO:0000269|PubMed:14561633"
SQ SEQUENCE 637 AA; 70539 MW; 5225EF0E9745CDB7 CRC64;
MATGQNRTTV PENLKKHLAV SVRNIQWSYG IFWSVSASQS GVLEWGDGYY NGDIKTRKTI
QASEIKADQL GLRRSEQLSE LYESLSVAES SSSGVAAGSQ VTRRASAAAL SPEDLADTEW
YYLVCMSFVF NIGEGMPGRT FANGEPIWLC NAHTADSKVF SRSLLAKSAA VKTVVCFPFL
GGVVEIGTTE HITEDMNVIQ CVKTSFLEAP DPYATILPAR SDYHIDNVLD PQQILGDEIY
APMFSTEPFP TASPSRTTNG FDQEHEQVAD DHDSFMTERI TGGASQVQSW QLMDDELSNC
VHQSLNSSDC VSQTFVEGAA GRVAYGARKS RVQRLGQIQE QQRNVKTLSF DPRNDDVHYQ
SVISTIFKTN HQLILGPQFR NCDKQSSFTR WKKSSSSSSG TATVTAPSQG MLKKIIFDVP
RVHQKEKLML DSPEARDETG NHAVLEKKRR EKLNERFMTL RKIIPSINKI DKVSILDDTI
EYLQELERRV QELESCREST DTETRGTMTM KRKKPCDAGE RTSANCANNE TGNGKKVSVN
NVGEAEPADT GFTGLTDNLR IGSFGNEVVI ELRCAWREGV LLEIMDVISD LHLDSHSVQS
STGDGLLCLT VNCKHKGSKI ATPGMIKEAL QRVAWIC
//
