MUTE_ARATH
ID MUTE_ARATH Reviewed; 202 AA.
AC Q9M8K6; A0MEU5;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Transcription factor MUTE;
DE AltName: Full=Basic helix-loop-helix protein 45;
DE Short=AtbHLH45;
DE Short=bHLH 45;
DE AltName: Full=Transcription factor EN 20;
DE AltName: Full=bHLH transcription factor bHLH045;
GN Name=MUTE; Synonyms=BHLH45, EN20; OrderedLocusNames=At3g06120;
GN ORFNames=F28L1.6;
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, INDUCTION, GENE FAMILY, AND
RP NOMENCLATURE.
RC STRAIN=cv. Columbia; TISSUE=Flower;
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 / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=17183267; DOI=10.1038/nature05467;
RA Pillitteri L.J., Sloan D.B., Bogenschutz N.L., Torii K.U.;
RT "Termination of asymmetric cell division and differentiation of stomata.";
RL Nature 445:501-505(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
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 REVIEW.
RX PubMed=17691100; DOI=10.1002/bies.20625;
RA Pillitteri L.J., Torii K.U.;
RT "Breaking the silence: three bHLH proteins direct cell-fate decisions
RT during stomatal development.";
RL Bioessays 29:861-870(2007).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17183265; DOI=10.1038/nature05491;
RA MacAlister C.A., Ohashi-Ito K., Bergmann D.C.;
RT "Transcription factor control of asymmetric cell divisions that establish
RT the stomatal lineage.";
RL Nature 445:537-540(2007).
RN [10]
RP REVIEW.
RX PubMed=17928257; DOI=10.1016/j.tplants.2007.08.016;
RA Serna L.;
RT "bHLH proteins know when to make a stoma.";
RL Trends Plant Sci. 12:483-485(2007).
CC -!- FUNCTION: Transcription factor. Together with FMA and SPCH, regulates
CC the stomata formation. Required for the differentiation of stomatal
CC guard cells, by promoting successive asymmetric cell divisions and the
CC formation of guard mother cells. Promotes the conversion of the leaf
CC epidermis into stomata. {ECO:0000269|PubMed:17183265,
CC ECO:0000269|PubMed:17183267}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:17183267}.
CC -!- TISSUE SPECIFICITY: Leaf epidermis and flowers.
CC {ECO:0000269|PubMed:12679534, ECO:0000269|PubMed:17183265}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in meristemoids and at lower
CC levels in guard mother cells (GMCs) and guard cells.
CC {ECO:0000269|PubMed:17183265, ECO:0000269|PubMed:17183267}.
CC -!- INDUCTION: By UV, flagellin, and jasmonic acid (JA) treatments.
CC {ECO:0000269|PubMed:12679534}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK28545.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF488580; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DQ863645; ABI74926.1; -; mRNA.
DR EMBL; DQ864972; ABI34465.1; -; Genomic_DNA.
DR EMBL; AC018907; AAF30305.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74347.1; -; Genomic_DNA.
DR EMBL; DQ446639; ABE65920.1; -; mRNA.
DR EMBL; DQ653068; ABK28545.1; ALT_SEQ; mRNA.
DR RefSeq; NP_187263.1; NM_111487.3.
DR AlphaFoldDB; Q9M8K6; -.
DR SMR; Q9M8K6; -.
DR BioGRID; 5120; 5.
DR IntAct; Q9M8K6; 2.
DR STRING; 3702.AT3G06120.1; -.
DR PaxDb; Q9M8K6; -.
DR PRIDE; Q9M8K6; -.
DR EnsemblPlants; AT3G06120.1; AT3G06120.1; AT3G06120.
DR GeneID; 819785; -.
DR Gramene; AT3G06120.1; AT3G06120.1; AT3G06120.
DR KEGG; ath:AT3G06120; -.
DR Araport; AT3G06120; -.
DR TAIR; locus:2082400; AT3G06120.
DR eggNOG; ENOG502QPVA; Eukaryota.
DR HOGENOM; CLU_044652_4_1_1; -.
DR InParanoid; Q9M8K6; -.
DR OMA; VQQSFCS; -.
DR OrthoDB; 1487079at2759; -.
DR PhylomeDB; Q9M8K6; -.
DR PRO; PR:Q9M8K6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M8K6; baseline and differential.
DR Genevisible; Q9M8K6; AT.
DR GO; GO:0005634; C:nucleus; IDA: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; IPI:TAIR.
DR GO; GO:0009913; P:epidermal cell differentiation; IMP:TAIR.
DR GO; GO:0010052; P:guard cell differentiation; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0010374; P:stomatal complex development; IMP:TAIR.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR044283; FAMA/SPEECHLESS/MUTE.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR PANTHER; PTHR46684; PTHR46684; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..202
FT /note="Transcription factor MUTE"
FT /id="PRO_0000358849"
FT DOMAIN 1..49
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
SQ SEQUENCE 202 AA; 22843 MW; 0F492189A0895B6B CRC64;
MSHIAVERNR RRQMNEHLKS LRSLTPCFYI KRGDQASIIG GVIEFIKELQ QLVQVLESKK
RRKTLNRPSF PYDHQTIEPS SLGAATTRVP FSRIENVMTT STFKEVGACC NSPHANVEAK
ISGSNVVLRV VSRRIVGQLV KIISVLEKLS FQVLHLNISS MEETVLYFFV VKIGLECHLS
LEELTLEVQK SFVSDEVIVS TN