BH093_ARATH
ID BH093_ARATH Reviewed; 351 AA.
AC Q9LSL1; Q0WPP5; Q8LEZ5;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Transcription factor bHLH93;
DE AltName: Full=Basic helix-loop-helix protein 93;
DE Short=AtbHLH93;
DE Short=bHLH 93;
DE AltName: Full=Transcription factor EN 47;
DE AltName: Full=bHLH transcription factor bHLH093;
GN Name=BHLH93; Synonyms=EN47; OrderedLocusNames=At5g65640;
GN ORFNames=K21L13.16;
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], GENE 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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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 [9]
RP FUNCTION, INTERACTION WITH FAMA, AND TISSUE SPECIFICITY.
RX PubMed=17088607; DOI=10.1105/tpc.106.046136;
RA Ohashi-Ito K., Bergmann D.C.;
RT "Arabidopsis FAMA controls the final proliferation/differentiation switch
RT during stomatal development.";
RL Plant Cell 18:2493-2505(2006).
CC -!- FUNCTION: Transcription factor. May be involved in the differentiation
CC of stomatal guard cells. {ECO:0000269|PubMed:17088607}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with FAMA.
CC {ECO:0000269|PubMed:17088607, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LSL1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LSL1-2; Sequence=VSP_036094;
CC -!- TISSUE SPECIFICITY: Broadly expressed. {ECO:0000269|PubMed:17088607}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AF488621; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AF488621; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB026639; BAA98183.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98080.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98081.1; -; Genomic_DNA.
DR EMBL; BT025665; ABF74726.1; -; mRNA.
DR EMBL; AK229018; BAF00904.1; -; mRNA.
DR EMBL; AY085134; AAM61687.1; -; mRNA.
DR RefSeq; NP_001078801.1; NM_001085332.2. [Q9LSL1-2]
DR RefSeq; NP_569014.1; NM_125962.4. [Q9LSL1-1]
DR AlphaFoldDB; Q9LSL1; -.
DR SMR; Q9LSL1; -.
DR BioGRID; 21932; 1.
DR STRING; 3702.AT5G65640.1; -.
DR PaxDb; Q9LSL1; -.
DR PRIDE; Q9LSL1; -.
DR ProteomicsDB; 240835; -. [Q9LSL1-1]
DR EnsemblPlants; AT5G65640.1; AT5G65640.1; AT5G65640. [Q9LSL1-1]
DR EnsemblPlants; AT5G65640.2; AT5G65640.2; AT5G65640. [Q9LSL1-2]
DR GeneID; 836690; -.
DR Gramene; AT5G65640.1; AT5G65640.1; AT5G65640. [Q9LSL1-1]
DR Gramene; AT5G65640.2; AT5G65640.2; AT5G65640. [Q9LSL1-2]
DR KEGG; ath:AT5G65640; -.
DR Araport; AT5G65640; -.
DR TAIR; locus:2155725; AT5G65640.
DR eggNOG; ENOG502QQHH; Eukaryota.
DR HOGENOM; CLU_035660_1_0_1; -.
DR InParanoid; Q9LSL1; -.
DR OMA; DTRVDIC; -.
DR OrthoDB; 1023623at2759; -.
DR PhylomeDB; Q9LSL1; -.
DR PRO; PR:Q9LSL1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LSL1; baseline and differential.
DR Genevisible; Q9LSL1; 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:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0045487; P:gibberellin catabolic process; IMP:TAIR.
DR GO; GO:0010371; P:regulation of gibberellin biosynthetic process; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
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 Alternative splicing; Developmental protein; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..351
FT /note="Transcription factor bHLH93"
FT /id="PRO_0000358784"
FT DOMAIN 174..223
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT VAR_SEQ 268..350
FT /note="FEIDRRDEDTRVDICCSPKPGLLLSTVNTLETLGLEIEQCVISCFSDFSLQA
FT SCSEGAEQRDFITSEDIKQALFRNAGYGGSC -> IVETRILELIYAARQNRDCYYL
FT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_036094"
SQ SEQUENCE 351 AA; 39484 MW; A28579226445A459 CRC64;
MELSTQMNVF EELLVPTKQE TTDNNINNLS FNGGFDHHHH QFFPNGYNID YLCFNNEEED
ENTLLYPSSF MDLISQPPPL LLHQPPPLQP LSPPLSSSAT AGATFDYPFL EALQEIIDSS
SSSPPLILQN GQEENFNNPM SYPSPLMESD QSKSFSVGYC GGETNKKKSK KLEGQPSKNL
MAERRRRKRL NDRLSMLRSI VPKISKMDRT SILGDAIDYM KELLDKINKL QDEEQELGNS
NNSHHSKLFG DLKDLNANEP LVRNSPKFEI DRRDEDTRVD ICCSPKPGLL LSTVNTLETL
GLEIEQCVIS CFSDFSLQAS CSEGAEQRDF ITSEDIKQAL FRNAGYGGSC L
