BH109_ARATH
ID BH109_ARATH Reviewed; 185 AA.
AC Q5XVH0; Q5XVH1; Q7XHI8; Q9C9F9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Transcription factor bHLH109;
DE AltName: Full=Basic helix-loop-helix protein 109;
DE Short=AtbHLH109;
DE Short=bHLH 109;
DE AltName: Full=bHLH transcription factor bHLH109;
GN Name=BHLH109; OrderedLocusNames=At1g68240; ORFNames=T22E19.13;
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] (ISOFORM 3), 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;
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 [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] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RX PubMed=12481096; DOI=10.1104/pp.010207;
RA Xiao Y.-L., Malik M., Whitelaw C.A., Town C.D.;
RT "Cloning and sequencing of cDNAs for hypothetical genes from chromosome 2
RT of Arabidopsis.";
RL Plant Physiol. 130:2118-2128(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=23874927; DOI=10.1371/journal.pone.0069261;
RA Gliwicka M., Nowak K., Balazadeh S., Mueller-Roeber B., Gaj M.D.;
RT "Extensive modulation of the transcription factor transcriptome during
RT somatic embryogenesis in Arabidopsis thaliana.";
RL PLoS ONE 8:E69261-E69261(2013).
RN [7]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=26973252; DOI=10.1016/j.jplph.2016.02.012;
RA Nowak K., Gaj M.D.;
RT "Stress-related function of bHLH109 in somatic embryo induction in
RT Arabidopsis.";
RL J. Plant Physiol. 193:119-126(2016).
CC -!- FUNCTION: Transcription factor involved in somatic embryogenesis. Acts
CC as positive regulator of somatic embryo formation (PubMed:23874927,
CC PubMed:26973252). Acts as positive regulator of ECP63 by targeting its
CC promoter and inducing its expression (PubMed:26973252).
CC {ECO:0000269|PubMed:23874927, ECO:0000269|PubMed:26973252}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- INTERACTION:
CC Q5XVH0; Q9LT23-2: BHLH121; NbExp=3; IntAct=EBI-15193531, EBI-15197803;
CC Q5XVH0; Q9LXD8: HEC3; NbExp=5; IntAct=EBI-15193531, EBI-1536734;
CC Q5XVH0; Q8L5W8: PIL1; NbExp=3; IntAct=EBI-15193531, EBI-630752;
CC Q5XVH0; Q9C707: RHD6; NbExp=3; IntAct=EBI-15193531, EBI-4424338;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5XVH0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5XVH0-2; Sequence=VSP_036098;
CC Name=3;
CC IsoId=Q5XVH0-3; Sequence=VSP_036097;
CC -!- DEVELOPMENTAL STAGE: Expressed during somatic embryogenesis.
CC {ECO:0000269|PubMed:26973252}.
CC -!- SIMILARITY: Belongs to the bHLH protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52603.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ577585; CAE12172.1; -; mRNA.
DR EMBL; AC016447; AAG52603.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34770.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34771.1; -; Genomic_DNA.
DR EMBL; AY735551; AAU44421.1; -; mRNA.
DR EMBL; AY735552; AAU44422.1; -; mRNA.
DR EMBL; AY924719; AAX23794.1; -; mRNA.
DR PIR; H96705; H96705.
DR RefSeq; NP_001031251.1; NM_001036174.2. [Q5XVH0-2]
DR RefSeq; NP_176991.2; NM_105495.3. [Q5XVH0-1]
DR AlphaFoldDB; Q5XVH0; -.
DR SMR; Q5XVH0; -.
DR BioGRID; 28374; 24.
DR IntAct; Q5XVH0; 24.
DR STRING; 3702.AT1G68240.1; -.
DR PaxDb; Q5XVH0; -.
DR PRIDE; Q5XVH0; -.
DR EnsemblPlants; AT1G68240.1; AT1G68240.1; AT1G68240. [Q5XVH0-1]
DR EnsemblPlants; AT1G68240.2; AT1G68240.2; AT1G68240. [Q5XVH0-2]
DR GeneID; 843153; -.
DR Gramene; AT1G68240.1; AT1G68240.1; AT1G68240. [Q5XVH0-1]
DR Gramene; AT1G68240.2; AT1G68240.2; AT1G68240. [Q5XVH0-2]
DR KEGG; ath:AT1G68240; -.
DR Araport; AT1G68240; -.
DR TAIR; locus:2199307; AT1G68240.
DR HOGENOM; CLU_1404194_0_0_1; -.
DR InParanoid; Q5XVH0; -.
DR OMA; HKEGTHE; -.
DR PhylomeDB; Q5XVH0; -.
DR PRO; PR:Q5XVH0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q5XVH0; baseline and differential.
DR Genevisible; Q5XVH0; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010262; P:somatic embryogenesis; IMP:UniProtKB.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR031066; bHLH_ALC-like_plant.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR PANTHER; PTHR45855; PTHR45855; 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 Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..185
FT /note="Transcription factor bHLH109"
FT /id="PRO_0000358795"
FT DOMAIN 67..117
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT VAR_SEQ 123
FT /note="V -> VSIKLYLI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12679534"
FT /id="VSP_036097"
FT VAR_SEQ 175..185
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12481096"
FT /id="VSP_036098"
FT CONFLICT 78
FT /note="Missing (in Ref. 1; CAE12172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 185 AA; 21674 MW; F603DEAE296A07DC CRC64;
MERNNRNEGT HEEEQCSLSD IIYSFCSENH SELNPLQEIF GVTKNNDHEK HDEEPDEESY
RMAKRQRSME YRMMMEKKRR KEIKDKVDIL QGLMPNHCTK PDLASKLENI IEYIKSLKYQ
VDVMSMAYTT TPVYTPPFYA AAQAPCMSPW GYYTPGVPMM PQQNMTYIPQ YPQVYGTVPP
NQTQP
