IBH1_ARATH
ID IBH1_ARATH Reviewed; 156 AA.
AC Q9SKX1;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Transcription factor IBH1;
DE Short=AtIBH1;
DE AltName: Full=BHLH transcription factor zeta;
DE Short=bHLH zeta;
DE AltName: Full=Basic helix-loop-helix protein 158;
DE Short=AtbHLH158;
DE Short=bHLH 158;
DE AltName: Full=Protein ILI1-BINDING BHLH 1;
DE AltName: Full=bHLH transcription factor bHLH158;
GN Name=IBH1; Synonyms=BHLH158; OrderedLocusNames=At2g43060; ORFNames=MFL8.8;
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.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, INTERACTION WITH PRE1, AND TISSUE SPECIFICITY.
RX PubMed=20009022; DOI=10.1105/tpc.109.070441;
RA Zhang L.Y., Bai M.Y., Wu J., Zhu J.Y., Wang H., Zhang Z., Wang W., Sun Y.,
RA Zhao J., Sun X., Yang H., Xu Y., Kim S.H., Fujioka S., Lin W.H., Chong K.,
RA Lu T., Wang Z.Y.;
RT "Antagonistic HLH/bHLH transcription factors mediate brassinosteroid
RT regulation of cell elongation and plant development in rice and
RT Arabidopsis.";
RL Plant Cell 21:3767-3780(2009).
RN [6]
RP FUNCTION, INTERACTION WITH PRE1; PRE3; PRE4; PRE5; BHLH49; BHLH63; BHLH74;
RP BHLH76 AND BHLH77, AND SUBCELLULAR LOCATION.
RX PubMed=23161888; DOI=10.1105/tpc.112.105023;
RA Ikeda M., Fujiwara S., Mitsuda N., Ohme-Takagi M.;
RT "A triantagonistic basic helix-loop-helix system regulates cell elongation
RT in Arabidopsis.";
RL Plant Cell 24:4483-4497(2012).
RN [7]
RP FUNCTION, AND INTERACTION WITH HBI1 AND PRE1.
RX PubMed=23221598; DOI=10.1105/tpc.112.105163;
RA Bai M.Y., Fan M., Oh E., Wang Z.Y.;
RT "A triple helix-loop-helix/basic helix-loop-helix cascade controls cell
RT elongation downstream of multiple hormonal and environmental signaling
RT pathways in Arabidopsis.";
RL Plant Cell 24:4917-4929(2012).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24505057; DOI=10.1073/pnas.1400203111;
RA Zhiponova M.K., Morohashi K., Vanhoutte I., Machemer-Noonan K.,
RA Revalska M., Van Montagu M., Grotewold E., Russinova E.;
RT "Helix-loop-helix/basic helix-loop-helix transcription factor network
RT represses cell elongation in Arabidopsis through an apparent incoherent
RT feed-forward loop.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:2824-2829(2014).
CC -!- FUNCTION: Atypical and probable non DNA-binding bHLH transcription
CC factor that acts as transcriptional repressor that negatively regulates
CC cell and organ elongation in response to gibberellin (GA) and
CC brassinosteroid (BR) signaling. Is able to form heterodimer with
CC BHLH49, thus inhibiting DNA binding of BHLH49, which is a
CC transcriptional activator that regulates the expression of a subset of
CC genes involved in cell expansion by binding to the G-box motif. Binds
CC and inhibits HBI1, a positive regulator of cell elongation that
CC directly binds to the promoters and activated the two expansin genes
CC EXPA1 and EXPA8, encoding cell wall loosening enzymes. The ability of
CC IBH1 to inhibit BHLH49 and HBI1 is counteracted by binding to the
CC antagonist bHLH transcription factor PRE1, restoring the
CC transcriptional activity of BHLH49 and HBI1 and resulting in induction
CC of cell elongation. Functions redundantly with IBL1/BHLH159 in a
CC regulation node known as the incoherent feed-forward loop (FFL)
CC (PubMed:24505057). {ECO:0000269|PubMed:20009022,
CC ECO:0000269|PubMed:23161888, ECO:0000269|PubMed:23221598,
CC ECO:0000269|PubMed:24505057}.
CC -!- SUBUNIT: Interacts with PRE1, PRE3, PRE4, PRE5, HBI1, BHLH49, BHLH63,
CC BHLH74, BHLH76 and BHLH77. {ECO:0000269|PubMed:20009022,
CC ECO:0000269|PubMed:23161888, ECO:0000269|PubMed:23221598}.
CC -!- INTERACTION:
CC Q9SKX1; Q93VJ4: BEE2; NbExp=4; IntAct=EBI-4433589, EBI-4424312;
CC Q9SKX1; Q8GY61: BHLH63; NbExp=3; IntAct=EBI-4433589, EBI-4469930;
CC Q9SKX1; Q9SZI2: NAP1;1; NbExp=4; IntAct=EBI-4433589, EBI-4424361;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:23161888}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots and at lower levels in
CC rosette leaves, stems and cauline leaves.
CC {ECO:0000269|PubMed:20009022}.
CC -!- INDUCTION: Repressed by epibrassinolide.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:24505057}.
CC -!- MISCELLANEOUS: Plants over-expressing IBH1 are dwarf with round-shaped,
CC dark-green leaves, short petioles, siliques and roots, and are
CC insensitive to brassinosteroid (PubMed:20009022, PubMed:23161888,
CC PubMed:23221598). Plants silencing IBH1 exhibit increased length of
CC hypocotyls and leaves (PubMed:23161888). {ECO:0000305|PubMed:20009022,
CC ECO:0000305|PubMed:23161888, ECO:0000305|PubMed:23221598}.
CC -!- SIMILARITY: Belongs to the bHLH protein family. {ECO:0000305}.
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DR EMBL; AJ576045; CAE09172.1; -; mRNA.
DR EMBL; AC006224; AAD22125.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10204.1; -; Genomic_DNA.
DR EMBL; AY062456; AAL32534.1; -; mRNA.
DR EMBL; AY093279; AAM13278.1; -; mRNA.
DR PIR; E84861; E84861.
DR RefSeq; NP_181834.1; NM_129867.3.
DR AlphaFoldDB; Q9SKX1; -.
DR SMR; Q9SKX1; -.
DR BioGRID; 4245; 16.
DR IntAct; Q9SKX1; 16.
DR STRING; 3702.AT2G43060.1; -.
DR iPTMnet; Q9SKX1; -.
DR PaxDb; Q9SKX1; -.
DR PRIDE; Q9SKX1; -.
DR ProteomicsDB; 232144; -.
DR EnsemblPlants; AT2G43060.1; AT2G43060.1; AT2G43060.
DR GeneID; 818908; -.
DR Gramene; AT2G43060.1; AT2G43060.1; AT2G43060.
DR KEGG; ath:AT2G43060; -.
DR Araport; AT2G43060; -.
DR TAIR; locus:2053718; AT2G43060.
DR eggNOG; ENOG502S9NU; Eukaryota.
DR HOGENOM; CLU_101547_1_0_1; -.
DR InParanoid; Q9SKX1; -.
DR OMA; SRIHRAT; -.
DR OrthoDB; 1453189at2759; -.
DR PRO; PR:Q9SKX1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SKX1; baseline and differential.
DR Genevisible; Q9SKX1; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0009742; P:brassinosteroid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR CDD; cd11444; bHLH_AtIBH1_like; 1.
DR InterPro; IPR044549; bHLH_AtIBH1-like.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR044660; IBH1-like.
DR PANTHER; PTHR33124; PTHR33124; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
PE 1: Evidence at protein level;
KW Brassinosteroid signaling pathway; Gibberellin signaling pathway;
KW Growth regulation; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..156
FT /note="Transcription factor IBH1"
FT /id="PRO_0000429104"
FT DOMAIN 90..139
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
SQ SEQUENCE 156 AA; 17825 MW; 7D8C75BE4047A48A CRC64;
MASADKLINT DVPEKDVFAF HFLQSLSNLR KQNPFDTPDQ KNYRVRKIKK AAYVSMARAA
GGSSRLWSRA LLRRADKDDN KIVRFSRRKW KISSKRRRSN QRAPVVEEAA ERLRNLVPGG
GGMETSKLME ETAHYIKCLS MQVKVMQCLV DGLSPK
