HBI1_ARATH
ID HBI1_ARATH Reviewed; 337 AA.
AC Q9ZPW3; Q8S3D8; Q945K8;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 3.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Transcription factor HBI1;
DE AltName: Full=Basic helix-loop-helix protein 64;
DE Short=AtbHLH64;
DE Short=bHLH 64;
DE AltName: Full=Protein HOMOLOG OF BEE2 INTERACTING WITH IBH1;
DE AltName: Full=Transcription factor EN 79;
DE AltName: Full=bHLH transcription factor bHLH064;
GN Name=HBI1; Synonyms=BHLH64, EN79; OrderedLocusNames=At2g18300;
GN ORFNames=T30D6.19;
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 [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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-337 (ISOFORM 1), TISSUE SPECIFICITY, GENE
RP FAMILY, AND 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 [5]
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 [6]
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 [7]
RP FUNCTION, INTERACTION WITH IBH1, AND TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Atypical bHLH transcription factor that acts as positive
CC regulator of cell elongation downstream of multiple external and
CC endogenous signals by direct binding to the promoters and activation of
CC the two expansin genes EXPA1 and EXPA8, encoding cell wall loosening
CC enzymes. Transcriptional activity is inhibited when binding to the bHLH
CC transcription factor IBH1. {ECO:0000269|PubMed:23221598}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with IBH1.
CC {ECO:0000269|PubMed:23221598, ECO:0000305}.
CC -!- INTERACTION:
CC Q9ZPW3-2; Q9C8Z9: BHLH148; NbExp=4; IntAct=EBI-15197377, EBI-4434374;
CC Q9ZPW3-2; Q9M0B9: IBL1; NbExp=3; IntAct=EBI-15197377, EBI-15192969;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ZPW3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ZPW3-2; Sequence=VSP_036089;
CC -!- TISSUE SPECIFICITY: Highly expressed in hypocotyls and cotyledons.
CC Expressed in leaves, stems, and flowers. {ECO:0000269|PubMed:12679534,
CC ECO:0000269|PubMed:23221598}.
CC -!- MISCELLANEOUS: Plants over-expressing HBI1 show increased petiole
CC length and early flowering, and plants suppressing HBI1 display dwarf,
CC short-petiole and late-flowering phenotype. Although HBI1 contains a
CC degenerate basic motif it can bind DNA in vitro.
CC {ECO:0000305|PubMed:23221598}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
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DR EMBL; AC006439; AAD15506.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC06752.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06753.1; -; Genomic_DNA.
DR EMBL; AF412099; AAL06552.1; -; mRNA.
DR EMBL; AY078030; AAL77731.1; -; mRNA.
DR EMBL; AF488597; AAM10953.1; -; mRNA.
DR PIR; G84562; G84562.
DR RefSeq; NP_565434.1; NM_127388.4. [Q9ZPW3-2]
DR RefSeq; NP_849976.1; NM_179645.3. [Q9ZPW3-1]
DR AlphaFoldDB; Q9ZPW3; -.
DR SMR; Q9ZPW3; -.
DR BioGRID; 1703; 24.
DR IntAct; Q9ZPW3; 22.
DR STRING; 3702.AT2G18300.3; -.
DR PaxDb; Q9ZPW3; -.
DR ProteomicsDB; 247163; -. [Q9ZPW3-1]
DR EnsemblPlants; AT2G18300.1; AT2G18300.1; AT2G18300. [Q9ZPW3-2]
DR EnsemblPlants; AT2G18300.2; AT2G18300.2; AT2G18300. [Q9ZPW3-1]
DR GeneID; 816346; -.
DR Gramene; AT2G18300.1; AT2G18300.1; AT2G18300. [Q9ZPW3-2]
DR Gramene; AT2G18300.2; AT2G18300.2; AT2G18300. [Q9ZPW3-1]
DR KEGG; ath:AT2G18300; -.
DR Araport; AT2G18300; -.
DR eggNOG; ENOG502SH3S; Eukaryota.
DR InParanoid; Q9ZPW3; -.
DR PhylomeDB; Q9ZPW3; -.
DR PRO; PR:Q9ZPW3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZPW3; baseline and differential.
DR Genevisible; Q9ZPW3; 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; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
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 Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR024097; bHLH_ZIP_TF.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR PANTHER; PTHR12565; PTHR12565; 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; Brassinosteroid signaling pathway; DNA-binding;
KW Gibberellin signaling pathway; Growth regulation; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..337
FT /note="Transcription factor HBI1"
FT /id="PRO_0000358759"
FT DOMAIN 191..241
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 119..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 271..272
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_036089"
FT CONFLICT 302..303
FT /note="LS -> SF (in Ref. 4; AAM10953)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="S -> F (in Ref. 4; AAM10953)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 37747 MW; 60043122CB19CE59 CRC64;
MLEGLVSQES LSLNSMDMSV LERLKWVQQQ QQQLQQVVSH SSNNSPELLQ ILQFHGSNND
ELLESSFSQF QMLGSGFGPN YNMGFGPPHE SISRTSSCHM EPVDTMEVLL KTGEETRAVA
LKNKRKPEVK TREEQKTEKK IKVEAETESS MKGKSNMGNT EASSDTSKET SKGASENQKL
DYIHVRARRG QATDRHSLAE RARREKISKK MKYLQDIVPG CNKVTGKAGM LDEIINYVQC
LQRQVEFLSM KLAVLNPELE LAVEDVSVKQ FQAYFTNVVA SKQSIMVDVP LFPLDQQGSL
DLSAINPNQT TSIEAPSGSW ETQSQSLYNT SSLGFHY
