BH078_ARATH
ID BH078_ARATH Reviewed; 498 AA.
AC Q9FJL4; Q8S3D4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Transcription factor bHLH78;
DE AltName: Full=Basic helix-loop-helix protein 78;
DE Short=AtbHLH78;
DE Short=bHLH 78;
DE AltName: Full=Transcription factor EN 86;
DE AltName: Full=bHLH transcription factor bHLH078;
GN Name=BHLH78; Synonyms=CIB2, EN86; OrderedLocusNames=At5g48560;
GN ORFNames=K15N18.2;
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, GENE FAMILY, AND
RP 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=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
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 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, AND INTERACTION WITH CRY2.
RX PubMed=24130508; DOI=10.1371/journal.pgen.1003861;
RA Liu Y., Li X., Li K., Liu H., Lin C.;
RT "Multiple bHLH proteins form heterodimers to mediate CRY2-dependent
RT regulation of flowering-time in Arabidopsis.";
RL PLoS Genet. 9:E1003861-E1003861(2013).
CC -!- FUNCTION: Transcription factor that binds DNA to G box 5'-CACGTG-3' and
CC to E-box 5'-CANNTG-3' (By similarity). Binds to chromatin DNA of the FT
CC gene and promotes its expression, and thus triggers flowering in
CC response to blue light (PubMed:24130508).
CC {ECO:0000250|UniProtKB:Q8GY61, ECO:0000269|PubMed:24130508}.
CC -!- SUBUNIT: Homodimer (Probable). Binds reversibly to CRY2 after blue
CC light illumination (PubMed:24130508). {ECO:0000269|PubMed:24130508,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- TISSUE SPECIFICITY: Expressed constitutively in roots, leaves, stems,
CC and flowers. {ECO:0000269|PubMed:12679534}.
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DR EMBL; AF488610; AAM10957.1; -; mRNA.
DR EMBL; AB015468; BAB10689.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95688.1; -; Genomic_DNA.
DR EMBL; BT002945; AAO22758.1; -; mRNA.
DR EMBL; BT005637; AAO64057.1; -; mRNA.
DR RefSeq; NP_199667.1; NM_124232.4.
DR AlphaFoldDB; Q9FJL4; -.
DR SMR; Q9FJL4; -.
DR BioGRID; 20158; 3.
DR IntAct; Q9FJL4; 1.
DR STRING; 3702.AT5G48560.1; -.
DR PaxDb; Q9FJL4; -.
DR EnsemblPlants; AT5G48560.1; AT5G48560.1; AT5G48560.
DR GeneID; 834912; -.
DR Gramene; AT5G48560.1; AT5G48560.1; AT5G48560.
DR KEGG; ath:AT5G48560; -.
DR Araport; AT5G48560; -.
DR TAIR; locus:2152551; AT5G48560.
DR eggNOG; ENOG502QRSF; Eukaryota.
DR HOGENOM; CLU_025018_6_1_1; -.
DR InParanoid; Q9FJL4; -.
DR OMA; FGQTANR; -.
DR OrthoDB; 616690at2759; -.
DR PhylomeDB; Q9FJL4; -.
DR PRO; PR:Q9FJL4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJL4; baseline and differential.
DR Genevisible; Q9FJL4; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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; TAS:TAIR.
DR GO; GO:0009637; P:response to blue light; IDA:UniProtKB.
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 DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..498
FT /note="Transcription factor bHLH78"
FT /id="PRO_0000358770"
FT DOMAIN 307..357
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 280
FT /note="E -> G (in Ref. 1; AAM10957)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 54878 MW; 848D588791A15E52 CRC64;
MDNELFMNTE FPPPPEMATH FEHQQSSSSA MMLNWALMDP NPHQDSSFLW EKSTEQQQQQ
SIFDSALSSL VSSPTPSNSN FSGGGGDGFL IRELIGKLGN IGNNNNNSGE IYGTPMSRSA
SCYATPMSSP PPPTNSNSQM MMNRTTPLTE FSADPGFAER AARFSCFGSR SFNGRTNTNL
PINNGNNMVN NSGKLTRVSS TPALKALVSP EVTPGGEFSR KRKSVPKGKS KENPISTASP
SPSFSKTAEK NGGKGGSKSS EEKGGKRRRE EEDDEEEEGE GEGNKSNNTK PPEPPKDYIH
VRARRGQATD SHSLAERVRR EKIGERMKLL QDLVPGCNKV TGKALMLDEI INYVQSLQRQ
VEFLSMKLSS VNDTRLDFNV DALVSKDVMI PSSNNRLHEE GLQSKSSSHH HQQQLNIYNN
NSQLLPNISS NNMMLQSPMN SLETSTLARS FTHLPTLTQF TDSISQYQMF SEEDLQSIVG
MGVAENPNNE SQHMKIEL
