BH068_ARATH
ID BH068_ARATH Reviewed; 407 AA.
AC Q8S3D1; Q9SZD9;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Transcription factor bHLH68;
DE AltName: Full=Basic helix-loop-helix protein 68;
DE Short=AtbHLH68;
DE Short=bHLH 68;
DE AltName: Full=Transcription factor EN 60;
DE AltName: Full=bHLH transcription factor bHLH068;
GN Name=BHLH68; Synonyms=EN60; OrderedLocusNames=At4g29100;
GN ORFNames=F19B15.130;
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;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 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).
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- INTERACTION:
CC Q8S3D1; Q93Y00: BHLH7; NbExp=4; IntAct=EBI-15192111, EBI-4442198;
CC Q8S3D1; Q9ZUG9: LRL1; NbExp=3; IntAct=EBI-15192111, EBI-15195343;
CC Q8S3D1; Q9C598: NAC081; NbExp=3; IntAct=EBI-15192111, EBI-1998565;
CC Q8S3D1; Q93Z00: TCP14; NbExp=3; IntAct=EBI-15192111, EBI-4424563;
CC Q8S3D1; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-15192111, EBI-4426144;
CC Q8S3D1; Q8LPR5: TCP4; NbExp=3; IntAct=EBI-15192111, EBI-15192325;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
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DR EMBL; AF488634; AAM10966.2; -; mRNA.
DR EMBL; AL078470; CAB43924.1; -; Genomic_DNA.
DR EMBL; AL161574; CAB79668.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85586.1; -; Genomic_DNA.
DR EMBL; AY081316; AAL91205.1; -; mRNA.
DR EMBL; BT000121; AAN15440.1; -; mRNA.
DR PIR; T08965; T08965.
DR RefSeq; NP_194639.1; NM_119054.6.
DR AlphaFoldDB; Q8S3D1; -.
DR SMR; Q8S3D1; -.
DR BioGRID; 14318; 25.
DR IntAct; Q8S3D1; 25.
DR STRING; 3702.AT4G29100.1; -.
DR PaxDb; Q8S3D1; -.
DR PRIDE; Q8S3D1; -.
DR ProteomicsDB; 240350; -.
DR EnsemblPlants; AT4G29100.1; AT4G29100.1; AT4G29100.
DR GeneID; 829031; -.
DR Gramene; AT4G29100.1; AT4G29100.1; AT4G29100.
DR KEGG; ath:AT4G29100; -.
DR Araport; AT4G29100; -.
DR TAIR; locus:2119901; AT4G29100.
DR eggNOG; ENOG502QUMC; Eukaryota.
DR HOGENOM; CLU_041735_3_0_1; -.
DR InParanoid; Q8S3D1; -.
DR OrthoDB; 932715at2759; -.
DR PhylomeDB; Q8S3D1; -.
DR PRO; PR:Q8S3D1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8S3D1; baseline and differential.
DR Genevisible; Q8S3D1; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR CDD; cd11393; bHLH_AtbHLH_like; 1.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR045239; bHLH95_bHLH.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
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..407
FT /note="Transcription factor bHLH68"
FT /id="PRO_0000358762"
FT DOMAIN 253..302
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 56..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 44584 MW; 9100CCF1F7E9B544 CRC64;
MNRGVLESSP VQQLMAAGNP NWWNVSGGMR PPPPLMGHQQ APLPPHMTPN NNYLRPRMMP
TPFPHFLPSP ATSSSSSSSS PSLPNNPNLS SWLESNDLPP ESWSLSQLLL GGLMMGEEER
LEMMNHHNHH DEQQHHGFQG KIRLENWEEQ VLSHQQASMV AVDIKQEGNI NNNNGYVISS
PNSPPNKSCV TTTTTTSLNS NDDNINNNNN MLDFSSNHNG LHLSEGRHTP PDRSSECNSL
EIGGSTNKKP RLQPSPSSQS TLKVRKEKLG GRIAALHQLV SPFGKTDTAS VLSEAIGYIR
FLQSQIEALS HPYFGTTASG NMRHQQHLQG DRSCIFPEDP GQLVNDQCMK RRGASSSSTD
NQNASEEPKK DLRSRGLCLV PISCTLQVGS DNGADYWAPA LGSAGFH
