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BH011_ARATH
ID   BH011_ARATH             Reviewed;         286 AA.
AC   Q8W2F2; O65643; Q8RX65;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Transcription factor bHLH11;
DE   AltName: Full=Basic helix-loop-helix protein 11;
DE            Short=AtbHLH11;
DE            Short=bHLH 11;
DE   AltName: Full=Transcription factor EN 137;
DE   AltName: Full=bHLH transcription factor bHLH011;
GN   Name=BHLH11; Synonyms=EN137; OrderedLocusNames=At4g36060;
GN   ORFNames=T19K4.190;
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 1), TISSUE SPECIFICITY, GENE FAMILY,
RP   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] (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   [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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8W2F2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8W2F2-2; Sequence=VSP_036074, VSP_036075;
CC   -!- TISSUE SPECIFICITY: Expressed consitutively in roots, leaves, stems,
CC       and flowers. {ECO:0000269|PubMed:12679534}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA18500.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB81515.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF251696; AAL55718.2; -; mRNA.
DR   EMBL; AL022373; CAA18500.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161588; CAB81515.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE86608.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86609.1; -; Genomic_DNA.
DR   EMBL; AY090362; AAL91266.1; -; mRNA.
DR   EMBL; BT000535; AAN18104.1; -; mRNA.
DR   PIR; T05498; T05498.
DR   RefSeq; NP_195330.2; NM_119773.3. [Q8W2F2-2]
DR   RefSeq; NP_849566.1; NM_179235.3. [Q8W2F2-1]
DR   AlphaFoldDB; Q8W2F2; -.
DR   SMR; Q8W2F2; -.
DR   BioGRID; 15044; 4.
DR   IntAct; Q8W2F2; 3.
DR   STRING; 3702.AT4G36060.1; -.
DR   PaxDb; Q8W2F2; -.
DR   PRIDE; Q8W2F2; -.
DR   ProteomicsDB; 241220; -. [Q8W2F2-1]
DR   EnsemblPlants; AT4G36060.1; AT4G36060.1; AT4G36060. [Q8W2F2-1]
DR   EnsemblPlants; AT4G36060.2; AT4G36060.2; AT4G36060. [Q8W2F2-2]
DR   GeneID; 829762; -.
DR   Gramene; AT4G36060.1; AT4G36060.1; AT4G36060. [Q8W2F2-1]
DR   Gramene; AT4G36060.2; AT4G36060.2; AT4G36060. [Q8W2F2-2]
DR   KEGG; ath:AT4G36060; -.
DR   Araport; AT4G36060; -.
DR   TAIR; locus:2135169; AT4G36060.
DR   eggNOG; ENOG502QRHF; Eukaryota.
DR   InParanoid; Q8W2F2; -.
DR   OMA; SQRTECK; -.
DR   PhylomeDB; Q8W2F2; -.
DR   PRO; PR:Q8W2F2; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8W2F2; baseline and differential.
DR   Genevisible; Q8W2F2; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
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:0055072; P:iron ion homeostasis; IEA:InterPro.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR044579; bHLH11/121.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   PANTHER; PTHR47001; PTHR47001; 2.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..286
FT                   /note="Transcription factor bHLH11"
FT                   /id="PRO_0000358728"
FT   DOMAIN          44..94
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        182..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..18
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_036074"
FT   VAR_SEQ         19..31
FT                   /note="SSASSSSSSGQNL -> MAVSCLFIVSSNY (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_036075"
FT   CONFLICT        143
FT                   /note="R -> G (in Ref. 4; AAN18104/AAL91266)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   286 AA;  31785 MW;  4BB093FEB87AB200 CRC64;
     MDQPMKPKTC SESDFADDSS ASSSSSSGQN LRGAEMVVEV KKEAVCSQKA EREKLRRDKL
     KEQFLELGNA LDPNRPKSDK ASVLTDTIQM LKDVMNQVDR LKAEYETLSQ ESRELIQEKS
     ELREEKATLK SDIEILNAQY QHRIKTMVPW VPHYSYHIPF VAITQGQSSF IPYSASVNPL
     TEQQASVQQH SSSSADASMK QDSKIKPLDL DLMMNSNHSG QGNDQKDDVR LKLELKIHAS
     SLAQQDVSGK EKKVSLTTTA SSSNSYSLSQ AVQDSSPGTV NDMLKP
 
 
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