BH047_ARATH
ID BH047_ARATH Reviewed; 240 AA.
AC Q9SN74;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Transcription factor bHLH47;
DE AltName: Full=Basic helix-loop-helix protein 47;
DE Short=AtbHLH47;
DE Short=bHLH 47;
DE AltName: Full=Protein POPEYE;
DE AltName: Full=Transcription factor EN 139;
DE AltName: Full=bHLH transcription factor bHLH047;
GN Name=BHLH47; Synonyms=EN139, PYE; OrderedLocusNames=At3g47640;
GN ORFNames=F1P2.190;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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].
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 36-240, 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 [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 SUBCELLULAR LOCATION, AND INTERACTION WITH BHLH115; BHLH104 AND ILR3.
RC STRAIN=cv. Columbia;
RX PubMed=25452667; DOI=10.1104/pp.114.250837;
RA Selote D., Samira R., Matthiadis A., Gillikin J.W., Long T.A.;
RT "Iron-binding E3 ligase mediates iron response in plants by targeting basic
RT helix-loop-helix transcription factors.";
RL Plant Physiol. 167:273-286(2015).
CC -!- SUBUNIT: Homodimer (Probable). Forms heterodimer with PYEL proteins
CC bHLH115, bHLH104 and ILR3 (PubMed:25452667).
CC {ECO:0000269|PubMed:25452667, ECO:0000305}.
CC -!- INTERACTION:
CC Q9SN74; Q8VZI9: At3g11100; NbExp=3; IntAct=EBI-4437532, EBI-1998580;
CC Q9SN74; Q93Y00: BHLH7; NbExp=3; IntAct=EBI-4437532, EBI-4442198;
CC Q9SN74; Q93Z00: TCP14; NbExp=3; IntAct=EBI-4437532, EBI-4424563;
CC Q9SN74; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-4437532, EBI-4426144;
CC Q9SN74; O64647: TCP9; NbExp=3; IntAct=EBI-4437532, EBI-9838721;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:25452667}.
CC -!- TISSUE SPECIFICITY: Expressed constitutively in roots, leaves, stems,
CC and flowers. {ECO:0000269|PubMed:12679534}.
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DR EMBL; AY080786; AAL87269.1; -; mRNA.
DR EMBL; AY114018; AAM45066.1; -; mRNA.
DR EMBL; AL132955; CAB61990.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78311.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78312.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78313.1; -; Genomic_DNA.
DR EMBL; AF488582; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T45724; T45724.
DR RefSeq; NP_001190029.1; NM_001203100.1.
DR RefSeq; NP_001190030.1; NM_001203101.1.
DR RefSeq; NP_190348.1; NM_114632.4.
DR AlphaFoldDB; Q9SN74; -.
DR SMR; Q9SN74; -.
DR BioGRID; 9238; 27.
DR IntAct; Q9SN74; 23.
DR STRING; 3702.AT3G47640.2; -.
DR PaxDb; Q9SN74; -.
DR PRIDE; Q9SN74; -.
DR EnsemblPlants; AT3G47640.1; AT3G47640.1; AT3G47640.
DR EnsemblPlants; AT3G47640.2; AT3G47640.2; AT3G47640.
DR EnsemblPlants; AT3G47640.3; AT3G47640.3; AT3G47640.
DR GeneID; 823918; -.
DR Gramene; AT3G47640.1; AT3G47640.1; AT3G47640.
DR Gramene; AT3G47640.2; AT3G47640.2; AT3G47640.
DR Gramene; AT3G47640.3; AT3G47640.3; AT3G47640.
DR KEGG; ath:AT3G47640; -.
DR Araport; AT3G47640; -.
DR TAIR; locus:2079102; AT3G47640.
DR eggNOG; ENOG502RYQ6; Eukaryota.
DR HOGENOM; CLU_053417_2_0_1; -.
DR InParanoid; Q9SN74; -.
DR OMA; CDKKAPK; -.
DR OrthoDB; 1207684at2759; -.
DR PhylomeDB; Q9SN74; -.
DR PRO; PR:Q9SN74; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SN74; baseline and differential.
DR Genevisible; Q9SN74; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0010106; P:cellular response to iron ion starvation; IMP:TAIR.
DR GO; GO:0055072; P:iron ion homeostasis; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR Gene3D; 4.10.280.10; -; 1.
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 Coiled coil; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..240
FT /note="Transcription factor bHLH47"
FT /id="PRO_0000358745"
FT DOMAIN 27..77
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 98..131
FT /evidence="ECO:0000255"
SQ SEQUENCE 240 AA; 26944 MW; 2D2D8BCB54C27822 CRC64;
MVSKTPSTSS DEANATADER CRKGKVPKRI NKAVRERLKR EHLNELFIEL ADTLELNQQN
SGKASILCEA TRFLKDVFGQ IESLRKEHAS LLSESSYVTT EKNELKEETS VLETEISKLQ
NEIEARANQS KPDLNTSPAP EYHHHHYQQQ HPERVSQFPG LPIFQGPGFQ QSATTLHPPA
TVLVLPIQPD PQTQDISEMT QAQQPLMFNS SNVSKPCPRY ASAADSWSSR LLGERLKASE
