BIM1_ARATH
ID BIM1_ARATH Reviewed; 529 AA.
AC Q9LEZ3; A1L4Z3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=Transcription factor BIM1;
DE AltName: Full=BES1-interacting Myc-like protein 1;
DE AltName: Full=Basic helix-loop-helix protein 46;
DE Short=AtbHLH46;
DE Short=bHLH 46;
DE AltName: Full=Transcription factor EN 126;
DE AltName: Full=bHLH transcription factor bHLH046;
GN Name=BIM1; Synonyms=BHLH46, EN126; OrderedLocusNames=At5g08130;
GN ORFNames=T22D6.70;
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, INDUCTION, GENE
RP 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 [MRNA] (ISOFORM 1), FUNCTION, DNA-BINDING, AND
RP INTERACTION WITH BZR2/BES1.
RX PubMed=15680330; DOI=10.1016/j.cell.2004.11.044;
RA Yin Y., Vafeados D., Tao Y., Yoshida S., Asami T., Chory J.;
RT "A new class of transcription factors mediates brassinosteroid-regulated
RT gene expression in Arabidopsis.";
RL Cell 120:249-259(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
RP INTERACTION WITH LHW.
RX PubMed=17626058; DOI=10.1242/dev.006296;
RA Ohashi-Ito K., Bergmann D.C.;
RT "Regulation of the Arabidopsis root vascular initial population by LONESOME
RT HIGHWAY.";
RL Development 134:2959-2968(2007).
CC -!- FUNCTION: Positive brassinosteroid-signaling protein. Transcription
CC factor that bind specifically to the DNA sequence 5'-CANNTG-3'(E box).
CC Can bind individually to the promoter as a homodimer or synergistically
CC as a heterodimer with BZR2/BES1. Does not itself activate transcription
CC but enhances BZR2/BES1-mediated target gene activation.
CC {ECO:0000269|PubMed:15680330}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with BZR2/BES1 through both C-
CC terminal and bHLH domains. Interacts also with LHW.
CC {ECO:0000269|PubMed:15680330, ECO:0000269|PubMed:17626058,
CC ECO:0000305}.
CC -!- INTERACTION:
CC Q9LEZ3; P32068: ASA1; NbExp=3; IntAct=EBI-617095, EBI-25514634;
CC Q9LEZ3; A0A178WJS6: At1g75000; NbExp=3; IntAct=EBI-617095, EBI-25514615;
CC Q9LEZ3; Q9LS86: At3g23060; NbExp=3; IntAct=EBI-617095, EBI-4445671;
CC Q9LEZ3; A0A178U7R5: At5g67220; NbExp=4; IntAct=EBI-617095, EBI-25511160;
CC Q9LEZ3; O04292: ATHB-9; NbExp=5; IntAct=EBI-617095, EBI-1536772;
CC Q9LEZ3; Q9LEZ3: BIM1; NbExp=3; IntAct=EBI-617095, EBI-617095;
CC Q9LEZ3; Q9CAA4: BIM2; NbExp=14; IntAct=EBI-617095, EBI-4476396;
CC Q9LEZ3; Q9FMB6: BIM3; NbExp=6; IntAct=EBI-617095, EBI-617113;
CC Q9LEZ3; Q17TI5: BRX; NbExp=5; IntAct=EBI-617095, EBI-4426649;
CC Q9LEZ3; Q9LN63: BZR2; NbExp=2; IntAct=EBI-617095, EBI-617078;
CC Q9LEZ3; Q8L925: CRC; NbExp=3; IntAct=EBI-617095, EBI-15197527;
CC Q9LEZ3; Q8GW17: ERF116; NbExp=3; IntAct=EBI-617095, EBI-4433324;
CC Q9LEZ3; Q9SAD4: ESR1; NbExp=4; IntAct=EBI-617095, EBI-1536756;
CC Q9LEZ3; Q9FYK5: ESR2; NbExp=2; IntAct=EBI-617095, EBI-1536925;
CC Q9LEZ3; Q93ZB9: FAR3; NbExp=3; IntAct=EBI-617095, EBI-25514661;
CC Q9LEZ3; F4IMQ0: FLX; NbExp=3; IntAct=EBI-617095, EBI-4447281;
CC Q9LEZ3; Q9FK45: MRG7.22; NbExp=3; IntAct=EBI-617095, EBI-4470510;
CC Q9LEZ3; Q9LMT2: PAPS1; NbExp=3; IntAct=EBI-617095, EBI-1775760;
CC Q9LEZ3; Q38845: PP2AA1; NbExp=3; IntAct=EBI-617095, EBI-1645478;
CC Q9LEZ3; Q9C8D1: PUB20; NbExp=3; IntAct=EBI-617095, EBI-25516153;
CC Q9LEZ3; Q9C5Z3: TIF3E1; NbExp=3; IntAct=EBI-617095, EBI-1635572;
CC Q9LEZ3; Q9XFB1: YAB3; NbExp=3; IntAct=EBI-617095, EBI-1115657;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LEZ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LEZ3-2; Sequence=VSP_035543;
CC -!- TISSUE SPECIFICITY: Expressed constitutively in roots.
CC {ECO:0000269|PubMed:12679534}.
CC -!- INDUCTION: Repressed by cold treatment. {ECO:0000269|PubMed:12679534}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB93714.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF488581; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL357612; CAB93714.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91250.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91251.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91253.1; -; Genomic_DNA.
DR EMBL; BT029780; ABM06050.1; -; mRNA.
DR PIR; T50498; T50498.
DR RefSeq; NP_001119190.1; NM_001125718.1. [Q9LEZ3-1]
DR RefSeq; NP_001190257.1; NM_001203328.2. [Q9LEZ3-1]
DR RefSeq; NP_001318507.1; NM_001342983.1. [Q9LEZ3-2]
DR AlphaFoldDB; Q9LEZ3; -.
DR SMR; Q9LEZ3; -.
DR BioGRID; 15986; 39.
DR IntAct; Q9LEZ3; 34.
DR STRING; 3702.AT5G08130.5; -.
DR iPTMnet; Q9LEZ3; -.
DR PaxDb; Q9LEZ3; -.
DR PRIDE; Q9LEZ3; -.
DR ProteomicsDB; 240426; -. [Q9LEZ3-1]
DR EnsemblPlants; AT5G08130.1; AT5G08130.1; AT5G08130. [Q9LEZ3-2]
DR EnsemblPlants; AT5G08130.2; AT5G08130.2; AT5G08130. [Q9LEZ3-1]
DR EnsemblPlants; AT5G08130.4; AT5G08130.4; AT5G08130. [Q9LEZ3-1]
DR GeneID; 830708; -.
DR Gramene; AT5G08130.1; AT5G08130.1; AT5G08130. [Q9LEZ3-2]
DR Gramene; AT5G08130.2; AT5G08130.2; AT5G08130. [Q9LEZ3-1]
DR Gramene; AT5G08130.4; AT5G08130.4; AT5G08130. [Q9LEZ3-1]
DR KEGG; ath:AT5G08130; -.
DR Araport; AT5G08130; -.
DR eggNOG; ENOG502QUDM; Eukaryota.
DR InParanoid; Q9LEZ3; -.
DR OMA; TKSHYIM; -.
DR PhylomeDB; Q9LEZ3; -.
DR PRO; PR:Q9LEZ3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LEZ3; baseline and differential.
DR Genevisible; Q9LEZ3; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR044295; BIM1/2/3.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR PANTHER; PTHR46412; PTHR46412; 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; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..529
FT /note="Transcription factor BIM1"
FT /id="PRO_0000127153"
FT DOMAIN 276..326
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..89
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..521
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..120
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_035543"
FT CONFLICT 282
FT /note="S -> P (in Ref. 1; AF488581)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="S -> P (in Ref. 1; AF488581)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="I -> T (in Ref. 1; AF488581)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 529 AA; 58710 MW; E6E2EA306895F92B CRC64;
MELPQPRPFK TQGRKPTHDF LSLCSHSTVH PDPKPTPPPS SQGSHLKTHD FLQPLECVGA
KEDVSRINST TTASEKPPPP APPPPLQHVL PGGIGTYTIS PIPYFHHHHQ RIPKPELSPP
MMFNANERNV LDENSNSNCS SYAAASSGFT LWDESASGKK GQTRKENSVG ERVNMRADVA
ATVGQWPVAE RRSQSLTNNH MSGFSSLSSS QGSVLKSQSF MDMIRSAKGS SQEDDLDDEE
DFIMKKESSS TSQSHRVDLR VKADVRGSPN DQKLNTPRSK HSATEQRRRS KINDRFQMLR
QLIPNSDQKR DKASFLLEVI EYIQFLQEKA DKYVTSYQGW NHEPAKLLNW QSNNNQQLVP
EGVAFAPKLE EEKNNIPVSV LATAQGVVID HPTTATTSPF PLSIQSNSFF SPVIAGNPVP
QFHARVASSE AVEPSPSSRS QKEEEDEEVL EGNIRISSVY SQGLVKTLRE ALENSGVDLT
KASISVEIEL AKQSSSSSFK DHEVREPVSR TRNDNVKQTR KPKRLKTGQ
