ILR3_ARATH
ID ILR3_ARATH Reviewed; 234 AA.
AC Q9FH37; Q8LD53;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Transcription factor ILR3;
DE AltName: Full=Basic helix-loop-helix protein 105;
DE Short=AtbHLH105;
DE Short=bHLH 105;
DE AltName: Full=Protein IAA-LEUCINE RESISTANT 3;
DE AltName: Full=Transcription factor EN 133;
DE AltName: Full=bHLH transcription factor bHLH105;
GN Name=ILR3; Synonyms=BHLH105, EN133; OrderedLocusNames=At5g54680;
GN ORFNames=K5F14.2;
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], GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia; TISSUE=Seed;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) 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 FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF 171-MET--ALA-234, AND TISSUE
RP SPECIFICITY.
RX PubMed=17028341; DOI=10.1534/genetics.106.061044;
RA Rampey R.A., Woodward A.W., Hobbs B.N., Tierney M.P., Lahner B., Salt D.E.,
RA Bartel B.;
RT "An Arabidopsis basic helix-loop-helix leucine zipper protein modulates
RT metal homeostasis and auxin conjugate responsiveness.";
RL Genetics 174:1841-1857(2006).
RN [9]
RP INTERACTION WITH BTS.
RC STRAIN=cv. Columbia;
RX PubMed=20675571; DOI=10.1105/tpc.110.074096;
RA Long T.A., Tsukagoshi H., Busch W., Lahner B., Salt D.E., Benfey P.N.;
RT "The bHLH transcription factor POPEYE regulates response to iron deficiency
RT in Arabidopsis roots.";
RL Plant Cell 22:2219-2236(2010).
RN [10]
RP INTERACTION WITH BTS AND BHLH47/PYE, AND SUBCELLULAR LOCATION.
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 -!- FUNCTION: Transcription factor. Plays a role in resistance to amide-
CC linked indole-3-acetic acid (IAA) conjugates such as IAA-Leu and IAA-
CC Phe. May regulate gene expression in response to metal homeostasis
CC changes. {ECO:0000269|PubMed:17028341}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with BTS and BHLH47/PYE
CC (PubMed:20675571, PubMed:25452667). {ECO:0000269|PubMed:20675571,
CC ECO:0000269|PubMed:25452667, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:25452667}.
CC -!- TISSUE SPECIFICITY: Widely expressed throughout development, mostly in
CC vasculatures. {ECO:0000269|PubMed:17028341}.
CC -!- DISRUPTION PHENOTYPE: Plants are more sensitive to IAA conjugates.
CC {ECO:0000269|PubMed:17028341}.
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DR EMBL; AF488629; AAM10964.1; -; mRNA.
DR EMBL; AB022214; BAB09934.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96526.1; -; Genomic_DNA.
DR EMBL; AY054585; AAK96776.1; -; mRNA.
DR EMBL; BT002189; AAN72200.1; -; mRNA.
DR EMBL; AY086197; AAM64276.1; -; mRNA.
DR RefSeq; NP_200279.1; NM_124849.4.
DR AlphaFoldDB; Q9FH37; -.
DR SMR; Q9FH37; -.
DR BioGRID; 20801; 4.
DR IntAct; Q9FH37; 1.
DR STRING; 3702.AT5G54680.1; -.
DR PaxDb; Q9FH37; -.
DR PRIDE; Q9FH37; -.
DR EnsemblPlants; AT5G54680.1; AT5G54680.1; AT5G54680.
DR GeneID; 835557; -.
DR Gramene; AT5G54680.1; AT5G54680.1; AT5G54680.
DR KEGG; ath:AT5G54680; -.
DR Araport; AT5G54680; -.
DR TAIR; locus:2157538; AT5G54680.
DR eggNOG; ENOG502QSHF; Eukaryota.
DR HOGENOM; CLU_078927_0_0_1; -.
DR InParanoid; Q9FH37; -.
DR OMA; SIGESDY; -.
DR OrthoDB; 1293523at2759; -.
DR PhylomeDB; Q9FH37; -.
DR PRO; PR:Q9FH37; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FH37; baseline and differential.
DR Genevisible; Q9FH37; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0019760; P:glucosinolate metabolic process; IMP:TAIR.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:InterPro.
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 InterPro; IPR044818; ILR3-like.
DR PANTHER; PTHR46133; PTHR46133; 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..234
FT /note="Transcription factor ILR3"
FT /id="PRO_0000358847"
FT DOMAIN 71..122
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 34..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 171..234
FT /note="MNAPQPSFFPAPPMMPTAFASAQGQAPGNKMVPIISYPGVAMWQFMPPASVD
FT TSQDHVLRPPVA->FKYVVFG: In ilr3-1; confers an increased
FT resistance to manganese and IAA conjugates."
FT /evidence="ECO:0000269|PubMed:17028341"
FT CONFLICT 171
FT /note="M -> I (in Ref. 5; AAM64276)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 25488 MW; 987EA114244F21D1 CRC64;
MVSPENANWI CDLIDADYGS FTIQGPGFSW PVQQPIGVSS NSSAGVDGSA GNSEASKEPG
SKKRGRCESS SATSSKACRE KQRRDRLNDK FMELGAILEP GNPPKTDKAA ILVDAVRMVT
QLRGEAQKLK DSNSSLQDKI KELKTEKNEL RDEKQRLKTE KEKLEQQLKA MNAPQPSFFP
APPMMPTAFA SAQGQAPGNK MVPIISYPGV AMWQFMPPAS VDTSQDHVLR PPVA
