PIL1_ARATH
ID PIL1_ARATH Reviewed; 416 AA.
AC Q8L5W8; O80727; Q84WY4;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Transcription factor PIL1;
DE AltName: Full=Basic helix-loop-helix protein 124;
DE Short=AtbHLH124;
DE Short=bHLH 124;
DE AltName: Full=Protein PHYTOCHROME INTERACTING FACTOR 3-LIKE 1;
DE AltName: Full=Transcription factor EN 110;
DE AltName: Full=bHLH transcription factor bHLH124;
GN Name=PIL1; Synonyms=BHLH124, EN110; OrderedLocusNames=At2g46970;
GN ORFNames=F14M4.20;
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], AND INTERACTION WITH APRR1/TOC1.
RX PubMed=11828023; DOI=10.1093/pcp/pcf005;
RA Makino S., Matsushika A., Kojima M., Yamashino T., Mizuno T.;
RT "The APRR1/TOC1 quintet implicated in circadian rhythms of Arabidopsis
RT thaliana: I. Characterization with APRR1-overexpressing plants.";
RL Plant Cell Physiol. 43:58-69(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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=12481096; DOI=10.1104/pp.010207;
RA Xiao Y.-L., Malik M., Whitelaw C.A., Town C.D.;
RT "Cloning and sequencing of cDNAs for hypothetical genes from chromosome 2
RT of Arabidopsis.";
RL Plant Physiol. 130:2118-2128(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
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 [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=14668869; DOI=10.1038/nature02174;
RA Salter M.G., Franklin K.A., Whitelam G.C.;
RT "Gating of the rapid shade-avoidance response by the circadian clock in
RT plants.";
RL Nature 426:680-683(2003).
RN [8]
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 [9]
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 [10]
RP INTERACTION WITH APRR1/TOC1, AND TISSUE SPECIFICITY.
RX PubMed=12826627; DOI=10.1093/pcp/pcg078;
RA Yamashino T., Matsushika A., Fujimori T., Sato S., Kato T., Tabata S.,
RA Mizuno T.;
RT "A link between circadian-controlled bHLH factors and the APRR1/TOC1
RT quintet in Arabidopsis thaliana.";
RL Plant Cell Physiol. 44:619-629(2003).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=16891401; DOI=10.1105/tpc.106.042200;
RA Khanna R., Shen Y., Toledo-Ortiz G., Kikis E.A., Johannesson H.,
RA Hwang Y.-S., Quail P.H.;
RT "Functional profiling reveals that only a small number of phytochrome-
RT regulated early-response genes in Arabidopsis are necessary for optimal
RT deetiolation.";
RL Plant Cell 18:2157-2171(2006).
RN [12]
RP FUNCTION, AND INDUCTION BY FAR-RED LIGHT.
RX PubMed=16565297; DOI=10.1104/pp.105.076331;
RA Roig-Villanova I., Bou J., Sorin C., Devlin P.F., Martinez-Garcia J.F.;
RT "Identification of primary target genes of phytochrome signaling. Early
RT transcriptional control during shade avoidance responses in Arabidopsis.";
RL Plant Physiol. 141:85-96(2006).
CC -!- FUNCTION: Transcription factor. Involved in responses to transient and
CC long-term shade. Required for the light-mediated inhibition of
CC hypocotyl elongation. Necessary for rapid light-induced expression of
CC the photomorphogenesis- and circadian-related gene APRR9. Seems to play
CC a role in multiple PHYB responses, such as flowering transition and
CC petiole elongation. {ECO:0000269|PubMed:14668869,
CC ECO:0000269|PubMed:16565297, ECO:0000269|PubMed:16891401}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with APRR1/TOC1.
CC {ECO:0000269|PubMed:11828023, ECO:0000269|PubMed:12826627,
CC ECO:0000305}.
CC -!- INTERACTION:
CC Q8L5W8; Q9LKL2: APRR1; NbExp=3; IntAct=EBI-630752, EBI-618423;
CC Q8L5W8; Q5XVH0: BHLH109; NbExp=3; IntAct=EBI-630752, EBI-15193531;
CC Q8L5W8; Q9LXU1: PIM1; NbExp=3; IntAct=EBI-630752, EBI-15193025;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:16891401}.
CC -!- TISSUE SPECIFICITY: Etiolated seedlings. {ECO:0000269|PubMed:12826627}.
CC -!- INDUCTION: Expressed with a circadian rhythm showing peaks during the
CC light period. Up-regulated by simulated shade in light-grown plants, in
CC a phytochrome-dependent manner; low red/far-red ratio (R/FR) light, but
CC repressed by a high R/FR light. Rapidly down-regulated after seedling
CC deetiolation. {ECO:0000269|PubMed:14668869,
CC ECO:0000269|PubMed:16565297, ECO:0000269|PubMed:16891401}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC34226.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB090873; BAC10689.1; -; Transcribed_RNA.
DR EMBL; AC004411; AAC34226.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10779.1; -; Genomic_DNA.
DR EMBL; AY219127; AAO37214.1; -; mRNA.
DR EMBL; AY954840; AAX55166.1; -; mRNA.
DR PIR; T02190; T02190.
DR RefSeq; NP_182220.2; NM_130265.4.
DR AlphaFoldDB; Q8L5W8; -.
DR SMR; Q8L5W8; -.
DR BioGRID; 4646; 19.
DR IntAct; Q8L5W8; 17.
DR STRING; 3702.AT2G46970.1; -.
DR PaxDb; Q8L5W8; -.
DR PRIDE; Q8L5W8; -.
DR EnsemblPlants; AT2G46970.1; AT2G46970.1; AT2G46970.
DR GeneID; 819311; -.
DR Gramene; AT2G46970.1; AT2G46970.1; AT2G46970.
DR KEGG; ath:AT2G46970; -.
DR Araport; AT2G46970; -.
DR TAIR; locus:2041369; AT2G46970.
DR eggNOG; ENOG502QV9I; Eukaryota.
DR HOGENOM; CLU_053768_0_0_1; -.
DR InParanoid; Q8L5W8; -.
DR OrthoDB; 973729at2759; -.
DR PhylomeDB; Q8L5W8; -.
DR PRO; PR:Q8L5W8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8L5W8; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:1990110; P:callus formation; IMP:TAIR.
DR GO; GO:0010017; P:red or far-red light signaling pathway; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009641; P:shade avoidance; IEP:TAIR.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR031066; bHLH_ALC-like_plant.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR PANTHER; PTHR45855; PTHR45855; 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 Coiled coil; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..416
FT /note="Transcription factor PIL1"
FT /id="PRO_0000358853"
FT DOMAIN 229..278
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 95..124
FT /evidence="ECO:0000255"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 302
FT /note="H -> K (in Ref. 4; AAO37214)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 46580 MW; 69B86687CC1901CF CRC64;
MEAKPLASSS SEPNMISPSS NIKPKLKDED YMELVCENGQ ILAKIRRPKN NGSFQKQRRQ
SLLDLYETEY SEGFKKNIKI LGDTQVVPVS QSKPQQDKET NEQMNNNKKK LKSSKIEFER
NVSKSNKCVE SSTLIDVSAK GPKNVEVTTA PPDEQSAAVG RSTELYFASS SKFSRGTSRD
LSCCSLKRKY GDIEEEESTY LSNNSDDESD DAKTQVHART RKPVTKRKRS TEVHKLYERK
RRDEFNKKMR ALQDLLPNCY KDDKASLLDE AIKYMRTLQL QVQMMSMGNG LIRPPTMLPM
GHYSPMGLGM HMGAAATPTS IPQFLPMNVQ ATGFPGMNNA PPQMLSFLNH PSGLIPNTPI
FSPLENCSQP FVVPSCVSQT QATSFTQFPK SASASNLEDA MQYRGSNGFS YYRSPN
