PIF7_ARATH
ID PIF7_ARATH Reviewed; 366 AA.
AC Q570R7; Q7XJ93; Q9FLK6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Transcription factor PIF7;
DE AltName: Full=Basic helix-loop-helix protein 72;
DE Short=AtbHLH72;
DE Short=bHLH 72;
DE AltName: Full=Phytochrome-interacting factor 7;
DE AltName: Full=Transcription factor EN 109;
DE AltName: Full=bHLH transcription factor bHLH072;
GN Name=BHLH72; Synonyms=EN109, PIF7; OrderedLocusNames=At5g61270;
GN ORFNames=MFB13.4;
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 2), TISSUE SPECIFICITY, GENE FAMILY,
RP AND NOMENCLATURE.
RC STRAIN=cv. Columbia; TISSUE=Flower;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 1).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15208423; DOI=10.1104/pp.104.042176;
RA Gong W., Shen Y.-P., Ma L.-G., Pan Y., Du Y.-L., Wang D.-H., Yang J.-Y.,
RA Hu L.-D., Liu X.-F., Dong C.-X., Ma L., Chen Y.-H., Yang X.-Y., Gao Y.,
RA Zhu D., Tan X., Mu J.-Y., Zhang D.-B., Liu Y.-L., Dinesh-Kumar S.P., Li Y.,
RA Wang X.-P., Gu H.-Y., Qu L.-J., Bai S.-N., Lu Y.-T., Li J.-Y., Zhao J.-D.,
RA Zuo J., Huang H., Deng X.-W., Zhu Y.-X.;
RT "Genome-wide ORFeome cloning and analysis of Arabidopsis transcription
RT factor genes.";
RL Plant Physiol. 135:773-782(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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 [9]
RP FUNCTION, AND INTERACTION WITH PHYB.
RX PubMed=15486100; DOI=10.1105/tpc.104.025643;
RA Khanna R., Huq E., Kikis E.A., Al-Sady B., Lanzatella C., Quail P.H.;
RT "A novel molecular recognition motif necessary for targeting photoactivated
RT phytochrome signaling to specific basic helix-loop-helix transcription
RT factors.";
RL Plant Cell 16:3033-3044(2004).
RN [10]
RP FUNCTION, MUTAGENESIS OF GLU-8 AND GLY-14, LACK OF PHOSPHORYLATION,
RP INTERACTION WITH PHYB, AND DISRUPTION PHENOTYPE.
RX PubMed=18252845; DOI=10.1105/tpc.107.052142;
RA Leivar P., Monte E., Al-Sady B., Carle C., Storer A., Alonso J.M.,
RA Ecker J.R., Quail P.H.;
RT "The Arabidopsis phytochrome-interacting factor PIF7, together with PIF3
RT and PIF4, regulates responses to prolonged red light by Modulating phyb
RT levels.";
RL Plant Cell 20:337-352(2008).
CC -!- FUNCTION: Transcription factor acting negatively in the phytochrome B
CC signaling pathway under prolonged red light. Regulates PHYB abundance
CC at the post-transcriptional level, possibly via the ubiquitin-
CC proteasome pathway. May regulate the expression of a subset of genes by
CC binding to the G-box motif. {ECO:0000269|PubMed:15486100,
CC ECO:0000269|PubMed:18252845}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts specifically with the Pfr form
CC of phytochrome B. {ECO:0000269|PubMed:15486100,
CC ECO:0000269|PubMed:18252845, ECO:0000305}.
CC -!- INTERACTION:
CC Q570R7; Q7XJU0-2: BHLH157; NbExp=3; IntAct=EBI-1638784, EBI-15196985;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Migrates rapidly to speckles upon
CC light exposure.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q570R7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q570R7-2; Sequence=VSP_032847;
CC -!- TISSUE SPECIFICITY: Expressed in flowers.
CC {ECO:0000269|PubMed:12679534}.
CC -!- DEVELOPMENTAL STAGE: Barely detectable in dark-grown seedlings. Induced
CC after 2 hours of light exposure.
CC -!- INDUCTION: By red light. Stable upon light exposure.
CC -!- DOMAIN: The active phytochrome binding (APB) motif (3-17) is involved
CC in interaction with PHYB.
CC -!- DOMAIN: The Gln-rich domain in the C-terminal region functions to
CC modulate the transcriptional activity of BHLH72/PIF7.
CC -!- PTM: Not phosphorylated upon light exposure.
CC -!- DISRUPTION PHENOTYPE: Plants are hypersensitive to red light,
CC exhibiting shorter hypocotyls and larger cotyledons.
CC {ECO:0000269|PubMed:18252845}.
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DR EMBL; AF488604; AAP86213.1; -; mRNA.
DR EMBL; AB010073; BAB08482.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97445.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97446.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70162.1; -; Genomic_DNA.
DR EMBL; BX831447; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY568656; AAS79546.1; -; mRNA.
DR EMBL; AJ630484; CAG25857.1; -; mRNA.
DR EMBL; AK220640; BAD95106.1; -; mRNA.
DR RefSeq; NP_001032117.1; NM_001037040.3. [Q570R7-2]
DR RefSeq; NP_001331793.1; NM_001345463.1. [Q570R7-2]
DR RefSeq; NP_200935.2; NM_125520.5. [Q570R7-1]
DR AlphaFoldDB; Q570R7; -.
DR SMR; Q570R7; -.
DR BioGRID; 21492; 17.
DR IntAct; Q570R7; 11.
DR STRING; 3702.AT5G61270.1; -.
DR iPTMnet; Q570R7; -.
DR PaxDb; Q570R7; -.
DR PRIDE; Q570R7; -.
DR ProteomicsDB; 235085; -. [Q570R7-1]
DR EnsemblPlants; AT5G61270.1; AT5G61270.1; AT5G61270. [Q570R7-1]
DR EnsemblPlants; AT5G61270.2; AT5G61270.2; AT5G61270. [Q570R7-2]
DR EnsemblPlants; AT5G61270.3; AT5G61270.3; AT5G61270. [Q570R7-2]
DR GeneID; 836248; -.
DR Gramene; AT5G61270.1; AT5G61270.1; AT5G61270. [Q570R7-1]
DR Gramene; AT5G61270.2; AT5G61270.2; AT5G61270. [Q570R7-2]
DR Gramene; AT5G61270.3; AT5G61270.3; AT5G61270. [Q570R7-2]
DR KEGG; ath:AT5G61270; -.
DR Araport; AT5G61270; -.
DR TAIR; locus:2163163; AT5G61270.
DR eggNOG; ENOG502QV9I; Eukaryota.
DR InParanoid; Q570R7; -.
DR OMA; WPCNEDS; -.
DR PhylomeDB; Q570R7; -.
DR PRO; PR:Q570R7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q570R7; baseline and differential.
DR GO; GO:0016607; C:nuclear speck; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:TAIR.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0009704; P:de-etiolation; IMP:TAIR.
DR GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IDA: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 Alternative splicing; DNA-binding; Nucleus; Phytochrome signaling pathway;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..366
FT /note="Transcription factor PIF7"
FT /id="PRO_0000328936"
FT DOMAIN 166..215
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 3..17
FT /note="Involved in interaction with phyB"
FT REGION 59..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..88
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12679534,
FT ECO:0000303|PubMed:15208423, ECO:0000303|Ref.6"
FT /id="VSP_032847"
FT MUTAGEN 8
FT /note="E->A: Loss of binding to phyB; when associated with
FT Ala-14."
FT /evidence="ECO:0000269|PubMed:18252845"
FT MUTAGEN 14
FT /note="G->A: Loss of binding to phyB; when associated with
FT Ala-8."
FT /evidence="ECO:0000269|PubMed:18252845"
FT CONFLICT 75
FT /note="K -> E (in Ref. 4; BX831447)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="Missing (in Ref. 1; AAP86213)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="F -> S (in Ref. 4; BX831447)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="M -> V (in Ref. 6; BAD95106)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 40826 MW; FB76B80512E3A307 CRC64;
MSNYGVKELT WENGQLTVHG LGDEVEPTTS NNPIWTQSLN GCETLESVVH QAALQQPSKF
QLQSPNGPNH NYESKDGSCS RKRGYPQEMD RWFAVQEESH RVGHSVTASA SGTNMSWASF
ESGRSLKTAR TGDRDYFRSG SETQDTEGDE QETRGEAGRS NGRRGRAAAI HNESERRRRD
RINQRMRTLQ KLLPTASKAD KVSILDDVIE HLKQLQAQVQ FMSLRANLPQ QMMIPQLPPP
QSVLSIQHQQ QQQQQQQQQQ QQQQQFQMSL LATMARMGMG GGGNGYGGLV PPPPPPPMMV
PPMGNRDCTN GSSATLSDPY SAFFAQTMNM DLYNKMAAAI YRQQSDQTTK VNIGMPSSSS
NHEKRD
