ID PIF3_ARATH Reviewed; 524 AA. AC O80536; A5Y7A2; A5Y7A3; A5Y7A4; A5Y7A5; A5Y7A6; A5Y7A7; A5Y7A8; A5Y7A9; AC A5Y7B0; A5Y7B1; A5Y7B2; A5Y7B3; A5Y7B4; A5Y7B5; A5Y7B6; Q9SBC5; DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 07-APR-2021, entry version 168. DE RecName: Full=Transcription factor PIF3; DE AltName: Full=Basic helix-loop-helix protein 8; DE Short=AtbHLH8; DE Short=bHLH 8; DE AltName: Full=Phytochrome-associated protein 3; DE AltName: Full=Phytochrome-interacting factor 3; DE AltName: Full=Transcription factor EN 100; DE AltName: Full=bHLH transcription factor bHLH008; GN Name=PIF3; Synonyms=BHLH8, EN100, PAP3; OrderedLocusNames=At1g09530; GN ORFNames=F14J9.19; 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 [GENOMIC DNA / MRNA]. RC STRAIN=cv. Columbia; RX PubMed=9845368; DOI=10.1016/s0092-8674(00)81636-0; RA Ni M., Tepperman J.M., Quail P.H.; RT "PIF3, a phytochrome-interacting factor necessary for normal photoinduced RT signal transduction, is a novel basic helix-loop-helix protein."; RL Cell 95:657-667(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY UV LIGHT, 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Columbia; RA Lee J., Yi H., Shin B., Song P.-S., Choi G.; RT "Identification and characterization of three phytochrome-associated RT proteins."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; RL Nature 408:816-820(2000). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=11910074; DOI=10.1126/science.1071006; RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., RA Shinagawa A., Shinozaki K.; RT "Functional annotation of a full-length Arabidopsis cDNA collection."; RL Science 296:141-145(2002). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-272, AND VARIANTS ASP-124; ASN-141; RP HIS-176; LYS-186; LEU-209; ILE-220 AND ILE-236. RC STRAIN=cv. An-2, cv. Bla-6, cv. Br-0, cv. Bu-2, cv. Columbia, cv. Di-1, RC cv. Et-0, cv. Kl-1, cv. Li-5:3, cv. Ma-2, cv. Mt-0, cv. Pa-2, cv. Pi-0, RC cv. Su-0, and cv. Tsu-1; RX PubMed=17614917; DOI=10.1111/j.1365-294x.2007.03298.x; RA Brock M.T., Tiffin P., Weinig C.; RT "Sequence diversity and haplotype associations with phenotypic responses to RT crowding: GIGANTEA affects fruit set in Arabidopsis thaliana."; RL Mol. Ecol. 16:3050-3062(2007). RN [8] RP FUNCTION. RX PubMed=10466729; DOI=10.1038/23500; RA Ni M., Tepperman J.M., Quail P.H.; RT "Binding of phytochrome B to its nuclear signalling partner PIF3 is RT reversibly induced by light."; RL Nature 400:781-784(1999). RN [9] RP FUNCTION. RX PubMed=10797009; DOI=10.1126/science.288.5467.859; RA Martinez-Garcia J.F., Huq E., Quail P.H.; RT "Direct targeting of light signals to a promoter element-bound RT transcription factor."; RL Science 288:859-863(2000). RN [10] RP INTERACTION WITH APRR1. 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 [11] RP GENE FAMILY, AND INTERACTION WITH PIF4. 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 [12] 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 [13] RP INTERACTION WITH APRR1. 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 [14] RP INTERACTION WITH PIA2, AND PHOSPHORYLATION BY PHYA. RC STRAIN=cv. Columbia; RX PubMed=27143545; DOI=10.1093/jb/mvw031; RA Yoo J., Cho M.-H., Lee S.-W., Bhoo S.H.; RT "Phytochrome-interacting ankyrin repeat protein 2 modulates phytochrome A- RT mediated PIF3 phosphorylation in light signal transduction."; RL J. Biochem. 160:243-249(2016). RN [15] RP INTERACTION WITH TOPP4, AND PHOSPHORYLATION. RX PubMed=26704640; DOI=10.1104/pp.15.01729; RA Yue J., Qin Q., Meng S., Jing H., Gou X., Li J., Hou S.; RT "TOPP4 regulates the stability of PHYTOCHROME INTERACTING FACTOR5 during RT photomorphogenesis in Arabidopsis."; RL Plant Physiol. 170:1381-1397(2016). RN [16] RP INTERACTION WITH FYPP1 AND FYPP3. RX PubMed=31527236; DOI=10.1073/pnas.1907540116; RA Yu X., Dong J., Deng Z., Jiang Y., Wu C., Qin X., Terzaghi W., Chen H., RA Dai M., Deng X.W.; RT "Arabidopsis PP6 phosphatases dephosphorylate PIF proteins to repress RT photomorphogenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 116:20218-20225(2019). CC -!- FUNCTION: Transcription factor acting positively in the phytochrome CC signaling pathway. Activates transcription by binding to the G box (5'- CC CACGTG-3'). {ECO:0000269|PubMed:10466729, ECO:0000269|PubMed:10797009}. CC -!- SUBUNIT: Homodimer (Probable). Can form a heterodimer with REP1 and CC PIF4. Phytochrome B binds specifically to DNA-bound PIF3, but only upon CC red light induced conversion to the Pfr form (PfrB). Reconversion to Pr CC form causes rapid dissociation. Interacts with APRR1/TOC1. Binds to CC PIA2; this interaction may trigger the repression of PHYA-mediated CC phosphorylation (PubMed:27143545). Interacts with TOPP4 CC (PubMed:26704640, PubMed:11828023, PubMed:12826627, PubMed:12897250, CC PubMed:27143545) (Probable). Interacts with FYPP1 AND FYPP3 CC (PubMed:31527236). {ECO:0000269|PubMed:11828023, CC ECO:0000269|PubMed:12826627, ECO:0000269|PubMed:12897250, CC ECO:0000269|PubMed:26704640, ECO:0000269|PubMed:27143545, CC ECO:0000269|PubMed:31527236, ECO:0000305}. CC -!- INTERACTION: CC O80536; Q9FE22: HFR1; NbExp=6; IntAct=EBI-625701, EBI-626001; CC O80536; P14712: PHYA; NbExp=8; IntAct=EBI-625701, EBI-624446; CC O80536; P14713: PHYB; NbExp=22; IntAct=EBI-625701, EBI-300727; CC O80536; Q8GZM7: PIF1; NbExp=6; IntAct=EBI-625701, EBI-630400; CC O80536; O80536: PIF3; NbExp=3; IntAct=EBI-625701, EBI-625701; CC O80536; Q8W2F3-2: PIF4; NbExp=3; IntAct=EBI-625701, EBI-625732; CC O80536; Q9SLH3: RGA; NbExp=6; IntAct=EBI-625701, EBI-963624; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- INDUCTION: By UV treatment. {ECO:0000269|PubMed:12679534}. CC -!- PTM: Phosphorylated by PHYA; this phosphorylation is repressed by PIA2. CC {ECO:0000269|PubMed:27143545}. CC -!- PTM: Dephosphorylated by TOPP4 during photomorphogenesis, leading to CC subsequent degradation of PIF3 by the proteasomal pathway. CC {ECO:0000269|PubMed:26704640}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF100166; AAC95156.1; -; mRNA. DR EMBL; AF251693; AAL55715.1; -; mRNA. DR EMBL; AF088280; AAC99771.1; -; mRNA. DR EMBL; AC003970; AAC33213.1; -; Genomic_DNA. DR EMBL; CP002684; AEE28457.1; -; Genomic_DNA. DR EMBL; CP002684; AEE28458.1; -; Genomic_DNA. DR EMBL; CP002684; ANM60410.1; -; Genomic_DNA. DR EMBL; CP002684; ANM60411.1; -; Genomic_DNA. DR EMBL; CP002684; ANM60412.1; -; Genomic_DNA. DR EMBL; CP002684; ANM60413.1; -; Genomic_DNA. DR EMBL; AK117255; BAC41930.1; -; mRNA. DR EMBL; EF193482; ABP96435.1; -; Genomic_DNA. DR EMBL; EF193483; ABP96436.1; -; Genomic_DNA. DR EMBL; EF193484; ABP96437.1; -; Genomic_DNA. DR EMBL; EF193485; ABP96438.1; -; Genomic_DNA. DR EMBL; EF193486; ABP96439.1; -; Genomic_DNA. DR EMBL; EF193487; ABP96440.1; -; Genomic_DNA. DR EMBL; EF193488; ABP96441.1; -; Genomic_DNA. DR EMBL; EF193489; ABP96442.1; -; Genomic_DNA. DR EMBL; EF193490; ABP96443.1; -; Genomic_DNA. DR EMBL; EF193491; ABP96444.1; -; Genomic_DNA. DR EMBL; EF193492; ABP96445.1; -; Genomic_DNA. DR EMBL; EF193493; ABP96446.1; -; Genomic_DNA. DR EMBL; EF193494; ABP96447.1; -; Genomic_DNA. DR EMBL; EF193495; ABP96448.1; -; Genomic_DNA. DR EMBL; EF193496; ABP96449.1; -; Genomic_DNA. DR PIR; H86228; H86228. DR RefSeq; NP_001318964.1; NM_001331836.1. DR RefSeq; NP_001318965.1; NM_001331837.1. DR RefSeq; NP_001322700.1; NM_001331838.1. DR RefSeq; NP_001322701.1; NM_001331839.1. DR RefSeq; NP_172424.1; NM_100824.3. DR RefSeq; NP_849626.1; NM_179295.3. DR SMR; O80536; -. DR BioGRID; 22720; 34. DR DIP; DIP-33892N; -. DR IntAct; O80536; 18. DR STRING; 3702.AT1G09530.2; -. DR PaxDb; O80536; -. DR PRIDE; O80536; -. DR ProteomicsDB; 236160; -. DR EnsemblPlants; AT1G09530.1; AT1G09530.1; AT1G09530. DR EnsemblPlants; AT1G09530.2; AT1G09530.2; AT1G09530. DR EnsemblPlants; AT1G09530.3; AT1G09530.3; AT1G09530. DR EnsemblPlants; AT1G09530.4; AT1G09530.4; AT1G09530. DR EnsemblPlants; AT1G09530.5; AT1G09530.5; AT1G09530. DR EnsemblPlants; AT1G09530.6; AT1G09530.6; AT1G09530. DR GeneID; 837479; -. DR Gramene; AT1G09530.1; AT1G09530.1; AT1G09530. DR Gramene; AT1G09530.2; AT1G09530.2; AT1G09530. DR Gramene; AT1G09530.3; AT1G09530.3; AT1G09530. DR Gramene; AT1G09530.4; AT1G09530.4; AT1G09530. DR Gramene; AT1G09530.5; AT1G09530.5; AT1G09530. DR Gramene; AT1G09530.6; AT1G09530.6; AT1G09530. DR KEGG; ath:AT1G09530; -. DR Araport; AT1G09530; -. DR TAIR; locus:2012345; AT1G09530. DR eggNOG; ENOG502QV9I; Eukaryota. DR HOGENOM; CLU_014289_0_0_1; -. DR InParanoid; O80536; -. DR OMA; MVDEIPM; -. DR OrthoDB; 583799at2759; -. DR PhylomeDB; O80536; -. DR PRO; PR:O80536; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; O80536; baseline and differential. DR Genevisible; O80536; AT. DR GO; GO:0005634; C:nucleus; IDA:TAIR. DR GO; GO:0003677; F:DNA binding; IDA:TAIR. DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IPI:TAIR. DR GO; GO:0009704; P:de-etiolation; IMP:TAIR. DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; IMP:TAIR. DR GO; GO:0031539; P:positive regulation of anthocyanin metabolic process; IMP:TAIR. DR GO; GO:0010017; P:red or far-red light signaling pathway; 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:0009639; P:response to red or far red light; IMP:TAIR. DR Gene3D; 4.10.280.10; -; 1. DR InterPro; IPR011598; bHLH_dom. DR InterPro; IPR036638; HLH_DNA-bd_sf. DR InterPro; IPR044273; PIF3-like. DR PANTHER; PTHR46807; PTHR46807; 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; Phosphoprotein; Phytochrome signaling pathway; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1..524 FT /note="Transcription factor PIF3" FT /id="PRO_0000127428" FT DOMAIN 343..392 FT /note="bHLH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981" FT COMPBIAS 353..358 FT /note="Poly-Arg" FT COMPBIAS 422..428 FT /note="Poly-Ala" FT VARIANT 124 FT /note="E -> D (in strain: cv. An-2 and cv. Su-0)" FT /evidence="ECO:0000269|PubMed:17614917" FT VARIANT 141 FT /note="K -> N (in strain: cv. An-2 and cv. Su-0)" FT /evidence="ECO:0000269|PubMed:17614917" FT VARIANT 176 FT /note="Q -> H (in strain: cv. An-2 and cv. Su-0)" FT /evidence="ECO:0000269|PubMed:17614917" FT VARIANT 186 FT /note="Q -> K (in strain: cv. An-2 and cv. Su-0)" FT /evidence="ECO:0000269|PubMed:17614917" FT VARIANT 209 FT /note="F -> L (in strain: cv. An-2 and cv. Su-0)" FT /evidence="ECO:0000269|PubMed:17614917" FT VARIANT 220 FT /note="T -> I (in strain: cv. An-2 and cv. Su-0)" FT /evidence="ECO:0000269|PubMed:17614917" FT VARIANT 236 FT /note="V -> I (in strain: cv. An-2 and cv. Su-0)" FT /evidence="ECO:0000269|PubMed:17614917" FT CONFLICT 15 FT /note="E -> D (in Ref. 3; AAC99771)" FT /evidence="ECO:0000305" FT CONFLICT 344 FT /note="S -> L (in Ref. 3; AAC99771)" FT /evidence="ECO:0000305" SQ SEQUENCE 524 AA; 56990 MW; 1044AC01D598DE7C CRC64; MPLFELFRLT KAKLESAQDR NPSPPVDEVV ELVWENGQIS TQSQSSRSRN IPPPQANSSR AREIGNGSKT TMVDEIPMSV PSLMTGLSQD DDFVPWLNHH PSLDGYCSDF LRDVSSPVTV NEQESDMAVN QTAFPLFQRR KDGNESAPAA SSSQYNGFQS HSLYGSDRAR DLPSQQTNPD RFTQTQEPLI TSNKPSLVNF SHFLRPATFA KTTNNNLHDT KEKSPQSPPN VFQTRVLGAK DSEDKVLNES VASATPKDNQ KACLISEDSC RKDQESEKAV VCSSVGSGNS LDGPSESPSL SLKRKHSNIQ DIDCHSEDVE EESGDGRKEA GPSRTGLGSK RSRSAEVHNL SERRRRDRIN EKMRALQELI PNCNKVDKAS MLDEAIEYLK SLQLQVQIMS MASGYYLPPA VMFPPGMGHY PAAAAAMAMG MGMPYAMGLP DLSRGGSSVN HGPQFQVSGM QQQPVAMGIP RVSGGGIFAG SSTIGNGSTR DLSGSKDQTT TNNNSNLKPI KRKQGSSDQF CGSS //