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 24-JAN-2024, entry version 179. DE RecName: Full=Transcription factor PIF3 {ECO:0000305}; DE AltName: Full=Basic helix-loop-helix protein 8 {ECO:0000303|PubMed:12679534}; DE Short=AtbHLH8 {ECO:0000303|PubMed:12679534}; DE Short=bHLH 8 {ECO:0000303|PubMed:12679534}; DE AltName: Full=Phytochrome-associated protein 3 {ECO:0000305}; DE AltName: Full=Phytochrome-interacting factor 3 {ECO:0000303|PubMed:9845368}; DE AltName: Full=Transcription factor EN 100 {ECO:0000305}; DE AltName: Full=bHLH transcription factor bHLH008 {ECO:0000305}; GN Name=PIF3 {ECO:0000303|PubMed:9845368}; GN Synonyms=BHLH8 {ECO:0000303|PubMed:12679534}, EN100 {ECO:0000305}, GN PAP3 {ECO:0000305}; GN OrderedLocusNames=At1g09530 {ECO:0000312|Araport:AT1G09530}; GN ORFNames=F14J9.19 {ECO:0000312|EMBL:AAC33213.1}; 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]. 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. RC Di-1, cv. Et-0, cv. Kl-1, cv. Li-5:3, cv. Ma-2, cv. Mt-0, cv. Pa-2, RC cv. Pi-0, 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 FUNCTION. RX PubMed=14508006; DOI=10.1105/tpc.014498; RA Kim J., Yi H., Choi G., Shin B., Song P.S., Choi G.; RT "Functional characterization of phytochrome interacting factor 3 in RT phytochrome-mediated light signal transduction."; RL Plant Cell 15:2399-2407(2003). RN [13] 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 [14] 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 [15] RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION BY COLD; HEAT; SALT; RP ABSCISIC ACID; ETHYLENE AND AUXIN, GENE FAMILY, NOMENCLATURE, AND REVIEW. RX PubMed=23708772; DOI=10.1007/s10059-013-0135-5; RA Jeong J., Choi G.; RT "Phytochrome-interacting factors have both shared and distinct biological RT roles."; RL Mol. Cells 35:371-380(2013). RN [16] RP FUNCTION, INTERACTION WITH HDA15, AND SUBCELLULAR LOCATION. RX PubMed=23548744; DOI=10.1105/tpc.113.109710; RA Liu X., Chen C.Y., Wang K.C., Luo M., Tai R., Yuan L., Zhao M., Yang S., RA Tian G., Cui Y., Hsieh H.L., Wu K.; RT "PHYTOCHROME INTERACTING FACTOR3 associates with the histone deacetylase RT HDA15 in repression of chlorophyll biosynthesis and photosynthesis in RT etiolated Arabidopsis seedlings."; RL Plant Cell 25:1258-1273(2013). RN [17] RP INTERACTION WITH PTAC12/HMR/PAP5, SUBUNIT, AND REPRESSION BY RP PTAC12/HMR/PAP5. RC STRAIN=cv. Columbia; RX PubMed=25944101; DOI=10.1105/tpc.114.136093; RA Qiu Y., Li M., Pasoreck E.K., Long L., Shi Y., Galvao R.M., Chou C.L., RA Wang H., Sun A.Y., Zhang Y.C., Jiang A., Chen M.; RT "HEMERA couples the proteolysis and transcriptional activity of PHYTOCHROME RT INTERACTING FACTORs in Arabidopsis photomorphogenesis."; RL Plant Cell 27:1409-1427(2015). RN [18] 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 [19] 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 [20] RP FUNCTION. RC STRAIN=cv. Columbia; RX PubMed=29167353; DOI=10.1104/pp.17.01109; RA Ma Q., Wang X., Sun J., Mao T.; RT "Coordinated regulation of hypocotyl cell elongation by light and ethylene RT through a microtubule destabilizing protein."; RL Plant Physiol. 176:678-690(2018). RN [21] 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). RN [22] RP FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=cv. Columbia, cv. En-2, cv. Landsberg erecta, and cv. RC Wassilewskija; RX PubMed=31638649; DOI=10.1093/jxb/erz453; RA Wang X., Ma Q., Wang R., Wang P., Liu Y., Mao T.; RT "Submergence stress-induced hypocotyl elongation through ethylene RT signaling-mediated regulation of cortical microtubules in Arabidopsis."; RL J. Exp. Bot. 71:1067-1077(2020). RN [23] RP ACTIVITY REGULATION, AND INTERACTION WITH PHYA. RC STRAIN=cv. Columbia; RX PubMed=31732705; DOI=10.1105/tpc.19.00515; RA Oh J., Park E., Song K., Bae G., Choi G.; RT "PHYTOCHROME INTERACTING FACTOR8 inhibits phytochrome a-mediated far-red RT light responses in Arabidopsis."; RL Plant Cell 32:186-205(2020). CC -!- FUNCTION: Transcription factor acting in the phytochrome signaling CC pathway (PubMed:10466729, PubMed:14508006). Activates transcription by CC binding to the G box (5'-CACGTG-3'), particularly in the dark but CC barely in far-red light (PubMed:10797009, PubMed:31732705). Acts as a CC negative regulator of phytochrome B signaling (PubMed:14508006). CC Represses chlorophyll biosynthesis and photosynthesis in the dark CC (PubMed:23548744). Recruits the histone deacetylase HDA15 to the CC promoters of chlorophyll biosynthetic and photosynthetic genes CC (PubMed:23548744). HDA15 represses their transcription by histone CC deacetylation (PubMed:23548744). Promotes the expression of MDP60 to CC modulate hypocotyl cell elongation in response to light and ethylene CC signaling (PubMed:29167353). Required for submergence-induced and CC ethylene-dependent underwater hypocotyl elongation (PubMed:31638649). CC {ECO:0000269|PubMed:10466729, ECO:0000269|PubMed:10797009, CC ECO:0000269|PubMed:14508006, ECO:0000269|PubMed:23548744, CC ECO:0000269|PubMed:29167353, ECO:0000269|PubMed:31638649, CC ECO:0000269|PubMed:31732705}. CC -!- ACTIVITY REGULATION: Sequestered by PhyA from its target genes CC promoters in far-red light. {ECO:0000269|PubMed:31732705}. CC -!- SUBUNIT: Homodimer (PubMed:25944101). Can form a heterodimer with REP1 CC and PIF4. Phytochrome B binds specifically to DNA-bound PIF3, but only CC upon red light induced conversion to the Pfr form (PfrB). Reconversion CC to Pr form causes rapid dissociation. Interacts with APRR1/TOC1. Binds CC to 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). Interacts with HDA15 in the dark (PubMed:23548744). CC Associates to PTAC12/HMR/PAP5 which acts as a transcriptional CC coactivator (PubMed:25944101). Binds to PhyA (PubMed:31732705). CC {ECO:0000269|PubMed:11828023, ECO:0000269|PubMed:12826627, CC ECO:0000269|PubMed:12897250, ECO:0000269|PubMed:23548744, CC ECO:0000269|PubMed:25944101, ECO:0000269|PubMed:26704640, CC ECO:0000269|PubMed:27143545, ECO:0000269|PubMed:31527236, CC ECO:0000269|PubMed:31732705, 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 {ECO:0000269|PubMed:23548744}. CC -!- TISSUE SPECIFICITY: Expressed in stems, leaves, seedlings, fruits and CC flowers, and, to a lower extent, in roots. CC {ECO:0000269|PubMed:23708772}. CC -!- DEVELOPMENTAL STAGE: Accumulates progressively in maturating seeds to CC reach a peak in dry seeds (PubMed:23708772). Expressed upon seed CC imbibition (PubMed:23708772). {ECO:0000269|PubMed:23708772}. CC -!- INDUCTION: By UV treatment (PubMed:12679534). Repressed by red (R) and CC far red (FR) light treatments in a phyB- and phyA-dependent manner, and CC via a PTAC12/HMR/PAP5 regulated process (PubMed:25944101). Up-regulated CC by abscisic acid (ABA), ethylene (ACC), auxin (IAA), salt (NaCl), cold CC and heat (PubMed:23708772). Follows a tenous circadian rhythm with CC slightly higher levels at the end of the light phase (PubMed:23708772). CC {ECO:0000269|PubMed:12679534, ECO:0000269|PubMed:23708772, CC ECO:0000269|PubMed:25944101}. 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 -!- DISRUPTION PHENOTYPE: Inhibited submergence-induced and ethylene- CC dependent underwater hypocotyl elongation. CC {ECO:0000269|PubMed:31638649}. 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 AlphaFoldDB; O80536; -. DR SMR; O80536; -. DR BioGRID; 22720; 34. DR DIP; DIP-33892N; -. DR IntAct; O80536; 18. DR STRING; 3702.O80536; -. DR PaxDb; 3702-AT1G09530-2; -. 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; AT1G09530; PIF3. DR eggNOG; ENOG502QV9I; Eukaryota. DR HOGENOM; CLU_014289_0_0_1; -. DR InParanoid; O80536; -. DR OMA; MVDEIPM; -. DR OrthoDB; 413453at2759; -. DR PhylomeDB; O80536; -. DR PRO; PR:O80536; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; O80536; baseline and differential. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:TAIR. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0000976; F:transcription cis-regulatory region 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 DNA-templated transcription; TAS:TAIR. DR GO; GO:0042548; P:regulation of photosynthesis, light reaction; IDA:UniProtKB. DR GO; GO:1905421; P:regulation of plant organ morphogenesis; IMP:UniProtKB. DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB. DR GO; GO:0009733; P:response to auxin; IEP:UniProtKB. DR GO; GO:0009409; P:response to cold; IEP:UniProtKB. DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB. DR GO; GO:0009408; P:response to heat; IEP:UniProtKB. DR GO; GO:0009639; P:response to red or far red light; IMP:TAIR. DR GO; GO:1902074; P:response to salt; IEP:UniProtKB. DR GO; GO:1990785; P:response to water-immersion restraint stress; IEP:UniProtKB. DR GO; GO:0009826; P:unidimensional cell growth; IMP:UniProtKB. DR CDD; cd11445; bHLH_AtPIF_like; 1. DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1. DR InterPro; IPR011598; bHLH_dom. DR InterPro; IPR036638; HLH_DNA-bd_sf. DR InterPro; IPR047265; PIF1-like_bHLH. DR InterPro; IPR044273; PIF3-like. DR PANTHER; PTHR46807; TRANSCRIPTION FACTOR PIF3; 1. DR PANTHER; PTHR46807:SF1; TRANSCRIPTION FACTOR PIF3; 1. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1. DR PROSITE; PS50888; BHLH; 1. DR Genevisible; O80536; AT. 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 REGION 38..70 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 141..194 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 239..259 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 281..358 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 483..524 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 38..66 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 145..194 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 281..305 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 306..329 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 124 FT /note="E -> D (in strain: cv. An-2 and cv. Su-0)" FT VARIANT 141 FT /note="K -> N (in strain: cv. An-2 and cv. Su-0)" 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:0000269|PubMed:17614917" FT CONFLICT 344 FT /note="S -> L (in Ref. 3; AAC99771)" FT /evidence="ECO:0000269|PubMed:17614917" 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 //