ID PIF3_ARATH Reviewed; 524 AA. AC O80536; A5Y7A2; A5Y7A3; A5Y7A4; A5Y7A5; A5Y7A6; A5Y7A7; A5Y7A8; AC A5Y7A9; A5Y7B0; A5Y7B1; A5Y7B2; A5Y7B3; A5Y7B4; A5Y7B5; A5Y7B6; AC Q9SBC5; DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 17-FEB-2016, entry version 132. 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; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC 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 RT photoinduced signal transduction, is a novel basic helix-loop-helix RT 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., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA 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., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). RN [5] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. 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., RA Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., RA Shibata K., 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; RP ASN-141; 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, RC cv. Di-1, cv. Et-0, cv. Kl-1, cv. Li-5:3, cv. Ma-2, cv. Mt-0, RC cv. Pa-2, 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 RT responses to crowding: GIGANTEA affects fruit set in Arabidopsis RT 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 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). CC -!- FUNCTION: Transcription factor acting positively in the CC phytochrome signaling pathway. Activates transcription by binding CC to the G box (5'-CACGTG-3'). {ECO:0000269|PubMed:10466729, CC ECO:0000269|PubMed:10797009}. CC -!- SUBUNIT: Homodimer (Probable). Can form a heterodimer with REP1 CC and PIF4. Phytochrome B binds specifically to DNA-bound PIF3, but CC only upon red light induced conversion to the Pfr form (PfrB). CC Reconversion to Pr form causes rapid dissociation. Interacts with CC APRR1/TOC1. {ECO:0000269|PubMed:11828023, CC ECO:0000269|PubMed:12826627, ECO:0000269|PubMed:12897250, CC ECO:0000305}. CC -!- INTERACTION: CC Self; NbExp=3; IntAct=EBI-625701, EBI-625701; CC Q9FE22:HFR1; NbExp=6; IntAct=EBI-625701, EBI-626001; CC P14712:PHYA; NbExp=8; IntAct=EBI-625701, EBI-624446; CC P14713:PHYB; NbExp=19; IntAct=EBI-625701, EBI-300727; CC Q8GZM7:PIF1; NbExp=6; IntAct=EBI-625701, EBI-630400; CC Q8W2F3-2:PIF4; NbExp=3; IntAct=EBI-625701, EBI-625732; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- INDUCTION: By UV treatment. {ECO:0000269|PubMed:12679534}. CC -!- SIMILARITY: Contains 1 bHLH (basic helix-loop-helix) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00981}. 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; 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_172424.1; NM_100824.2. DR RefSeq; NP_849626.1; NM_179295.2. DR UniGene; At.10926; -. DR ProteinModelPortal; O80536; -. DR SMR; O80536; 352-395. DR BioGrid; 22720; 28. DR DIP; DIP-33892N; -. DR IntAct; O80536; 12. DR MINT; MINT-8058904; -. DR STRING; 3702.AT1G09530.1; -. DR PaxDb; O80536; -. DR PRIDE; O80536; -. DR EnsemblPlants; AT1G09530.1; AT1G09530.1; AT1G09530. DR EnsemblPlants; AT1G09530.2; AT1G09530.2; AT1G09530. DR GeneID; 837479; -. DR Gramene; AT1G09530.1; AT1G09530.1; AT1G09530. DR Gramene; AT1G09530.2; AT1G09530.2; AT1G09530. DR KEGG; ath:AT1G09530; -. DR TAIR; AT1G09530; -. DR eggNOG; ENOG410IV8V; Eukaryota. DR eggNOG; ENOG4111SYS; LUCA. DR InParanoid; O80536; -. DR KO; K12126; -. DR OMA; DNQKACL; -. DR PhylomeDB; O80536; -. DR PRO; PR:O80536; -. DR Proteomes; UP000006548; Chromosome 1. DR Genevisible; O80536; AT. DR GO; GO:0005634; C:nucleus; IDA:TAIR. DR GO; GO:0003677; F:DNA binding; IDA:TAIR. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS: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 GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 4.10.280.10; -; 1. DR InterPro; IPR011598; bHLH_dom. 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 Complete proteome; DNA-binding; Nucleus; KW Phytochrome signaling pathway; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 524 Transcription factor PIF3. FT /FTId=PRO_0000127428. FT DOMAIN 343 392 bHLH. {ECO:0000255|PROSITE- FT ProRule:PRU00981}. FT COMPBIAS 353 358 Poly-Arg. FT COMPBIAS 422 428 Poly-Ala. FT VARIANT 124 124 E -> D (in strain: cv. An-2 and cv. Su- FT 0). {ECO:0000269|PubMed:17614917}. FT VARIANT 141 141 K -> N (in strain: cv. An-2 and cv. Su- FT 0). {ECO:0000269|PubMed:17614917}. FT VARIANT 176 176 Q -> H (in strain: cv. An-2 and cv. Su- FT 0). {ECO:0000269|PubMed:17614917}. FT VARIANT 186 186 Q -> K (in strain: cv. An-2 and cv. Su- FT 0). {ECO:0000269|PubMed:17614917}. FT VARIANT 209 209 F -> L (in strain: cv. An-2 and cv. Su- FT 0). {ECO:0000269|PubMed:17614917}. FT VARIANT 220 220 T -> I (in strain: cv. An-2 and cv. Su- FT 0). {ECO:0000269|PubMed:17614917}. FT VARIANT 236 236 V -> I (in strain: cv. An-2 and cv. Su- FT 0). {ECO:0000269|PubMed:17614917}. FT CONFLICT 15 15 E -> D (in Ref. 3; AAC99771). FT {ECO:0000305}. FT CONFLICT 344 344 S -> L (in Ref. 3; AAC99771). FT {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 //