ID PIF3_ARATH STANDARD; PRT; 524 AA. AC O80536; Q9SBC5; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Phytochrome-interacting factor 3 (Phytochrome-associated protein 3) DE (Basic helix-loop-helix protein 8) (bHLH8). GN PIF3 OR PAP3 OR AT1G09530 OR F14J9.19. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Columbia; RX MEDLINE=99059501; PubMed=9845368; 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 SEQUENCE FROM N.A. 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 [3] RP SEQUENCE FROM N.A. RC STRAIN=cv. Columbia; RA Schoenbohm C., Weisshaar B.; RT "Overview of the BHLH transcription factor gene family in Arabidopsis RT thaliana."; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; 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 FUNCTION. RX MEDLINE=99394605; PubMed=10466729; 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 [6] RP FUNCTION. RX MEDLINE=20259742; PubMed=10797009; 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). CC -!- FUNCTION: Transcription factor acting positively in the CC phytochrome signaling pathway. Activates transcription by binding CC to the G box (5'-CACGTG-3'). CC -!- SUBUNIT: Homodimer (Probable). Can form a heterodimer with REP1. CC Phytochrome B binds specifically to DNA-bound PIF3, but only upon CC red light induced conversion to the Pfr form (PfrB). Reconversion CC to Pr form causes rapid dissociation. CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- SIMILARITY: BELONGS TO THE BASIC HELIX-LOOP-HELIX (BHLH) FAMILY OF CC TRANSCRIPTION FACTORS. 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; -. DR EMBL; AF088280; AAC99771.1; -. DR EMBL; AF251693; AAL55715.1; -. DR EMBL; AC003970; AAC33213.1; -. DR PIR; H86228; H86228. DR HSSP; P25912; 1HLO. DR TRANSFAC; T04492; -. DR InterPro; IPR001092; HLH_basic. DR Pfam; PF00010; HLH; 1. DR SMART; SM00353; HLH; 1. DR PROSITE; PS00038; HLH_1; 1. DR PROSITE; PS50888; HLH_2; 1. KW Nuclear protein; Transcription regulation; DNA-binding; KW Phytochrome signaling pathway. FT DNA_BIND 340 356 BASIC DOMAIN (BY SIMILARITY). FT DOMAIN 357 393 HELIX-LOOP-HELIX MOTIF (BY SIMILARITY). FT DOMAIN 353 358 POLY-ARG. FT DOMAIN 422 428 POLY-ALA. FT CONFLICT 15 15 E -> D (IN REF. 2). FT CONFLICT 344 344 S -> L (IN REF. 2). 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 //