ID   CPRF1_PETCR             Reviewed;         411 AA.
AC   Q99089;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Common plant regulatory factor 1;
DE            Short=CPRF-1;
GN   Name=CPRF1; Synonyms=CPRF-1;
OS   Petroselinum crispum (Parsley) (Petroselinum hortense).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC   Apieae; Petroselinum.
OX   NCBI_TaxID=4043;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2050115; DOI=10.1002/j.1460-2075.1991.tb07702.x;
RA   Weisshaar B., Armstrong G.A., Block A., da Costa e Silva O., Hahlbrock K.;
RT   "Light-inducible and constitutively expressed DNA-binding proteins
RT   recognizing a plant promoter element with functional relevance in light
RT   responsiveness.";
RL   EMBO J. 10:1777-1786(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Hamburger Schnitt;
RX   PubMed=8757392; DOI=10.1007/bf02174110;
RA   Feldbruegge M., Hahlbrock K., Weisshaar B.;
RT   "The transcriptional regulator CPRF1: expression analysis and gene
RT   structure.";
RL   Mol. Gen. Genet. 251:619-627(1996).
CC   -!- FUNCTION: Binds to the G-box-like motif (5'-ACGTGGC-3') of the chalcone
CC       synthase (CHS) gene promoter. G-box and G-box-like motifs are defined
CC       in promoters of certain plant genes which are regulated by such diverse
CC       stimuli as light-induction or hormone control.
CC   -!- SUBUNIT: Binds DNA as a dimer.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- INDUCTION: By light.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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; X58575; CAA41451.1; -; mRNA.
DR   EMBL; U46217; AAC49398.1; -; Genomic_DNA.
DR   PIR; S16322; S16322.
DR   AlphaFoldDB; Q99089; -.
DR   SMR; Q99089; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   CDD; cd14702; bZIP_plant_GBF1; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR045314; bZIP_plant_GBF1.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR044827; GBF-like.
DR   InterPro; IPR012900; MFMR.
DR   PANTHER; PTHR45967; PTHR45967; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   Pfam; PF07777; MFMR; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Transcription; Transcription regulation.
FT   CHAIN           1..411
FT                   /note="Common plant regulatory factor 1"
FT                   /id="PRO_0000076572"
FT   DOMAIN          269..332
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          232..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..290
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          297..332
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          346..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..168
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..185
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..293
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..390
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   411 AA;  43990 MW;  2FAF63164BFEF3BE CRC64;
     MGNTDDVKAV KPEKLSSPPP PAAPDQSNSH VYPDWAAMQA YYGPRVALPP YFNPAVASGQ
     SPHPYMWGPP QPVMPPYGVP YAALYAHGGV YAHPGVPLAA SPMSMDTHAK SSGTNEHGLI
     KKLKGHDDLA MSIGNGKADS SEGEMERTLS QSKETEGSSD GSNENSKRAA VNGRKRGRDE
     APNMIGEVKI ETQSSVIPSP RAKSEKLLGI TVATPMVAGK VVGTVVSPSM TSSLELKDSP
     KEHAVNSPAG GQQPSTMMPN DSWLHNDRDL KRERRKQSNR ESARRSRLRK QAEAEELAIK
     VDSLTAENMA LKAEINRLTL TAEKLTNDNS RLLEVMKNAQ AERAADVGLG NNNEKKASTL
     STANLLSRVD NAGSGDRDEG ESDVYEKTTK SGAKLHQLLD ANPRTDAVAA G