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Database: UniProt
Entry: Q99090
LinkDB: Q99090
Original site: Q99090 
ID   CPRF2_PETCR             Reviewed;         401 AA.
AC   Q99090;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-MAY-2023, entry version 87.
DE   RecName: Full=Light-inducible protein CPRF2;
DE   AltName: Full=Common plant regulatory factor 2;
DE            Short=CPRF-2;
GN   Name=CPRF2; Synonyms=CPRF-2;
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].
RA   Weisshaar B.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-401.
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).
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   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR   EMBL; X58577; CAA41453.1; -; mRNA.
DR   PIR; S16321; S16321.
DR   AlphaFoldDB; Q99090; -.
DR   SMR; Q99090; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   CDD; cd14702; bZIP_plant_GBF1; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   InterPro; IPR020983; Basic_leucine-zipper_C.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR045314; bZIP_plant_GBF1.
DR   InterPro; IPR046347; bZIP_sf.
DR   PANTHER; PTHR46408; BASIC LEUCINE ZIPPER 63; 1.
DR   PANTHER; PTHR46408:SF10; BASIC LEUCINE ZIPPER 63; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   Pfam; PF12498; bZIP_C; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 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..401
FT                   /note="Light-inducible protein CPRF2"
FT                   /id="PRO_0000076573"
FT   DOMAIN          198..261
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          113..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..219
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          226..247
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          300..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        9..13
FT                   /note="DISDQ -> EFAAA (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   401 AA;  43839 MW;  21E9E1D1DF48814D CRC64;
     MDRVFSVEDI SDQFWSPPAR EDSSKLVMNR SDSEWAFQSF LQQASALESS QPLPSDPVPV
     AGDVKNPVEI PANVPVDSED YQAYLKSRLD LACAAVALTR ASSLKPQDSA ALLDNGSQAS
     NTSQLVSQVP PKGSGHDLSK EEDKEALAAT ATPLLPALQK KSAIQVKSTT SGSSRDHSDD
     DDELEGETET TRNGDPSDAK RVRRMLSNRE SARRSRRRKQ AHMTELETQV SQLRVENSSL
     LKRLTDISQR YNDAAVDNRV LKADIETMRA KVKMAEETVK RVTGLNPMFQ SMSSEISTIG
     MQSFSGSPSD TSADTTQDGS KQHFYQPAPT SHMPAQDQKI QNGLLQVPPV DNLQQHSASG
     PVEGNKMERT SSMQRVASLE HLQKRIRGGV SSCEAQVSGK Q
//
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