ID   OP2_MAIZE               Reviewed;         453 AA.
AC   P12959;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Regulatory protein opaque-2;
GN   Name=O2;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AC 1503 GM 1407;
RX   PubMed=2798113; DOI=10.1093/nar/17.18.7532;
RA   Maddaloni M., di Fonzo N., Hartings H., Lazzaroni N., Salamini F.,
RA   Thompson R.D., Motto M.;
RT   "The sequence of the zein regulatory gene opaque-2 (O2) of Zea mays.";
RL   Nucleic Acids Res. 17:7532-7532(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AC 1503 GM 1407; TISSUE=Seed endosperm;
RX   PubMed=2479535; DOI=10.1002/j.1460-2075.1989.tb08425.x;
RA   Hartings H., Maddaloni M., Lazzaroni N., di Fonzo N., Motto M.,
RA   Salamini F., Thompson R.D.;
RT   "The O2 gene which regulates zein deposition in maize endosperm encodes a
RT   protein with structural homologies to transcriptional activators.";
RL   EMBO J. 8:2795-2801(1989).
RN   [3]
RP   FUNCTION.
RX   PubMed=2001677; DOI=10.1002/j.1460-2075.1991.tb07989.x;
RA   Lohmer S., Maddaloni M., Motto M., di Fonzo N., Hartings H., Salamini F.,
RA   Thompson R.D.;
RT   "The maize regulatory locus Opaque-2 encodes a DNA-binding protein which
RT   activates the transcription of the b-32 gene.";
RL   EMBO J. 10:617-624(1991).
RN   [4]
RP   TISSUE SPECIFICITY, AND INTERACTION WITH PBF.
RX   PubMed=9207153; DOI=10.1073/pnas.94.14.7685;
RA   Vicente-Carbajosa J., Moose S.P., Parsons R.L., Schmidt R.J.;
RT   "A maize zinc-finger protein binds the prolamin box in zein gene promoters
RT   and interacts with the basic leucine zipper transcriptional activator
RT   Opaque-2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:7685-7690(1997).
CC   -!- FUNCTION: Involved in the regulation of the endosperm-specific
CC       production of albumin b-32 and other zein proteins. It is a trans-
CC       acting transcriptional activator that binds to the consensus sequence
CC       5'-GATGAYRTGR-3'. {ECO:0000269|PubMed:2001677}.
CC   -!- SUBUNIT: Interacts with the Dof zinc finger protein PBF.
CC       {ECO:0000269|PubMed:9207153}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Seed endosperm. {ECO:0000269|PubMed:9207153}.
CC   -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR   EMBL; X15544; CAA33550.1; -; Genomic_DNA.
DR   EMBL; X16618; CAA34614.1; -; mRNA.
DR   PIR; S06022; S06022.
DR   AlphaFoldDB; P12959; -.
DR   SMR; P12959; -.
DR   STRING; 4577.GRMZM2G015534_P01; -.
DR   PaxDb; P12959; -.
DR   PRIDE; P12959; -.
DR   MaizeGDB; 24976; -.
DR   eggNOG; ENOG502QS0A; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P12959; baseline and differential.
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   InterPro; IPR020983; Basic_leucine-zipper_C.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR045314; bZIP_plant_GBF1.
DR   InterPro; IPR046347; bZIP_sf.
DR   Pfam; PF00170; bZIP_1; 1.
DR   Pfam; PF12498; bZIP_C; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..453
FT                   /note="Regulatory protein opaque-2"
FT                   /id="PRO_0000076542"
FT   DOMAIN          225..288
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          145..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..251
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          253..274
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   COMPBIAS        145..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        26
FT                   /note="E -> EPEPEPE (in Ref. 2; CAA34614)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        144
FT                   /note="D -> A (in Ref. 2; CAA34614)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        231
FT                   /note="K -> KR (in Ref. 2; CAA34614)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   453 AA;  49357 MW;  513A8AB8D5ABD999 CRC64;
     MEHVISMEEI LGPFWELLPP PAPEPEREQP PVTGIVVGSV IDVAAAGHGD GDMMDQQHAT
     EWTFERLLEE EALTTSTPPP VVVVPNSCCS GALNADRPPV MEEAVTMAPA AVSSAVVGDP
     MEYNAILRRK LEEDLEAFKM WRADSSVVTS DQRSQGSNNH TGGSSIRNNP VQNKLMNGED
     PINNNHAQTA GLGVRLATSS SSRDPSPSDE DMDGEVEILG FKMPTEERVR KKESNRESAR
     RSRYRKAAHL KELEDQVAQL KAENSCLLRR IAALNQKYND ANVDNRVLRA DMETLRAKVK
     MGEDSLKRVI EMSSSVPSSM PISAPTPSSD APVPPPPIRD SIVGYFSATA ADDDASVGNG
     FLRLQAHQEP ASMVVGGTLS ATEMNRVAAA THCAGAMELI QTAMGSMPPT SASGSTPPPQ
     IMSCWVQMGP YTWTCIRHCG FRDRWEHFIC RRR