OCS1_MAIZE
ID OCS1_MAIZE Reviewed; 151 AA.
AC P24068;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Ocs element-binding factor 1;
DE Short=OCSBF-1;
GN Name=OBF1;
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 [MRNA].
RC TISSUE=Root;
RX PubMed=2152133; DOI=10.2307/3869325;
RA Singh K., Dennis E.S., Ellis J.G., Llewellyn D.J., Tokuhisa J.G.,
RA Wahleithner J.A., Peacock W.J.;
RT "OCSBF-1, a maize ocs enhancer binding factor: isolation and expression
RT during development.";
RL Plant Cell 2:891-903(1990).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Singh K.B.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May contribute to developmentally specific patterns of gene
CC expression. Binds specifically to ocs elements which are
CC transcriptional enhancer found in the promoters of several plant genes.
CC OCSBF-1 is able to bind to a site within each half of the ocs element
CC as well as to animal AP-1 and CREB sites.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Roots and shoots of young plants, and basal portion
CC of leaves.
CC -!- MISCELLANEOUS: A derivative of OCSBF-1 that contains only the 76 N-
CC terminal amino acids is still able to bind to the ocs element.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
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DR EMBL; X62745; CAA44607.1; -; mRNA.
DR PIR; JQ0984; JQ0984.
DR PIR; T03642; T03642.
DR RefSeq; NP_001105439.1; NM_001111969.1.
DR AlphaFoldDB; P24068; -.
DR SMR; P24068; -.
DR PaxDb; P24068; -.
DR PRIDE; P24068; -.
DR GeneID; 542394; -.
DR KEGG; zma:542394; -.
DR MaizeGDB; 64064; -.
DR eggNOG; ENOG502S1GC; Eukaryota.
DR OrthoDB; 1416695at2759; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P24068; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd14702; bZIP_plant_GBF1; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR045314; bZIP_plant_GBF1.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF00170; bZIP_1; 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; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..151
FT /note="Ocs element-binding factor 1"
FT /id="PRO_0000076564"
FT DOMAIN 24..87
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 26..45
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 52..59
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 151 AA; 16976 MW; DCDB2B5F5A0245A6 CRC64;
MSSSSLSPTA GRTSGSDGDS AADTHRREKR RLSNRESARR SRLRKQQHLD ELVQEVARLQ
ADNARVAARA RDIASQYTRV EQENTVLRAR AAELGDRLRS VNEVLRLVEE FSGVAMDIQE
EMPADDPLLR PWQLPYPAAA MPMGAPHMLH Y