CEBP_DROVI
ID CEBP_DROVI Reviewed; 451 AA.
AC Q02638;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=CCAAT/enhancer-binding protein;
DE Short=C/EBP;
DE AltName: Full=Slow border cell protein;
GN Name=slbo;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1394432; DOI=10.1016/0092-8674(92)90265-e;
RA Montell D.J., Rorth P., Spradling A.C.;
RT "Slow border cells, a locus required for a developmentally regulated cell
RT migration during oogenesis, encodes Drosophila C/EBP.";
RL Cell 71:51-62(1992).
CC -!- FUNCTION: May be required for the expression of gene products mediating
CC border cell migration. Among the DNA sequences that this protein binds
CC with high affinity is a conserved site within the promoter of its gene.
CC -!- SUBUNIT: Binds DNA as a dimer and can form stable heterodimers.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
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DR EMBL; L00725; AAA28416.1; -; Genomic_DNA.
DR AlphaFoldDB; Q02638; -.
DR SMR; Q02638; -.
DR STRING; 7244.FBpp0235158; -.
DR eggNOG; KOG3119; Eukaryota.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:EnsemblMetazoa.
DR GO; GO:0007298; P:border follicle cell migration; IEA:EnsemblMetazoa.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IEA:EnsemblMetazoa.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblMetazoa.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Nucleus; Transcription; Transcription regulation.
FT CHAIN 1..451
FT /note="CCAAT/enhancer-binding protein"
FT /id="PRO_0000076632"
FT DOMAIN 365..428
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 210..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..398
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 400..407
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 210..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 50801 MW; 2AB7D00740DC01AF CRC64;
MLNMESPQMY ADAVQTLAHV DLKKQPQPLP QQATIGQITL TAMSSAQQQQ QQQQQQQQQQ
QQQQQQQQQV TTDANNNATV QDAALLVKQH AMQQMQLSNN NSNNLLQKQM LQQYSTQTDL
DELTTQEITL DLQHLIDDQF RDTETLGIFS DMVTSPGGLS ATLPPSGMVS AAAKVLQQQQ
QTLANARQQQ HSYGRAALAY MRQAVHSNAT YNNHSSDENS SVGSDSSSTI KEEPIDPDYR
RHLQESVTGQ AAAAFINNSN GLYNAYQSNN LSNNNSSSNN SSNNSSNNSS NSNTNSTNAA
QFTNLTTANV LAHHSLPHLT ANTAQQLLKH HSKLQQTQQQ HAQQQQQHAQ QQHRKHSNKH
VDKGTEEYRR RRERNNIAVR KSREKAKVRS KEVEERVKSL LKEKDALLRQ LSEMTNELSL
HKQIYMQLMN HTNPEVSRVC RSFLNTNEHA L
