ID A0A2U9BB19_SCOMX Unreviewed; 302 AA.
AC A0A2U9BB19;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=CCAAT/enhancer-binding protein {ECO:0000256|PIRNR:PIRNR005879};
GN Name=cebpa {ECO:0000313|Ensembl:ENSSMAP00000042618.1};
GN ORFNames=SMAX5B_004737 {ECO:0000313|EMBL:AWP01020.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP01020.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP01020.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSMAP00000042618.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR005879}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily.
CC {ECO:0000256|ARBA:ARBA00006951, ECO:0000256|PIRNR:PIRNR005879}.
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DR EMBL; CP026247; AWP01020.1; -; Genomic_DNA.
DR Ensembl; ENSSMAT00000084178.1; ENSSMAP00000042618.1; ENSSMAG00000033368.1.
DR GeneTree; ENSGT00940000162646; -.
DR OrthoDB; 2959124at2759; -.
DR Proteomes; UP000246464; Chromosome 5.
DR Proteomes; UP000694558; Chromosome 5.
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 GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd14712; bZIP_CEBPB; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR031106; C/EBP.
DR InterPro; IPR016468; C/EBP_chordates.
DR PANTHER; PTHR23334; CCAAT/ENHANCER BINDING PROTEIN; 1.
DR PANTHER; PTHR23334:SF5; CCAAT_ENHANCER-BINDING PROTEIN ALPHA; 1.
DR Pfam; PF07716; bZIP_2; 1.
DR PIRSF; PIRSF005879; CCAAT/enhancer-binding; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; Leucine zipper domain; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|PIRNR:PIRNR005879};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|PIRNR:PIRNR005879};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR005879};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Transcription {ECO:0000256|PIRNR:PIRNR005879};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR005879}.
FT DOMAIN 229..292
FT /note="BZIP"
FT /evidence="ECO:0000259|PROSITE:PS50217"
FT REGION 118..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 254..288
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 118..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 302 AA; 34537 MW; 2D26FC3F7CB6CDA6 CRC64;
MELANLYEVA PRPLMNSLAH GQQPSSGYRD PADLGGEIGD NETSIDLSAY IDPSAFNDDF
LADLFHHSSR QDKLKIMNGE YESAPCGPGP QQLYMSNYME SKLEPLYEHN PQRIRPVAIK
QEPRDDEDLN PGMPPTYHHP HPHPQQYSQH AQQQQPQPQM SHLQYQIAHC AQTTMHLQPG
HPTPPPTPVP SPHQQQHHHQ HHHPQQGGLK LLEHHRGGGK GKKNVDKSSP EYRLRRERNN
VAVRKSRDKA KVRNIETQQK VVELSTDNDR LRRRVEHLTR ELDTLRGIFR QLPDGSFKPM
GS
//
