CEBPE_SHEEP
ID CEBPE_SHEEP Reviewed; 281 AA.
AC O77728;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=CCAAT/enhancer-binding protein epsilon;
DE Short=C/EBP epsilon;
GN Name=CEBPE;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=9856407; DOI=10.2527/1998.76112953x;
RA Sabatakos G., Kousteni S., Cryer A., Ramji D.P.;
RT "Nucleotide sequence of ovine C/EBPepsilon gene.";
RL J. Anim. Sci. 76:2953-2954(1998).
CC -!- FUNCTION: Transcriptional activator. C/EBP are DNA-binding proteins
CC that recognize two different motifs: the CCAAT homology common to many
CC promoters and the enhanced core homology common to many enhancers.
CC Required for the promyelocyte-myelocyte transition in myeloid
CC differentiation. {ECO:0000250|UniProtKB:Q15744}.
CC -!- SUBUNIT: Binds DNA as a homodimer and as a heterodimer. Can form stable
CC heterodimers with CEBPA, CEBPB and CEBPD (By similarity). Interacts
CC with GATA1 AND SPI1 (By similarity). Interacts with SMARCD2 (By
CC similarity). {ECO:0000250|UniProtKB:P56261,
CC ECO:0000250|UniProtKB:Q15744}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
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DR EMBL; AJ222689; CAA10944.1; -; Genomic_DNA.
DR AlphaFoldDB; O77728; -.
DR SMR; O77728; -.
DR STRING; 9940.ENSOARP00000020798; -.
DR eggNOG; KOG3119; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
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 InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR016468; C/EBP_chordates.
DR Pfam; PF07716; bZIP_2; 1.
DR PIRSF; PIRSF005879; CCAAT/enhancer-binding; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..281
FT /note="CCAAT/enhancer-binding protein epsilon"
FT /id="PRO_0000076627"
FT DOMAIN 204..267
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..228
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 230..237
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PZD9"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15744"
SQ SEQUENCE 281 AA; 30639 MW; 14C8B841D40A29D7 CRC64;
MSHGTYYECE PRAGQQPLEF SGARAGPGEL GDMCEHEASI DLSAYIESGE EQLLSDLFAV
KPAPEARELK GPGTPAFPHY LPADPRPFTY PPHTFGPDRK ALGPGIYSSP GSYDPRAVAV
KEEPRGPEGS RGASRSGYNP LQYQVAHCGQ TAMHLPPGLA SPSQPLRVLK APLAAAAPPC
SPLLKAPSPA GPSHKGKKAV NKDSLEYRLR RERNNIAVRK SRDKAKRRIL ETQQKVLEYM
AENERLRSRV EQLTQELDTL RNLFRQIPEA ANLIKGVGGC S
