CEBPE_RAT
ID CEBPE_RAT Reviewed; 281 AA.
AC P56261;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=CCAAT/enhancer-binding protein epsilon;
DE Short=C/EBP epsilon;
DE AltName: Full=C/EBP-related protein 1 {ECO:0000303|PubMed:1884998};
GN Name=Cebpe; Synonyms=Crp1 {ECO:0000303|PubMed:1884998};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9593684; DOI=10.1074/jbc.273.22.13493;
RA Williams S.C., Du Y., Schwartz R.C., Weiler S.R., Ortiz M., Keller J.R.,
RA Johnson P.F.;
RT "C/EBPepsilon is a myeloid-specific activator of cytokine, chemokine, and
RT macrophage-colony-stimulating factor receptor genes.";
RL J. Biol. Chem. 273:13493-13501(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-281, AND SUBUNIT.
RX PubMed=1884998; DOI=10.1101/gad.5.9.1553;
RA Williams S.C., Cantwell C.A., Johnson P.F.;
RT "A family of C/EBP-related proteins capable of forming covalently linked
RT leucine zipper dimers in vitro.";
RL Genes Dev. 5:1553-1567(1991).
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 (PubMed:1884998). Interacts
CC with GATA1 AND SPI1 (By similarity). Interacts with SMARCD2 (By
CC similarity). {ECO:0000250|UniProtKB:Q15744,
CC ECO:0000269|PubMed:1884998}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15744}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
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DR EMBL; AF034716; AAC24455.1; -; Genomic_DNA.
DR PIR; A37280; A37280.
DR RefSeq; NP_058791.1; NM_017095.1.
DR AlphaFoldDB; P56261; -.
DR SMR; P56261; -.
DR STRING; 10116.ENSRNOP00000019154; -.
DR PaxDb; P56261; -.
DR Ensembl; ENSRNOT00000019155; ENSRNOP00000019154; ENSRNOG00000014282.
DR GeneID; 25410; -.
DR KEGG; rno:25410; -.
DR UCSC; RGD:2329; rat.
DR CTD; 1053; -.
DR RGD; 2329; Cebpe.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00940000161681; -.
DR HOGENOM; CLU_043327_0_0_1; -.
DR InParanoid; P56261; -.
DR OMA; CDHEASI; -.
DR OrthoDB; 1284308at2759; -.
DR PhylomeDB; P56261; -.
DR TreeFam; TF105008; -.
DR PRO; PR:P56261; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000014282; Expressed in thymus and 7 other tissues.
DR Genevisible; P56261; RN.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0042742; P:defense response to bacterium; ISO:RGD.
DR GO; GO:0030851; P:granulocyte differentiation; ISO:RGD.
DR GO; GO:0030225; P:macrophage differentiation; ISO:RGD.
DR GO; GO:0030099; P:myeloid cell differentiation; IEP:RGD.
DR GO; GO:0006909; P:phagocytosis; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 1: Evidence at protein 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_0000076626"
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..245
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 246..267
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; 30590 MW; 68B16455C034E250 CRC64;
MSHGTYYECE PRGGQQPLEF SGGRAGPGEL GDMCEHEASI DLSAYIESGE EQLLSDLFAM
KPTPEARSLK GPGTPSFPHY LPADPRPFAY PSHTFGPDRK ALGPGIYSNP GSYDPRAVAV
KEEPRGPEGN RGTGRGSYNP LQYQVAHCGQ TAVHLPPTLA APGQPLRVLK APVAAAAPPC
SPLLKAPSPA GPSHKGKKAV NKDSLEYRLR RERNNIAVRK SRDKAKRRIM ETQQKVLEYM
AENERLRSRV DQLTQELDTL RNLFRQIPEA ASLIKGVGGC S
