CEBPD_BOVIN
ID CEBPD_BOVIN Reviewed; 256 AA.
AC O02756; A3KN42;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=CCAAT/enhancer-binding protein delta;
DE Short=C/EBP delta;
GN Name=CEBPD;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Japanese black;
RX PubMed=9051484; DOI=10.2527/1997.752586x;
RA Taniguchi Y., Sasaki Y.;
RT "Nucleotide sequence of bovine C/EBP delta gene.";
RL J. Anim. Sci. 75:586-586(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription activator that recognizes two different DNA
CC motifs: the CCAAT homology common to many promoters and the enhanced
CC core homology common to many enhancers. Important transcription factor
CC regulating the expression of genes involved in immune and inflammatory
CC responses. Transcriptional activator that enhances IL6 transcription
CC alone and as heterodimer with CEBPB. {ECO:0000250|UniProtKB:P49716}.
CC -!- SUBUNIT: Binds DNA as a homodimer and as a heterodimer. Can form stable
CC heterodimers with CEBPB. Can form stable heterodimers with CEBPA and
CC CEBPE. Interacts with SPI1/PU.1. Interacts with PRDM16.
CC {ECO:0000250|UniProtKB:P49716, ECO:0000250|UniProtKB:Q00322}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
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DR EMBL; D82986; BAA20097.1; -; Genomic_DNA.
DR EMBL; BC133581; AAI33582.1; -; mRNA.
DR RefSeq; NP_776692.2; NM_174267.2.
DR AlphaFoldDB; O02756; -.
DR SMR; O02756; -.
DR PRIDE; O02756; -.
DR Ensembl; ENSBTAT00000064621; ENSBTAP00000070327; ENSBTAG00000046307.
DR GeneID; 281678; -.
DR KEGG; bta:281678; -.
DR CTD; 1052; -.
DR VEuPathDB; HostDB:ENSBTAG00000046307; -.
DR VGNC; VGNC:106685; CEBPD.
DR GeneTree; ENSGT00940000163032; -.
DR InParanoid; O02756; -.
DR OMA; QIATCAQ; -.
DR OrthoDB; 1284308at2759; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000046307; Expressed in ureter and 100 other tissues.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Activator; DNA-binding; Isopeptide bond; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P49716"
FT CHAIN 2..256
FT /note="CCAAT/enhancer-binding protein delta"
FT /id="PRO_0000310863"
FT DOMAIN 178..241
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 18..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..209
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 213..241
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 144..163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P49716"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CONFLICT 178
FT /note="S -> G (in Ref. 2; AAI33582)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 256 AA; 27137 MW; E4C81840EF98BC3E CRC64;
MSAALFSLDG PARGAPWTAE PAAFYEPGRA GKPGRGAEPA ASAMYDDESA IDFSAYIDSM
AAVPTLELCH DELFADLFNS NHKAGALELL PGGPARLGGP GPAPRPLKRE PDWGDGDAPG
SLLPAQVAAC AQTVVSLAAA AQPTPPASPE PPRRSPAPPA PGPARDKAAG KRGPDRGSPE
YRQRRERNNI AVRKSRDKAK RRNQEMQQKL VELSAENEKL QQRVEQLTRD LAGLRRFFKQ
LPGAPFLPGA GAADAR
