CEBPD_SHEEP
ID CEBPD_SHEEP Reviewed; 255 AA.
AC Q9N0J3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=CCAAT/enhancer-binding protein delta;
DE Short=C/EBP delta;
GN Name=CEBPD;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=10799300; DOI=10.1006/bbrc.2000.2630;
RA Davies G.E., Sabatakos G., Cryer A., Ramji D.P.;
RT "The ovine CCAAT-enhancer binding protein delta gene: cloning,
RT characterization, and species-specific autoregulation.";
RL Biochem. Biophys. Res. Commun. 271:346-352(2000).
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 (PubMed:10799300). Important
CC transcription factor regulating the expression of genes involved in
CC immune and inflammatory responses. Transcriptional activator that
CC enhances IL6 transcription alone and as heterodimer with CEBPB (By
CC similarity). {ECO:0000250|UniProtKB:P49716,
CC ECO:0000269|PubMed:10799300}.
CC -!- SUBUNIT: Binds DNA as a homodimer and as a heterodimer. Can form stable
CC heterodimers with CEBPA, CEBPB and CEBPE. Interacts with SPI1/PU.1.
CC Interacts with PRDM16. {ECO:0000250|UniProtKB:P49716,
CC ECO:0000250|UniProtKB:Q00322}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000305|PubMed:10799300}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
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DR EMBL; AJ276820; CAB92973.1; -; Genomic_DNA.
DR PIR; JC7264; JC7264.
DR AlphaFoldDB; Q9N0J3; -.
DR SMR; Q9N0J3; -.
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 3: Inferred from homology;
KW Activator; DNA-binding; Isopeptide bond; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..255
FT /note="CCAAT/enhancer-binding protein delta"
FT /id="PRO_0000310864"
FT DOMAIN 177..240
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..208
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 212..240
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 141..162
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 107
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 255 AA; 27040 MW; 85227319B6DE4F13 CRC64;
MTCALQPGRP SGGAPWTAEP AAFYEPGRAG KPGRGAEPAA PAMYDDESAI DFSAYIDSMA
AVPTLELCHD ELFADLFNSN HKAGALELLP GGPARLGGPG PAPRPLKREP DWGDGDAPGS
LLPAQVAACA QTVVSLAPAA QPTPPASPDP PRRSPAPPAP GPARDKAAGK RGPDRGSPEY
RQRRERNNIA VRKSRDKAKR RNQEMQQKLV ELSAENEKLQ QRVEQLTRDL AGLRRFFKQL
PGAPFLPGAG AADAR