CEBPD_RAT
ID CEBPD_RAT Reviewed; 268 AA.
AC Q03484;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=CCAAT/enhancer-binding protein delta;
DE Short=C/EBP delta;
DE AltName: Full=Transcription factor CELF;
GN Name=Cebpd; Synonyms=Celf;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1714459; DOI=10.1016/s0021-9258(18)98648-5;
RA Kageyama R., Sasai Y., Nakanishi S.;
RT "Molecular characterization of transcription factors that bind to the cAMP
RT responsive region of the substance P precursor gene. cDNA cloning of a
RT novel C/EBP-related factor.";
RL J. Biol. Chem. 266:15525-15531(1991).
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:1714459). 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:1714459}.
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:0000305|PubMed:1714459}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:1714459}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
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DR EMBL; M65149; AAA40913.1; -; mRNA.
DR PIR; B39429; B39429.
DR RefSeq; NP_037286.1; NM_013154.2.
DR AlphaFoldDB; Q03484; -.
DR SMR; Q03484; -.
DR STRING; 10116.ENSRNOP00000064025; -.
DR iPTMnet; Q03484; -.
DR PhosphoSitePlus; Q03484; -.
DR PaxDb; Q03484; -.
DR Ensembl; ENSRNOT00000074586; ENSRNOP00000064025; ENSRNOG00000050869.
DR GeneID; 25695; -.
DR KEGG; rno:25695; -.
DR CTD; 1052; -.
DR RGD; 2328; Cebpd.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00940000163032; -.
DR HOGENOM; CLU_043327_2_1_1; -.
DR InParanoid; Q03484; -.
DR OMA; QIATCAQ; -.
DR OrthoDB; 1284308at2759; -.
DR PhylomeDB; Q03484; -.
DR PRO; PR:Q03484; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000050869; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; Q03484; RN.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0045444; P:fat cell differentiation; ISO:RGD.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0048839; P:inner ear development; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
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..268
FT /note="CCAAT/enhancer-binding protein delta"
FT /id="PRO_0000076623"
FT DOMAIN 191..254
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..222
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 226..254
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 156..171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..223
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 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 268 AA; 28600 MW; EF12ABA104C7B9F8 CRC64;
MSAALFSLDS PARGAPWPTE PAAFYEPGRV GKPGRGPEPG DLGEPGSTTP AMYDDESAID
FSAYIDSMAA VPTLELCHDE IFADLFNSNH KAAGAGSLEL LQGGPTRPPG VGSIARGPLK
REPDWGDGDA PGSLLPAQVA VCAQTVVSLA AAAQPTPPTS PEPPRGSPGP SLAPGPVREK
GAGKRGPDRG SPEYRQRRER NNIAVRKSRD KAKRRNQEMQ QKLVELSAEN EKLHQRVEQL
TRDLASLRQF FKELPSPPFL PPTGTDCR
