CEBPD_MOUSE
ID CEBPD_MOUSE Reviewed; 268 AA.
AC Q00322; Q3U937; Q8BW92;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=CCAAT/enhancer-binding protein delta;
DE Short=C/EBP delta;
DE AltName: Full=C/EBP-related protein 3 {ECO:0000303|PubMed:1884998};
GN Name=Cebpd; Synonyms=Crp3 {ECO:0000303|PubMed:1884998};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1840554; DOI=10.1101/gad.5.9.1538;
RA Cao Z., Umek R.M., McKnight S.L.;
RT "Regulated expression of three C/EBP isoforms during adipose conversion of
RT 3T3-L1 cells.";
RL Genes Dev. 5:1538-1552(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RC TISSUE=Adipose tissue, and Lung;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP INTERACTION WITH SPI1, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7594592;
RA Nagulapalli S., Pongubala J.M., Atchison M.L.;
RT "Multiple proteins physically interact with PU.1. Transcriptional synergy
RT with NF-IL6 beta (C/EBP delta, CRP3).";
RL J. Immunol. 155:4330-4338(1995).
RN [5]
RP INTERACTION WITH PRDM16.
RX PubMed=19641492; DOI=10.1038/nature08262;
RA Kajimura S., Seale P., Kubota K., Lunsford E., Frangioni J.V., Gygi S.P.,
RA Spiegelman B.M.;
RT "Initiation of myoblast to brown fat switch by a PRDM16-C/EBP-beta
RT transcriptional complex.";
RL Nature 460:1154-1158(2009).
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:7594592,
CC PubMed:19641492). Important transcription factor regulating the
CC expression of genes involved in immune and inflammatory responses.
CC Transcriptional activator that enhances IL6 transcription alone and as
CC heterodimer with CEBPB (By similarity). {ECO:0000250|UniProtKB:P49716,
CC ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:7594592}.
CC -!- SUBUNIT: Binds DNA as a homodimer and as a heterodimer. Can form stable
CC heterodimers with CEBPA, CEBPB and CEBPE (PubMed:1884998). Interacts
CC with SPI1/PU.1 (PubMed:7594592). Interacts with PRDM16
CC (PubMed:19641492). {ECO:0000269|PubMed:1884998,
CC ECO:0000269|PubMed:19641492, ECO:0000269|PubMed:7594592}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:7594592}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
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DR EMBL; X61800; CAA43905.1; -; mRNA.
DR EMBL; M85144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK053190; BAC35305.1; -; mRNA.
DR EMBL; AK151958; BAE30830.1; -; mRNA.
DR CCDS; CCDS84207.1; -.
DR PIR; B37279; B37279.
DR RefSeq; NP_031705.3; NM_007679.4.
DR AlphaFoldDB; Q00322; -.
DR SMR; Q00322; -.
DR BioGRID; 198670; 8.
DR DIP; DIP-41645N; -.
DR IntAct; Q00322; 4.
DR iPTMnet; Q00322; -.
DR PhosphoSitePlus; Q00322; -.
DR MaxQB; Q00322; -.
DR PRIDE; Q00322; -.
DR ProteomicsDB; 281459; -.
DR Antibodypedia; 24255; 266 antibodies from 29 providers.
DR DNASU; 12609; -.
DR Ensembl; ENSMUST00000096232; ENSMUSP00000148145; ENSMUSG00000071637.
DR GeneID; 12609; -.
DR KEGG; mmu:12609; -.
DR UCSC; uc007yhx.1; mouse.
DR CTD; 1052; -.
DR MGI; MGI:103573; Cebpd.
DR VEuPathDB; HostDB:ENSMUSG00000071637; -.
DR GeneTree; ENSGT00940000163032; -.
DR InParanoid; Q00322; -.
DR OMA; QIATCAQ; -.
DR OrthoDB; 1284308at2759; -.
DR PhylomeDB; Q00322; -.
DR BioGRID-ORCS; 12609; 2 hits in 18 CRISPR screens.
DR ChiTaRS; Cebpd; mouse.
DR PRO; PR:Q00322; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q00322; protein.
DR Bgee; ENSMUSG00000071637; Expressed in left lung lobe and 197 other tissues.
DR ExpressionAtlas; Q00322; baseline and differential.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
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; IPI:MGI.
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; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IDA:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:MGI.
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; IDA:MGI.
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 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_0000076622"
FT DOMAIN 191..254
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..219
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..170
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..219
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"
FT CONFLICT 41
FT /note="D -> E (in Ref. 1; CAA43905)"
FT /evidence="ECO:0000305"
FT CONFLICT 255..258
FT /note="PSPP -> AQPA (in Ref. 3; BAC35305)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 268 AA; 28631 MW; 151F765946CDB275 CRC64;
MSAALFSLDS PVRGTPWPTE PAAFYEPGRV DKPGRGPEPG DLGELGSTTP AMYDDESAID
FSAYIDSMAA VPTLELCHDE LFADLFNSNH KAAGAGGLEL LQGGPTRPPG VGSVARGPLK
REPDWGDGDA PGSLLPAQVA VCAQTVVSLA AAAQPTPPTS PEPPRGSPGP SLAPGTVREK
GAGKRGPDRG SPEYRQRRER NNIAVRKSRD KAKRRNQEMQ QKLVELSAEN EKLHQRVEQL
TRDLAGLRQF FKKLPSPPFL PPTGADCR
