Q00322 (CEBPD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CCAAT/enhancer-binding protein delta
Short name=C/EBP delta

Alternative name(s):
C/EBP-related protein 3

Gene names

Name:	Cebpd
Synonyms:	Crp3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	268 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	C/EBP is a DNA-binding protein that recognizes two different motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers. Important transcriptional activator in the regulation of genes involved in immune and inflammatory responses, may play an important role in the regulation of the several genes associated with activation and/or differentiation of macrophages By similarity.
Subunit structure	Binds DNA as a dimer and can form stable heterodimers with C/EBP alpha. Interacts with SPI1/PU.1. Interacts with PRDM16. Ref.4 Ref.5
Subcellular location	Nucleus.
Sequence similarities	Belongs to the bZIP family. C/EBP subfamily. Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Activator
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fat cell differentiation Inferred from direct assay PubMed 17888405. Source: MGI inner ear development Inferred from direct assay PubMed 21795542. Source: MGI negative regulation of transcription, DNA-dependent Inferred from direct assay PubMed 15175325. Source: MGI positive regulation of osteoblast differentiation Inferred from direct assay PubMed 15175325. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 18632661. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	protein heterodimerization activity Inferred from direct assay PubMed 12177065. Source: UniProtKB protein homodimerization activity Inferred from direct assay PubMed 12821655. Source: MGI sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro transcription regulatory region DNA binding Inferred from direct assay PubMed 18632661. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 268	268	CCAAT/enhancer-binding protein delta		PRO_0000076622
Regions
	Domain	191 – 254	64	bZIP
	Region	195 – 222	28	Basic motif By similarity
	Region	226 – 254	29	Leucine-zipper By similarity
Amino acid modifications
	Cross-link	120		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Experimental info
	Sequence conflict	41	1	D → E in CAA43905. Ref.1
	Sequence conflict	255 – 258	4	PSPP → AQPA in BAC35305. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q00322 [UniParc]. Last modified November 13, 2007. Version 2. Checksum: 151F765946CDB275	FASTA	268	28,631
	10 20 30 40 50 60 MSAALFSLDS PVRGTPWPTE PAAFYEPGRV DKPGRGPEPG DLGELGSTTP AMYDDESAID 70 80 90 100 110 120 FSAYIDSMAA VPTLELCHDE LFADLFNSNH KAAGAGGLEL LQGGPTRPPG VGSVARGPLK 130 140 150 160 170 180 REPDWGDGDA PGSLLPAQVA VCAQTVVSLA AAAQPTPPTS PEPPRGSPGP SLAPGTVREK 190 200 210 220 230 240 GAGKRGPDRG SPEYRQRRER NNIAVRKSRD KAKRRNQEMQ QKLVELSAEN EKLHQRVEQL 250 260 TRDLAGLRQF FKKLPSPPFL PPTGADCR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Regulated expression of three C/EBP isoforms during adipose conversion of 3T3-L1 cells." Cao Z., Umek R.M., McKnight S.L. Genes Dev. 5:1538-1552(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"A family of C/EBP-related proteins capable of forming covalently linked leucine zipper dimers in vitro." Williams S.C., Cantwell C.A., Johnson P.F. Genes Dev. 5:1553-1567(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Adipose tissue and Lung.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone marrow and Lung.
[4]	"Multiple proteins physically interact with PU.1. Transcriptional synergy with NF-IL6 beta (C/EBP delta, CRP3)." Nagulapalli S., Pongubala J.M., Atchison M.L. J. Immunol. 155:4330-4338(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SPI1.
[5]	"Initiation of myoblast to brown fat switch by a PRDM16-C/EBP-beta transcriptional complex." Kajimura S., Seale P., Kubota K., Lunsford E., Frangioni J.V., Gygi S.P., Spiegelman B.M. Nature 460:1154-1158(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRDM16.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X61800 mRNA. Translation: CAA43905.1. M85144 Genomic DNA. No translation available. AK053190 mRNA. Translation: BAC35305.1. AK151958 mRNA. Translation: BAE30830.1.
IPI	IPI00466759.
PIR	B37279.
RefSeq	NP_031705.3. NM_007679.4.
UniGene	Mm.347407.
3D structure databases
ProteinModelPortal	Q00322.
SMR	Q00322. Positions 191-248.
ModBase	Search...
PTM databases
PhosphoSite	Q00322.
Proteomic databases
PRIDE	Q00322.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	12609.
KEGG	mmu:12609.
Organism-specific databases
CTD	1052.
MGI	MGI:103573. Cebpd.
Phylogenomic databases
HOVERGEN	HBG050879.
KO	K10050.
Enzyme and pathway databases
Reactome	REACT_127416. Developmental Biology. REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
Gene expression databases
CleanEx	MM_CEBPD.
Genevestigator	Q00322.
Family and domain databases
InterPro	IPR004827. bZIP. IPR016468. CCAAT/enhancer-binding. [Graphical view]
Pfam	PF07716. bZIP_2. 1 hit. [Graphical view]
PIRSF	PIRSF005879. CCAAT/enhancer-binding. 1 hit.
SMART	SM00338. BRLZ. 1 hit. [Graphical view]
PROSITE	PS50217. BZIP. 1 hit. PS00036. BZIP_BASIC. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	281762.
SOURCE	Search...

Entry information

Entry name

CEBPD_MOUSE

Accession

Primary (citable) accession number: Q00322
Secondary accession number(s): Q3U937, Q8BW92

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	November 13, 2007
Last modified:	April 3, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program