O70302 (CIDEA_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified May 1, 2013. Version 78. History...
Names and origin
|Protein names||Recommended name:|
Cell death activator CIDE-A
Cell death-inducing DFFA-like effector A
|Organism||Mus musculus (Mouse) [Reference proteome]|
|Taxonomic identifier||10090 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus|
|Sequence length||217 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair and occurs at a lower rate than that promoted by CIDEC. Acts as a CEBPB coactivator in mammary epithelial cells to control the expression of a subset of CEBPB downstream target genes, including ID2, IGF1, PRLR, SOCS1, SOCS3, XDH, but not casein. By interacting with CEBPB, strengthens the association of CEBPB with the XDH promoter, increases histone acetylation and dissociates HDAC1 from the promoter. When overexpressed, induces apoptosis. The physiological significance of its role in apoptosis is unclear. Ref.1 Ref.6 Ref.7 Ref.8
Interacts with CIDEC By similarity. Directly interacts with CEBPB. Ref.8
Lipid droplet. Nucleus. Note: Enriched at lipid droplet contact sites. Using a GFP-tagged construct, has been shown to localize to mitonchondria, where it could interact with UCP1 and hence inhibit UCP1 uncoupling activity (Ref.5). These data could not be confirmed (Ref.8, Ref.6). Ref.5 Ref.6 Ref.7 Ref.8
Highly expressed in brown adipose tissue and, at lower levels, in white adipose tissue (at protein level). Expressed in mammary gland during pregnancy and lactation, in epithelial cells, but not in the surrounding adipose tissue. Secreted into milk via milk fat globules. Undetectable in undifferentiated preadipocytes. Ref.5 Ref.6 Ref.8
Expressed at 15 dpc in the interscapular region of the embryo, that could correspond to the developing brown adipose tissue. Expression continues in the interscapular region at 18 dpc and postnatally. In mammary glands, begins to be highly expressed at day 14.5 of pregnancy. Expression is maintained at high levels throughout lactation and declines during post-lactational involution. Ref.8
Up-regulated under conditions that enhance triacylglycerol deposition, including rosiglitazone treatment and high-fat diet. This up-regulation is mediated by PPARG. Ref.6
Mutant animals appear normal and fertile and produce the expected Mendelian ratio of heterozygous and homozygous descendents. They are lean and resistant to diet-induced obesity and diabetes. They exhibit higher metabolic rate, lipolysis in brown adipose tissue and core body temperature when subjected to cold treatment. Mutant females are unable to properly feed their pups who die within 3 days postpartum due to severely reduced milk lipids. Ref.5 Ref.8
Contains 1 CIDE-N domain.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 217||217||Cell death activator CIDE-A||PRO_0000144719|
|Domain||33 – 110||78||CIDE-N|
|Mutagenesis||23||1||K → A: Sustantial reduction in nuclear localization and loss of XDH induction; when associated with A-24. Ref.8|
|Mutagenesis||23||1||K → R: Increased nuclear localization. Ref.8|
|Mutagenesis||24||1||K → A: Sustantial reduction in nuclear localization and loss of XDH induction; when associated with A-23. Ref.8|
|Sequence conflict||165||1||S → R in AAC34985. Ref.1|
|||"CIDE, a novel family of cell death activators with homology to the 45 kDa subunit of the DNA fragmentation factor."|
Inohara N., Koseki T., Chen S., Wu X., Nunez G.
EMBO J. 17:2526-2533(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN APOPTOSIS.
|||"Lineage-specific biology revealed by a finished genome assembly of the mouse."|
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
|||Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.|
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
|||"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."|
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland.
|||"Cidea-deficient mice have lean phenotype and are resistant to obesity."|
Zhou Z., Yon Toh S., Chen Z., Guo K., Ng C.P., Ponniah S., Lin S.C., Hong W., Li P.
Nat. Genet. 35:49-56(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
|||"Cidea is associated with lipid droplets and insulin sensitivity in humans."|
Puri V., Ranjit S., Konda S., Nicoloro S.M., Straubhaar J., Chawla A., Chouinard M., Lin C., Burkart A., Corvera S., Perugini R.A., Czech M.P.
Proc. Natl. Acad. Sci. U.S.A. 105:7833-7838(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
|||"Fsp27 promotes lipid droplet growth by lipid exchange and transfer at lipid droplet contact sites."|
Gong J., Sun Z., Wu L., Xu W., Schieber N., Xu D., Shui G., Yang H., Parton R.G., Li P.
J. Cell Biol. 195:953-963(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
|||"Cidea is an essential transcriptional coactivator regulating mammary gland secretion of milk lipids."|
Wang W., Lv N., Zhang S., Shui G., Qian H., Zhang J., Chen Y., Ye J., Xie Y., Shen Y., Wenk M.R., Li P.
Nat. Med. 18:235-243(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A CEBPB COACTIVATOR, INTERACTION WITH CEBPB, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-23 AND LYS-24.
|+||Additional computationally mapped references.|
|AF041376 mRNA. Translation: AAC34985.1.|
AC154125 Genomic DNA. No translation available.
CH466528 Genomic DNA. Translation: EDL09649.1.
CH466528 Genomic DNA. Translation: EDL09650.1.
BC096649 mRNA. Translation: AAH96649.1.
|RefSeq||NP_031728.2. NM_007702.2. |
3D structure databases
|SMR||O70302. Positions 33-110. |
Protein-protein interaction databases
Protocols and materials databases
Genome annotation databases
|Ensembl||ENSMUST00000025404; ENSMUSP00000025404; ENSMUSG00000024526. |
|MGI||MGI:1270845. Cidea. |
Gene expression databases
|GermOnline||ENSMUSG00000024526. Mus musculus. |
Family and domain databases
|InterPro||IPR003508. CAD. |
|Pfam||PF02017. CIDE-N. 1 hit. |
|SMART||SM00266. CAD. 1 hit. |
|PROSITE||PS51135. CIDE_N. 1 hit. |
|Accession||Primary (citable) accession number: O70302|
Secondary accession number(s): Q4V9X2
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|