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Protein

Cell death activator CIDE-3

Gene

Cidec

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1. May act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment. As mature adipocytes, that express high CIDEC levels, are quite resistant to apoptotic stimuli, the physiological significance of its role in apoptosis is unclear. May play a role in the modulation of the response to osmotic stress by preventing NFAT5 to translocate into the nucleus and activate its target genes expression.4 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Chemistry

SwissLipidsiSLP:000000723.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell death activator CIDE-3
Alternative name(s):
Cell death-inducing DFFA-like effector protein C
Fat-specific protein FSP27
Gene namesi
Name:Cidec
Synonyms:Fsp27
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:95585. Cidec.

Subcellular locationi

  • Lipid droplet
  • Endoplasmic reticulum
  • Nucleus

  • Note: Diffuses quickly on lipid droplet surface, but becomes trapped and clustered at lipid droplet contact sites, thereby enabling its rapid enrichment at lipid droplet contact sites.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Lipid droplet, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mutant animals are born in a Mendelian ratio and appear physically normal at birth. The body weights of wild-type and mutant mice fed a standard diet do not differ up to 14 weeks of age, nor does food intake. From 16 weeks of age, the body weight of mutant mice significantly decreases compared with that of wild-type mice. When animals are fed a high-fat diet, the gain in body weight is significantly smaller for mutant mice than for wild-type. Under these feeding conditions, mutant mice are also protected from insulin resistance and from accumulation of fat in the liver. The body temperature do not differ significantly between mutant and wild-type mice maintained at room temperature, but the basal rate of oxygen consumption is significantly increased in mutants.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461R → E: Abolishes CIDE-N/CIDE-N interaction between the 2 homodimer subunits. 1 Publication
Mutagenesisi53 – 531K → A: Slightly inhibits interaction with PLIN1. 1 Publication
Mutagenesisi55 – 551R → E: Abolishes CIDE-N/CIDE-N interaction between the 2 homodimer subunits. 1 Publication
Mutagenesisi75 – 751K → A: Inhibits interaction with PLIN1; when associated with A-77. 1 Publication
Mutagenesisi77 – 771K → A: Inhibits interaction with PLIN1; when associated with A-75. 1 Publication
Mutagenesisi86 – 883EED → QQN: Abolishes CIDE-N/CIDE-N interaction between the 2 homodimer subunits and inhibits lipid droplet enlargement. No effect on homodimerization. 1 Publication
Mutagenesisi87 – 882ED → QN: Reduces CIDE-N/CIDE-N interaction between the 2 homodimer subunits and inhibits lipid droplet enlargement. 1 Publication
Mutagenesisi112 – 1121K → A: Slightly inhibits interaction with PLIN1; when associated with A-115. 1 Publication
Mutagenesisi115 – 1151K → A: Slightly inhibits interaction with PLIN1; when associated with A-112 or A-117. 1 Publication
Mutagenesisi117 – 1171K → A: Slightly inhibits interaction with PLIN1; when associated with A-115. 1 Publication
Mutagenesisi182 – 1821K → A: Abolishes lipid droplet enlargement activity, but not localization to lipid droplets, nor enrichement at contact sites; when associated with A-186 and A-190. 1 Publication
Mutagenesisi186 – 1861K → A: Abolishes lipid droplet enlargement activity, but not localization to lipid droplets, nor enrichement at contact sites; when associated with A-182 and A-190. 1 Publication
Mutagenesisi190 – 1901R → A: Abolishes lipid droplet enlargement activity, but not localization to lipid droplets, nor enrichement at contact sites; when associated with A-182 and A-186. 1 Publication
Mutagenesisi224 – 2241K → A: No effect on protein stability; when associated with A-226. Drastically increased protein stability and decreased ubiquitination; when associated with A-226 and A-236. 1 Publication
Mutagenesisi226 – 2261K → A: No effect on protein stability; when associated with A-226. Drastically increased protein stability and decreased ubiquitination; when associated with A-224 and A-236. 1 Publication
Mutagenesisi236 – 2361K → A: No effect on protein stability. Drastically increased protein stability and decreased ubiquitination; when associated with A-224 and A-226. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 239239Cell death activator CIDE-3PRO_0000144723Add
BLAST

Post-translational modificationi

Ubiquitinated and targeted to proteasomal degradation, resulting in a short half-life (about 15 minutes in 3T3-L1 cells). Protein stability depends on triaclyglycerol synthesis, fatty acid availability and lipid droplet formation.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiP56198.
PRIDEiP56198.

PTM databases

iPTMnetiP56198.
PhosphoSiteiP56198.

Expressioni

Tissue specificityi

Expressed almost exclusively in adipose tissue, including subcutaneous and epididymal white adipose tissue (at protein level). Although abundantly present in brown adipose tissue at the mRNA level, the protein is almost undetectable in this tissue (PubMed:18654663), or at moderate levels (PubMed:22245780, PubMed:12910269). Expressed in the mammary gland, in stromal adipose tissue, but becomes undetectable at the end of pregnancy and during lactation (at protein level). Expressed at low levels in skeletal muscle and heart.5 Publications

Developmental stagei

Up-regulated during differentiation into adipocytes in various cell lines, including TA1 and 3T3-L1. Decreases in the mammary gland during pregnancy from day 14.5 until 18.5, when it becomes hardly detectable, and during lactation.4 Publications

Inductioni

Up-regulated under conditions that enhance triacylglycerol deposition, including rosiglitazone treatment and high-fat diet. This up-regulation is mediated by PPARG. Up-regulated by isoproterenol, a beta-agonist, and oleic acid treatment. This induction is due to protein stabilization. Down-regulated upon hypertonic conditions.3 Publications

Gene expression databases

CleanExiMM_CIDEC.
ExpressionAtlasiP56198. baseline and differential.
GenevisibleiP56198. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with CIDEA. Interacts with NFAT5; this interaction is direct and retains NFAT5 in the cytoplasm (By similarity). Interacts with CEBPB. Interacts with PLIN1.By similarity2 Publications

Protein-protein interaction databases

BioGridi199749. 1 interaction.
IntActiP56198. 1 interaction.
MINTiMINT-6768962.
STRINGi10090.ENSMUSP00000032416.

Structurei

Secondary structure

1
239
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 485Combined sources
Beta strandi55 – 595Combined sources
Helixi63 – 7311Combined sources
Beta strandi82 – 854Combined sources
Turni86 – 883Combined sources
Helixi95 – 1006Combined sources
Beta strandi106 – 1105Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IKGX-ray1.93A39-118[»]
4MACX-ray2.00A/B32-120[»]
ProteinModelPortaliP56198.
SMRiP56198. Positions 5-119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 11878CIDE-NPROSITE-ProRule annotationAdd
BLAST

Domaini

The CIDE-N domain is involved in homodimerization which is crucial for its function in promoting lipid exchange and transfer.1 Publication

Sequence similaritiesi

Contains 1 CIDE-N domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IWQS. Eukaryota.
ENOG4111HCT. LUCA.
GeneTreeiENSGT00390000018596.
HOGENOMiHOG000029211.
HOVERGENiHBG050961.
InParanoidiP56198.
OrthoDBiEOG7C2R2P.
TreeFamiTF334321.

Family and domain databases

InterProiIPR003508. CIDE-N_dom.
[Graphical view]
PfamiPF02017. CIDE-N. 1 hit.
[Graphical view]
SMARTiSM00266. CAD. 1 hit.
[Graphical view]
PROSITEiPS51135. CIDE_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56198-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYAMKSLSL LYPRSLSRHV AVSTAVVTQQ LVSKPSRETP RARPCRVSTA
60 70 80 90 100
DRKVRKGIMA HSLEDLLNKV QDILKLKDKP FSLVLEEDGT IVETEEYFQA
110 120 130 140 150
LAKDTMFMVL LKGQKWKPPS EQRKKRAQLA LSQKPTKKID VARVTFDLYK
160 170 180 190 200
LNPQDFIGCL NVKATLYDTY SLSYDLHCYK AKRIVKEMLR WTLFSMQATG
210 220 230
HMLLGTSSYM QQFLDATEEE QPAKAKPSSL LPACLKMLQ
Length:239
Mass (Da):27,324
Last modified:October 3, 2012 - v2
Checksum:i7F4E6C5D2E24A161
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1892ML → IV in M61737 (PubMed:1339452).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61737 mRNA. No translation available.
AK080133 mRNA. Translation: BAC37830.1.
AC153910 Genomic DNA. No translation available.
BC099676 mRNA. Translation: AAH99676.1.
CCDSiCCDS20418.1.
PIRiA42445.
RefSeqiNP_001288224.1. NM_001301295.1.
NP_848460.1. NM_178373.3.
UniGeneiMm.10026.

Genome annotation databases

EnsembliENSMUST00000032416; ENSMUSP00000032416; ENSMUSG00000030278.
ENSMUST00000113089; ENSMUSP00000108712; ENSMUSG00000030278.
GeneIDi14311.
KEGGimmu:14311.
UCSCiuc009dgb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61737 mRNA. No translation available.
AK080133 mRNA. Translation: BAC37830.1.
AC153910 Genomic DNA. No translation available.
BC099676 mRNA. Translation: AAH99676.1.
CCDSiCCDS20418.1.
PIRiA42445.
RefSeqiNP_001288224.1. NM_001301295.1.
NP_848460.1. NM_178373.3.
UniGeneiMm.10026.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IKGX-ray1.93A39-118[»]
4MACX-ray2.00A/B32-120[»]
ProteinModelPortaliP56198.
SMRiP56198. Positions 5-119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199749. 1 interaction.
IntActiP56198. 1 interaction.
MINTiMINT-6768962.
STRINGi10090.ENSMUSP00000032416.

Chemistry

SwissLipidsiSLP:000000723.

PTM databases

iPTMnetiP56198.
PhosphoSiteiP56198.

Proteomic databases

PaxDbiP56198.
PRIDEiP56198.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032416; ENSMUSP00000032416; ENSMUSG00000030278.
ENSMUST00000113089; ENSMUSP00000108712; ENSMUSG00000030278.
GeneIDi14311.
KEGGimmu:14311.
UCSCiuc009dgb.2. mouse.

Organism-specific databases

CTDi63924.
MGIiMGI:95585. Cidec.

Phylogenomic databases

eggNOGiENOG410IWQS. Eukaryota.
ENOG4111HCT. LUCA.
GeneTreeiENSGT00390000018596.
HOGENOMiHOG000029211.
HOVERGENiHBG050961.
InParanoidiP56198.
OrthoDBiEOG7C2R2P.
TreeFamiTF334321.

Miscellaneous databases

NextBioi285735.
PROiP56198.
SOURCEiSearch...

Gene expression databases

CleanExiMM_CIDEC.
ExpressionAtlasiP56198. baseline and differential.
GenevisibleiP56198. MM.

Family and domain databases

InterProiIPR003508. CIDE-N_dom.
[Graphical view]
PfamiPF02017. CIDE-N. 1 hit.
[Graphical view]
SMARTiSM00266. CAD. 1 hit.
[Graphical view]
PROSITEiPS51135. CIDE_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and transcriptional regulation of a novel adipocyte-specific gene, FSP27. CAAT-enhancer-binding protein (C/EBP) and C/EBP-like proteins interact with sequences required for differentiation-dependent expression."
    Danesch U., Hoeck W., Ringold G.M.
    J. Biol. Chem. 267:7185-7193(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  2. "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.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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].
    Strain: FVB/N.
    Tissue: Kidney.
  5. "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: TISSUE SPECIFICITY.
  6. Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  7. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  8. Cited for: INDUCTION.
  9. "Fat-specific protein 27 undergoes ubiquitin-dependent degradation regulated by triacylglycerol synthesis and lipid droplet formation."
    Nian Z., Sun Z., Yu L., Toh S.Y., Sang J., Li P.
    J. Biol. Chem. 285:9604-9615(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, UBIQUITINATION, INDUCTION, MUTAGENESIS OF LYS-224; LYS-226 AND LYS-236.
  10. "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, MUTAGENESIS OF LYS-182; LYS-186 AND ARG-190.
  11. "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.
  12. "Perilipin1 promotes unilocular lipid droplet formation through the activation of Fsp27 in adipocytes."
    Sun Z., Gong J., Wu H., Xu W., Wu L., Xu D., Gao J., Wu J.W., Yang H., Yang M., Li P.
    Nat. Commun. 4:1594-1594(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UNILOCULAR LIPID DROPLET FORMATION, SUBUNIT, INTERACTION WITH PLIN1, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-46; LYS-53; ARG-55; LYS-75; LYS-77; 86-GLU--ASP-88; 87-GLU-ASP-88; LYS-112; LYS-115 AND LYS-117.
  13. "Fat-specific protein 27 modulates nuclear factor of activated T cells 5 and the cellular response to stress."
    Ueno M., Shen W.J., Patel S., Greenberg A.S., Azhar S., Kraemer F.B.
    J. Lipid Res. 54:734-743(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION BY OSMOTIC STRESS.

Entry informationi

Entry nameiCIDEC_MOUSE
AccessioniPrimary (citable) accession number: P56198
Secondary accession number(s): Q499X5, Q8BNV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 3, 2012
Last modified: May 11, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.