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Protein

Cell death activator CIDE-A

Gene

Cidea

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 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.4 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell death Source: BHF-UCL
  • lipid metabolic process Source: MGI
  • lipid storage Source: BHF-UCL
  • negative regulation of cytokine secretion Source: MGI
  • negative regulation of execution phase of apoptosis Source: BHF-UCL
  • negative regulation of lipid catabolic process Source: BHF-UCL
  • negative regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  • negative regulation of tumor necrosis factor production Source: MGI
  • positive regulation of sequestering of triglyceride Source: BHF-UCL
  • regulation of apoptotic DNA fragmentation Source: BHF-UCL
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • response to stilbenoid Source: UniProtKB
  • temperature homeostasis Source: BHF-UCL
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-73923. Lipid digestion, mobilization, and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell death activator CIDE-A
Alternative name(s):
Cell death-inducing DFFA-like effector A
Gene namesi
Name:Cidea
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1270845. Cidea.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • lipid particle Source: UniProtKB-SubCell
  • mitochondrial envelope Source: MGI
  • mitochondrion Source: MGI
  • nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Lipid droplet, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23K → A: Sustantial reduction in nuclear localization and loss of XDH induction; when associated with A-24. 1 Publication1
Mutagenesisi23K → R: Increased nuclear localization. 1 Publication1
Mutagenesisi24K → A: Sustantial reduction in nuclear localization and loss of XDH induction; when associated with A-23. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001447191 – 217Cell death activator CIDE-AAdd BLAST217

Proteomic databases

PaxDbiO70302.
PRIDEiO70302.

Expressioni

Tissue specificityi

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.3 Publications

Developmental stagei

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.1 Publication

Inductioni

Up-regulated under conditions that enhance triacylglycerol deposition, including rosiglitazone treatment and high-fat diet. This up-regulation is mediated by PPARG.1 Publication

Gene expression databases

BgeeiENSMUSG00000024526.
GenevisibleiO70302. MM.

Interactioni

Subunit structurei

Interacts with CIDEC (By similarity). Directly interacts with CEBPB.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PRKAB1Q9Y4784EBI-7927848,EBI-719769From a different organism.

GO - Molecular functioni

  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi198712. 3 interactors.
IntActiO70302. 7 interactors.
STRINGi10090.ENSMUSP00000025404.

Structurei

3D structure databases

ProteinModelPortaliO70302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 110CIDE-NPROSITE-ProRule annotationAdd BLAST78

Sequence similaritiesi

Contains 1 CIDE-N domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IVIC. Eukaryota.
ENOG4111SUV. LUCA.
GeneTreeiENSGT00390000018596.
HOGENOMiHOG000029211.
HOVERGENiHBG050961.
InParanoidiO70302.
OMAiAQITGQF.
OrthoDBiEOG091G0H6W.
TreeFamiTF334321.

Family and domain databases

InterProiIPR032936. CIDE-A.
IPR003508. CIDE-N_dom.
[Graphical view]
PANTHERiPTHR12306:SF8. PTHR12306:SF8. 1 hit.
PfamiPF02017. CIDE-N. 1 hit.
[Graphical view]
SMARTiSM00266. CAD. 1 hit.
[Graphical view]
PROSITEiPS51135. CIDE_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O70302-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METARDYAGA LIRPLTFMGL QTKKVLLTPL IHPARPFRVS NHDRSSRRGV
60 70 80 90 100
MASSLQELIS KTLDVLVITT GLVTLVLEED GTVVDTEEFF QTLRDNTHFM
110 120 130 140 150
ILEKGQKWTP GSKYVPVCKQ PKKSGIARVT FDLYRLNPKD FLGCLNVKAT
160 170 180 190 200
MYEMYSVSYD IRCTSFKAVL RNLLRFMSYA AQMTGQFLVY AGTYMLRVLG
210
DTEEQPSPKP STKGWFM
Length:217
Mass (Da):24,669
Last modified:October 3, 2012 - v2
Checksum:iC9E406895CFD4CBA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti165S → R in AAC34985 (PubMed:9564035).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS37846.1.
RefSeqiNP_031728.2. NM_007702.2.
UniGeneiMm.449.

Genome annotation databases

EnsembliENSMUST00000025404; ENSMUSP00000025404; ENSMUSG00000024526.
GeneIDi12683.
KEGGimmu:12683.
UCSCiuc012beh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS37846.1.
RefSeqiNP_031728.2. NM_007702.2.
UniGeneiMm.449.

3D structure databases

ProteinModelPortaliO70302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198712. 3 interactors.
IntActiO70302. 7 interactors.
STRINGi10090.ENSMUSP00000025404.

Proteomic databases

PaxDbiO70302.
PRIDEiO70302.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025404; ENSMUSP00000025404; ENSMUSG00000024526.
GeneIDi12683.
KEGGimmu:12683.
UCSCiuc012beh.1. mouse.

Organism-specific databases

CTDi1149.
MGIiMGI:1270845. Cidea.

Phylogenomic databases

eggNOGiENOG410IVIC. Eukaryota.
ENOG4111SUV. LUCA.
GeneTreeiENSGT00390000018596.
HOGENOMiHOG000029211.
HOVERGENiHBG050961.
InParanoidiO70302.
OMAiAQITGQF.
OrthoDBiEOG091G0H6W.
TreeFamiTF334321.

Enzyme and pathway databases

ReactomeiR-MMU-73923. Lipid digestion, mobilization, and transport.

Miscellaneous databases

PROiO70302.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024526.
GenevisibleiO70302. MM.

Family and domain databases

InterProiIPR032936. CIDE-A.
IPR003508. CIDE-N_dom.
[Graphical view]
PANTHERiPTHR12306:SF8. PTHR12306:SF8. 1 hit.
PfamiPF02017. CIDE-N. 1 hit.
[Graphical view]
SMARTiSM00266. CAD. 1 hit.
[Graphical view]
PROSITEiPS51135. CIDE_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCIDEA_MOUSE
AccessioniPrimary (citable) accession number: O70302
Secondary accession number(s): Q4V9X2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 3, 2012
Last modified: November 2, 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.