Q5XI33 · CIDEC_RAT
- ProteinLipid transferase CIDEC
- GeneCidec
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids238 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Lipid transferase specifically expressed in white adipose tissue, which promotes unilocular lipid droplet formation by mediating lipid droplet fusion (By similarity).
Lipid droplet fusion promotes their enlargement, restricting lipolysis and favoring lipid storage (By similarity).
Localizes on the lipid droplet surface, at focal contact sites between lipid droplets, and mediates atypical lipid droplet fusion by undergoing liquid-liquid phase separation (LLPS) and promoting directional net neutral lipid transfer from the smaller to larger lipid droplets (By similarity).
The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair (By similarity).
Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1 (By similarity).
May also 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 (PubMed:23233732).
When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment (By similarity).
Lipid droplet fusion promotes their enlargement, restricting lipolysis and favoring lipid storage (By similarity).
Localizes on the lipid droplet surface, at focal contact sites between lipid droplets, and mediates atypical lipid droplet fusion by undergoing liquid-liquid phase separation (LLPS) and promoting directional net neutral lipid transfer from the smaller to larger lipid droplets (By similarity).
The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair (By similarity).
Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1 (By similarity).
May also 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 (PubMed:23233732).
When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment (By similarity).
Catalytic activity
- a triacyl-sn-glycerol(in) = a triacyl-sn-glycerol(out)
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | lipid droplet | |
Cellular Component | nucleus | |
Molecular Function | lipid transfer activity | |
Molecular Function | molecular condensate scaffold activity | |
Molecular Function | phosphatidic acid binding | |
Molecular Function | phosphatidylinositol binding | |
Molecular Function | phosphatidylserine binding | |
Biological Process | apoptotic process | |
Biological Process | execution phase of apoptosis | |
Biological Process | lipid droplet fusion | |
Biological Process | lipid droplet organization | |
Biological Process | lipid storage | |
Biological Process | negative regulation of lipid catabolic process | |
Biological Process | negative regulation of triglyceride metabolic process | |
Biological Process | regulation of apoptotic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLipid transferase CIDEC
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ5XI33
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000419721 | 1-238 | Lipid transferase CIDEC | |||
Sequence: MDYAMKSLSLLYPRSLSRHVAVSTAVVTQQLVSEPSRETPRARPCRVSTADRKVRKGIMAHSLEDLLGKVQDILKLKDKPFSLVLEEDGTIVETEEYFQALPRDTVFMVLQKGQKWKSPSEQRKKKAQLSLSQKPTKKIDVARVTFDLYKLNPQDFIGCLNVKATLYDTYSLSYDLHCYRAKRIVKEMLRWTLFSMQATGHMLLGTSSYMQQFLDATEEEQPSKAKASLLPACLKMLQ |
Post-translational modification
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.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Homodimer (By similarity).
Interacts with CIDEA (By similarity).
Homooligomer; undergoes liquid-liquid phase separation (LLPS) via its N-terminus, facilitating lipid droplet fusion, occurs at the lipid droplet contact sites (By similarity).
Interacts with PLIN1 (By similarity).
Interacts with NFAT5; this interaction is direct and retains NFAT5 in the cytoplasm (PubMed:23233732).
Interacts with CEBPB (By similarity).
Interacts with isoform CLSTN3beta of CLSTN3; inhibiting the lipid transferase activity of CIDEC (By similarity).
Interacts with CIDEA (By similarity).
Homooligomer; undergoes liquid-liquid phase separation (LLPS) via its N-terminus, facilitating lipid droplet fusion, occurs at the lipid droplet contact sites (By similarity).
Interacts with PLIN1 (By similarity).
Interacts with NFAT5; this interaction is direct and retains NFAT5 in the cytoplasm (PubMed:23233732).
Interacts with CEBPB (By similarity).
Interacts with isoform CLSTN3beta of CLSTN3; inhibiting the lipid transferase activity of CIDEC (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-35 | Required for liquid-liquid phase separation (LLPS) | ||||
Sequence: MDYAMKSLSLLYPRSLSRHVAVSTAVVTQQLVSEP | ||||||
Domain | 41-118 | CIDE-N | ||||
Sequence: RARPCRVSTADRKVRKGIMAHSLEDLLGKVQDILKLKDKPFSLVLEEDGTIVETEEYFQALPRDTVFMVLQKGQKWKS |
Domain
The CIDE-N domain is involved in homodimerization which is crucial for its function in promoting lipid exchange and transfer.
Sequence similarities
Belongs to the CIDE family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length238
- Mass (Da)27,214
- Last updated2004-11-23 v1
- ChecksumE6489A38F1CA5277
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0G2K551 | A0A0G2K551_RAT | Cidec | 248 | ||
A0A8I6AQV9 | A0A8I6AQV9_RAT | Cidec | 261 | ||
A0A8I6A975 | A0A8I6A975_RAT | Cidec | 254 | ||
A0A8I6GGI9 | A0A8I6GGI9_RAT | Cidec | 239 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC083860 EMBL· GenBank· DDBJ | AAH83860.1 EMBL· GenBank· DDBJ | mRNA |