Q9UHD4 · CIDEB_HUMAN
- ProteinLipid transferase CIDEB
- GeneCIDEB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids219 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Lipid transferase specifically expressed in hepatocytes, which promotes unilocular lipid droplet formation by mediating lipid droplet fusion (PubMed:35939579).
Lipid droplet fusion promotes their enlargement, restricting lipolysis and favoring lipid storage (PubMed:35939579).
Localizes on the lipid droplet surface, at focal contact sites between lipid droplets, and mediates atypical lipid droplet fusion by 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).
Promotes lipid exchange and lipid droplet fusion in both small and large lipid droplet-containing hepatocytes (By similarity).
In addition to its role in lipid droplet fusion, also involved in cytoplasmic vesicle biogenesis and transport (By similarity).
Required for very-low-density lipoprotein (VLDL) lipidation and maturation (By similarity).
Probably involved in the biogenesis of VLDL transport vesicles by forming a COPII vesicle coat and facilitating the formation of endoplasmic reticulum-derived large vesicles (By similarity).
Also involved in sterol-regulated export of the SCAP-SREBP complex, composed of SCAP, SREBF1/SREBP1 and SREBF2/SREBP2, by promoting loading of SCAP-SREBP into COPII vesicles (By similarity).
May also activate apoptosis (PubMed:10619428).
Lipid droplet fusion promotes their enlargement, restricting lipolysis and favoring lipid storage (PubMed:35939579).
Localizes on the lipid droplet surface, at focal contact sites between lipid droplets, and mediates atypical lipid droplet fusion by 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).
Promotes lipid exchange and lipid droplet fusion in both small and large lipid droplet-containing hepatocytes (By similarity).
In addition to its role in lipid droplet fusion, also involved in cytoplasmic vesicle biogenesis and transport (By similarity).
Required for very-low-density lipoprotein (VLDL) lipidation and maturation (By similarity).
Probably involved in the biogenesis of VLDL transport vesicles by forming a COPII vesicle coat and facilitating the formation of endoplasmic reticulum-derived large vesicles (By similarity).
Also involved in sterol-regulated export of the SCAP-SREBP complex, composed of SCAP, SREBF1/SREBP1 and SREBF2/SREBP2, by promoting loading of SCAP-SREBP into COPII vesicles (By similarity).
May also activate apoptosis (PubMed:10619428).
(Microbial infection) Involved in Hepatatis C virus (HCV) assembly and required for HCV entry into hepatocytes.
GO annotations
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLipid transferase CIDEB
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9UHD4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Peripheral membrane protein
Note: Enriched at lipid droplet contact sites.
Keywords
- Cellular component
Disease & Variants
Variants
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The viewer provides 459 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000144720 | 1-219 | Lipid transferase CIDEB | |||
Sequence: MEYLSALNPSDLLRSVSNISSEFGRRVWTSAPPPQRPFRVCDHKRTIRKGLTAATRQELLAKALETLLLNGVLTLVLEEDGTAVDSEDFFQLLEDDTCLMVLQSGQSWSPTRSGVLSYGLGRERPKHSKDIARFTFDVYKQNPRDLFGSLNVKATFYGLYSMSCDFQGLGPKKVLRELLRWTSTLLQGLGHMLLGISSTLRHAVEGAEQWQQKGRLHSY |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in liver and small intestine and, at lower levels, in colon, kidney and spleen.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with DFFA (PubMed:10619428).
Interacts with DFFB; inhibited by DFFB (PubMed:10619428).
Interacts with APOB. Interacts with PREB/SEC12; facilitating loading of SCAP-SREBP into COPII vesicles (By similarity).
Interacts with DFFB; inhibited by DFFB (PubMed:10619428).
Interacts with APOB. Interacts with PREB/SEC12; facilitating loading of SCAP-SREBP into COPII vesicles (By similarity).
(Microbial infection) Interacts (via N-terminus) with HCV non-structural protein 5A (via N-terminus); this interaction seems to regulate the association of HCV particles with ApoE.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 34-110 | CIDE-N | ||||
Sequence: PQRPFRVCDHKRTIRKGLTAATRQELLAKALETLLLNGVLTLVLEEDGTAVDSEDFFQLLEDDTCLMVLQSGQSWSP |
Sequence similarities
Belongs to the CIDE family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length219
- Mass (Da)24,678
- Last updated2002-03-27 v2
- ChecksumE0B4E5EF1F7C912D
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
G3V4E2 | G3V4E2_HUMAN | CIDEB | 61 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 120 | in Ref. 1; AAF23324 | ||||
Sequence: L → P | ||||||
Sequence conflict | 124 | in Ref. 1; AAF23324 | ||||
Sequence: R → S | ||||||
Sequence conflict | 132 | in Ref. 1; AAF23324 | ||||
Sequence: A → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF190901 EMBL· GenBank· DDBJ | AAF23324.1 EMBL· GenBank· DDBJ | mRNA | ||
AF218586 EMBL· GenBank· DDBJ | AAF27658.1 EMBL· GenBank· DDBJ | mRNA | ||
AF544398 EMBL· GenBank· DDBJ | AAN37907.1 EMBL· GenBank· DDBJ | mRNA | ||
AK000387 EMBL· GenBank· DDBJ | BAA91132.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471078 EMBL· GenBank· DDBJ | EAW66031.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471078 EMBL· GenBank· DDBJ | EAW66032.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471078 EMBL· GenBank· DDBJ | EAW66033.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC035970 EMBL· GenBank· DDBJ | AAH35970.1 EMBL· GenBank· DDBJ | mRNA |