ELOVL1
Domain
The C-terminal di-lysine motif may confer endoplasmic reticulum localization.
Function
Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle (PubMed:29496980, PubMed:30487246). This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that exhibits activity toward saturated and monounsaturated acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. May participate in the production of both saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. Important for saturated C24:0 and monounsaturated C24:1 sphingolipid synthesis (PubMed:20937905). Indirectly inhibits RPE65 via production of VLCFAs.
Involvement in disease
Ichthyotic keratoderma, spasticity, hypomyelination, and dysmorphic facies
IKSHD
An autosomal dominant disease characterized by ichthyosis due to epidermal hyperproliferation and increased keratinisation, hypomyelination of the central white matter, spastic paraplegia, central nystagmus, optic atrophy, reduction of peripheral vision and visual acuity, and dysmorphic facial features.
None
The disease is caused by variants affecting the gene represented in this entry.
Pathway
Lipid metabolism; fatty acid biosynthesis.
Sequence Similarities
Belongs to the ELO family. ELOVL1 subfamily.
Tissue Specificity
Ubiquitous.
Cellular localization
- Endoplasmic reticulum membrane
- Multi-pass membrane protein
Alternative names
SSC1, CGI-88, ELOVL1, Very long chain fatty acid elongase 1, 3-keto acyl-CoA synthase ELOVL1, ELOVL fatty acid elongase 1, Elongation of very long chain fatty acids protein 1, Very long chain 3-ketoacyl-CoA synthase 1, Very long chain 3-oxoacyl-CoA synthase 1, ELOVL FA elongase 1