Elongation of very long chain fatty acids protein 1 (ELOVL1) is a component of the the long-chain fatty acids elongation cycle. It is a transmembrane enzyme in the endoplasmic reticulum that adds two carbons per cycle to long- and very long-chain fatty acids with a preference for condensing saturated C18 to C26 acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA [].
This entry represents a conserved site found in the ELO (Elongation of fatty acids protein) family members, such as:Mammalian proteins ELOVL1 (Elongation of very long chain fatty acids protein 1) to ELOVL4 []. These proteins all seem to beinvolved in the synthesis of very long chain fatty acids.Yeast ELO1, ELO2 and ELO3 []. They seem to be components of membrane-boundfatty acid elongation systems.Caenorhabditis elegans hypothetical protein C40H1.4.Caenorhabditis elegans hypothetical protein D2024.3.The proteins have from 271 to 435 amino acid residues. Structurally, they seemto be formed of three sections: a N-terminal region with two transmembranedomains, a central hydrophilic loop and a C-terminal region that contains fromone to three transmembrane domains. This entry represents aconserved region that contains three histidines. This region is located in thehydrophilic loop.
The ELO family consist of eukaryotic integral membrane proteins involved in fatty acid elongation. This family consist of:Mammalian proteins ELOVL1 to ELOVL7 [, ]. These proteins catalyse the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle, each of them has a specific substrate specificity and physiological functions.Yeast ELO1, ELO2 and ELO3 [, ]. They are components of a microsomal membrane-bound long-chain fatty acid elongation system.Caenorhabditis elegans hypothetical protein C40H1.4.Caenorhabditis elegans hypothetical protein D2024.3.This group of eukaryotic integral membrane proteinsare evolutionary related and have from 290 to 435 amino acid residues. Structurally, they seem to be formed of three sections: a N-terminal region with two transmembrane domains, a central hydrophilic loop and a C-terminal region that contains from one to three transmembrane domains. Members of this family are involved in long chain fatty acid elongation systems that produce the 26-carbon precursors for ceramide and sphingolipid synthesis []. Yeast ELO3 () affects plasma membrane H+-ATPase activity, and may act on a glucose-signalling pathway that controls the expression of several genes that are transcriptionally regulated by glucose such as PMA1 []. It plays an important role in lipotoxic cell death induced by oleic acid through maintaining a balanced fatty acid composition in the plasma membrane []. Mammalian ELOVLs are also associated with known pathologies. ELOVL1 catalyses elongation of saturated and monounsaturated C22-C26-VLCFAs, and dominant mutations cause ichthyosis, hypomyelination of the central white matter that leads to spastic paraplegia and central nystagmus and optic atrophy [], dominant ELOVL4 mutations cause a juvenile macular dystrophy (Stargardt disease-3) and Elovl4 knockout mice die soon after birth due to a deficiency in skin barrier formation. Studies in Elovl6-null mice have revealed that ELOVL6 is involved in an obesity-induced insulin resistance and ELOVL7 is involved in prostate cancer growth [].
