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Annotation rule MF_03201 |
Accession | MF_03201 |
Dates | 16-DEC-2013 (Created) 20-NOV-2019 (Last updated, Version 13) |
Name | VLCF_elongase_1 |
Scope | Eukaryota; Vertebrata |
Templates | Q9BW60 (ELOV1_HUMAN); Q9JLJ5 (ELOV1_MOUSE): [Recover all] |
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Function | Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. 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 C18 to C26 acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. May participate to 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. Indirectly inhibits @gn(RPE65) via production of VLCFAs. |
Function | Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. 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 C18 to C26 acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. May participate to 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. |
Catalytic activity | RHEA:32727: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC 2.3.1.199 |
Subunit | Interacts with @gn(LASS2), @gn(TECR) and @gn(HSD17B12). |
Pathway | Lipid metabolism; fatty acid biosynthesis. |
Subcellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein. |
Domain | The C-terminal di-lysine motif may confer endoplasmic reticulum localization. |
Similarity | Belongs to the ELO family. ELOVL1 subfamily. |
General | Transmembrane; -; 7; trigger=yes; |
From: ELOV1_HUMAN (Q9BW60) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
MOTIF | Cter-4 | Cter | Di-lysine motif | ERmotif | K-x-K-x(2)> |