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Annotation rule MF_03202 |
Accession | MF_03202 |
Dates | 16-DEC-2013 (Created) 20-NOV-2019 (Last updated, Version 11) |
Name | VLCF_elongase_2 |
Scope | Eukaryota; Vertebrata |
Templates | Q9NXB9 (ELOV2_HUMAN); Q9JLJ4 (ELOV2_MOUSE); D4A612 (ELOV2_RAT): [Recover all] |
Triggered by |
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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. Acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C20:4(n-6) acyl-CoA. Condensing enzyme that catalyzes the synthesis of polyunsaturated very long chain fatty acid (C20- and C22-PUFA). May participate to the production of polyunsaturated 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 |
Pathway | Lipid metabolism; polyunsaturated 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. ELOVL2 subfamily. |
General | Transmembrane; -; 7; trigger=yes; |
From: ELOV2_HUMAN (Q9NXB9) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
MOTIF | Cter-3 | Cter | Di-lysine motif | ERmotif | K-K-x(2)> |
Size range | 257-343 amino acids |
Related rules | MF_03205 (ELOV5) |
Fusion | None |