UniProt ID: Q6P978 |
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 specifically elongates C24:0 and C26:0 acyl-CoAs. May participate to the production of saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. {ECO:0000256|HAMAP-Rule:MF_03204}. CATALYTIC ACTIVITY: Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long- chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736; EC=2.3.1.199; Evidence={ECO:0000256|HAMAP-Rule:MF_03204, ECO:0000256|RuleBase:RU361115}; PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP- Rule:MF_03204}. SUBUNIT: Oligomer. {ECO:0000256|HAMAP-Rule:MF_03204}. SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03204}; Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03204}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. DOMAIN: The C-terminal di-lysine motif may confer endoplasmic reticulum localization. {ECO:0000256|HAMAP-Rule:MF_03204}. SIMILARITY: Belongs to the ELO family. ELOVL4 subfamily. {ECO:0000256|HAMAP-Rule:MF_03204}. |
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