HAMAP rule MF_03201
General rule information
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Accession | MF_03201 |
Dates | 16-DEC-2013 (Created)
29-SEP-2022 (Last updated, Version 14) |
Name | VLCF_elongase_1 |
Scope(s) |
Eukaryota Vertebrata |
Template(s) | Q9BW60 (ELOV1_HUMAN); Q9JLJ5 (ELOV1_MOUSE); [ Recover all ] |
Triggered by |
HAMAP; MF_03201 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | ELOV1 |
Protein name | RecName: Full=Elongation of very long chain fatty acids protein 1; EC=2.3.1.199; AltName: Full=3-keto acyl-CoA synthase AltName: Full=ELOVL fatty acid elongase 1; Short=ELOVL FA elongase 1; AltName: Full=Very long chain 3-ketoacyl-CoA synthase 1; AltName: Full=Very long chain 3-oxoacyl-CoA synthase 1; |
Gene name | Name=ELOVL1; |
Comments
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case <OC:Mammalia> | |
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. |
else | |
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. |
end case | |
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; |
case <OC:Mammalia> | |
SUBUNIT | Interacts with @gn(LASS2), @gn(TECR) and @gn(HSD17B12). |
end case | |
PATHWAY | Lipid metabolism; fatty acid biosynthesis. |
SUBCELLULAR LOCATION | Endoplasmic reticulum membrane; Multi-pass membrane protein. |
case <FTTag:ERmotif> | |
DOMAIN | The C-terminal di-lysine motif may confer endoplasmic reticulum localization. |
end case | |
SIMILARITY | Belongs to the ELO family. ELOVL1 subfamily. |
Keywords
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Endoplasmic reticulum |
Fatty acid biosynthesis |
Fatty acid metabolism |
Lipid biosynthesis |
Lipid metabolism |
Membrane |
Transferase |
Gene Ontology
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GO:0005789; Cellular component:endoplasmic reticulum membrane |
GO:0016020; Cellular component:membrane |
GO:0009922; Molecular function:fatty acid elongase activity |
GO:0006636; Biological process:unsaturated fatty acid biosynthetic process |
GO:0019367; Biological process:fatty acid elongation, saturated fatty acid |
GO:0034625; Biological process:fatty acid elongation, monounsaturated fatty acid |
GO:0035338; Biological process:long-chain fatty-acyl-CoA biosynthetic process |
GO:0042761; Biological process:very long-chain fatty acid biosynthetic process |
Cross-references
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PROSITE | PS01188; ELO; 1; |
Pfam | PF01151; ELO; 1; |
General | Transmembrane; -; 7; |
Features
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From: ELOV1_HUMAN (Q9BW60) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
MOTIF | Cter-4 | Cter | /note="Di-lysine motif" | ERmotif | K-x-K-x(2)> |
Additional information
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Size range | 276-368 amino acids |
Related rules |
MF_03204 MF_03207 |
Fusion | Nter: None Cter: None |