HAMAP rule MF_03207
General rule information
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| Accession | MF_03207 |
| Dates | 16-DEC-2013 (Created)
3-SEP-2024 (Last updated, Version 12) |
| Name | VLCF_elongase_7 |
| Scope(s) |
Eukaryota Vertebrata |
| Template(s) | A1L3X0 (ELOV7_HUMAN); [ Recover all ] |
| Triggered by |
HAMAP; MF_03207 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | ELOV7 |
| Protein name | RecName: Full=Elongation of very long chain fatty acids protein 7; EC=2.3.1.199; AltName: Full=3-keto acyl-CoA synthase AltName: Full=ELOVL fatty acid elongase 7; Short=ELOVL FA elongase 7; AltName: Full=Very long chain 3-ketoacyl-CoA synthase 7; AltName: Full=Very long chain 3-oxoacyl-CoA synthase 7; |
| Gene name | Name=ELOVL7; |
Comments
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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 with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. May participate to the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. |
| CATALYTIC ACTIVITY | Reaction=a very-long-chain acyl-CoA + malonyl-CoA + H(+) = 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; |
| 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. ELOVL7 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:0034626; Biological process:fatty acid elongation, polyunsaturated 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: ELOV7_HUMAN (A1L3X0) | ||||||||||||
| 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 | 268-304 amino acids |
| Related rules |
MF_03201 MF_03204 |
| Fusion | Nter: None Cter: None |