HAMAP rule MF_03202
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_03202 |
| Accession | MF_03202 |
| Dates | 16-DEC-2013 (Created)
03-SEP-2024 (Last updated, Version 15) |
| Name | VLCF_elongase_2 |
| Scope(s) |
Eukaryota Vertebrata |
| Template(s) | Q9NXB9; Q9JLJ4; D4A612; [ Recover all ] |
| Triggered by |
HAMAP; MF_03202 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | ELOV2 |
| Protein name | RecName: Full=Elongation of very long chain fatty acids protein 2; EC=2.3.1.199; AltName: Full=3-keto acyl-CoA synthase AltName: Full=ELOVL fatty acid elongase 2; Short=ELOVL FA elongase 2; AltName: Full=Very long chain 3-ketoacyl-CoA synthase 2; AltName: Full=Very long chain 3-oxoacyl-CoA synthase 2; |
| Gene name | Name=ELOVL2; |
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. 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 | 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; polyunsaturated 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. ELOVL2 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:0034626; Biological process:fatty acid elongation, polyunsaturated fatty acid |
| GO:0042761; Biological process:very long-chain fatty acid biosynthetic process |
| GO:0006636; Biological process:unsaturated 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: ELOV2_HUMAN (Q9NXB9) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| MOTIF | Cter-3 | Cter | /note="Di-lysine motif" | ERmotif | K-K-x(2)> | |||||||
Additional information
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| Size range | 257-343 amino acids |
| Related rules |
MF_03205 |
| Fusion | Nter: None Cter: None |