A0A3B4WBD4 · A0A3B4WBD4_SERLL
- ProteinElongation of very long chain fatty acids protein 5
- GeneELOVL5
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids294 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
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 acts specifically toward polyunsaturated acyl-CoA with the higher activity toward C18:3(n-6) acyl-CoA. May participate to the production of monounsaturated and of polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Catalytic activity
- (11Z)-octadecenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(13Z)-eicosenoyl-CoA + CO2 + CoAThis reaction proceeds in the forward direction.
- (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H+ + malonyl-CoA = (7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + CO2 + CoAThis reaction proceeds in the forward direction.
- (6Z,9Z,12Z)-octadecatrienoyl-CoA + H+ + malonyl-CoA = (8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoAThis reaction proceeds in the forward direction.
- (6Z,9Z,12Z,15Z)-octadecatetraenoyl-CoA + H+ + malonyl-CoA = (8Z,11Z,14Z,17Z)-3-oxoicosatetraenoyl-CoA + CO2 + CoAThis reaction proceeds in the forward direction.
- (9Z)-hexadecenoyl-CoA + H+ + malonyl-CoA = 3-oxo-(11Z)-octadecenoyl-CoA + CO2 + CoAThis reaction proceeds in the forward direction.
- (9Z)-octadecenoyl-CoA + H+ + malonyl-CoA = (11Z)-3-oxoicosenoyl-CoA + CO2 + CoAThis reaction proceeds in the forward direction.
- (9Z,12Z)-octadecadienoyl-CoA + H+ + malonyl-CoA = (11Z,14Z)-3-oxoicosa-11,14-dienoyl-CoA + CO2 + CoAThis reaction proceeds in the forward direction.
- (9Z,12Z,15Z)-octadecatrienoyl-CoA + H+ + malonyl-CoA = (11Z,14Z,17Z)-3-oxoeicosatrienoyl-CoA + CO2 + CoAThis reaction proceeds in the forward direction.
Pathway
Lipid metabolism; polyunsaturated fatty acid biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | dendrite | |
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | fatty acid elongase activity | |
Biological Process | fatty acid elongation, monounsaturated fatty acid | |
Biological Process | fatty acid elongation, polyunsaturated fatty acid | |
Biological Process | fatty acid elongation, saturated fatty acid | |
Biological Process | long-chain fatty acid biosynthetic process | |
Biological Process | long-chain fatty-acyl-CoA biosynthetic process | |
Biological Process | unsaturated fatty acid biosynthetic process | |
Biological Process | very long-chain fatty acid biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameElongation of very long chain fatty acids protein 5
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Carangaria > Carangiformes > Carangidae > Seriola
Accessions
- Primary accessionA0A3B4WBD4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Note: In Purkinje cells, the protein localizes to the soma and proximal portion of the dendritic tree.
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 32-49 | Helical | ||||
Sequence: YPPTFALTVMYLLIVWMG | ||||||
Transmembrane | 61-81 | Helical | ||||
Sequence: CRGLLVLYNLGLTLLSFYMFY | ||||||
Transmembrane | 114-132 | Helical | ||||
Sequence: WWYYFSKLIEFMDTFFFIL | ||||||
Transmembrane | 144-161 | Helical | ||||
Sequence: IYHHATMLNIWWFVMNWI | ||||||
Transmembrane | 207-224 | Helical | ||||
Sequence: LIQFFLTMSQTMCAVIWP | ||||||
Transmembrane | 230-251 | Helical | ||||
Sequence: GWLYFQISYMVTLIILFSNFYI |
Keywords
- Cellular component
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 261-294 | Disordered | ||||
Sequence: LKKEHQNGSPVSTNGHANGTPSMEHNVHKKLRVD | ||||||
Compositional bias | 264-281 | Polar residues | ||||
Sequence: EHQNGSPVSTNGHANGTP |
Sequence similarities
Belongs to the ELO family. ELOVL5 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length294
- Mass (Da)35,115
- Last updated2018-12-05 v1
- ChecksumFB59407C1BA8FDA7
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 264-281 | Polar residues | ||||
Sequence: EHQNGSPVSTNGHANGTP |