A0A485MVX2 · A0A485MVX2_LYNPA
- ProteinElongation of very long chain fatty acids protein 3
- GeneELOVL3
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids270 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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 with higher activity toward C18 acyl-CoAs, especially C18:0 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.
Catalytic activity
- a very-long-chain acyl-CoA + H+ + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
Pathway
Lipid metabolism; polyunsaturated fatty acid biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
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-acyl-CoA biosynthetic process | |
Biological Process | sphingolipid 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 3
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Feliformia > Felidae > Felinae > Lynx
Accessions
- Primary accessionA0A485MVX2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 33-55 | Helical | ||||
Sequence: YWATSFPIALVYLLLIFVGQNYM | ||||||
Transmembrane | 67-87 | Helical | ||||
Sequence: LILWSFCLAIFSILGAVRTWG | ||||||
Transmembrane | 166-185 | Helical | ||||
Sequence: AGGWFMTMNYGVHAIMYIYY | ||||||
Transmembrane | 197-223 | Helical | ||||
Sequence: WLPKLITSLQILQMFMGTIVGILTYIW | ||||||
Transmembrane | 235-254 | Helical | ||||
Sequence: HFFWSLVLYTTYFILFAHYF |
Keywords
- Cellular component
PTM/Processing
Post-translational modification
N-Glycosylated.
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 266-270 | Di-lysine motif | ||||
Sequence: KTKSQ |
Domain
The C-terminal di-lysine motif may confer endoplasmic reticulum localization.
Sequence similarities
Belongs to the ELO family. ELOVL3 subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length270
- Mass (Da)31,607
- Last updated2019-06-05 v1
- ChecksumF39B9B6965B5A94A
Keywords
- Technical term