A0A2K6RTD7 · A0A2K6RTD7_RHIRO
- ProteinElongation of very long chain fatty acids protein 6
- GeneELOVL6
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids265 (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 elongates fatty acids with 12, 14 and 16 carbons with higher activity toward C16:0 acyl-CoAs. Catalyzes the synthesis of unsaturated C16 long chain fatty acids and, to a lesser extent, C18:0 and those with low desaturation degree. 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
- (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.
- H+ + hexadecanoyl-CoA + malonyl-CoA = 3-oxooctadecanoyl-CoA + CO2 + CoAThis reaction proceeds in the forward direction.
- H+ + malonyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA + CO2 + CoAThis reaction proceeds in the forward direction.
- dodecanoyl-CoA + H+ + malonyl-CoA = 3-oxotetradecanoyl-CoA + CO2 + CoAThis reaction proceeds in the forward direction.
Pathway
Lipid metabolism; fatty acid biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | fatty acid elongase complex | |
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 | 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 6
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Colobinae > Rhinopithecus
Accessions
- Primary accessionA0A2K6RTD7
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 | 34-51 | Helical | ||||
Sequence: FLFSALYAAFIFGGRHLM | ||||||
Transmembrane | 63-91 | Helical | ||||
Sequence: LVLWSLTLAVFSIFGALRTGACMVYILMT | ||||||
Transmembrane | 139-156 | Helical | ||||
Sequence: FLHWYHHITVLLYSWYSY | ||||||
Transmembrane | 162-183 | Helical | ||||
Sequence: GGGWFMTMNYGVHAVMYSYYAL | ||||||
Transmembrane | 195-220 | Helical | ||||
Sequence: AMFITLSQITQMLMGCVVNYLVFYWM | ||||||
Transmembrane | 232-251 | Helical | ||||
Sequence: IFWSSLMYLSYLVLFCHFFF |
Keywords
- Cellular component
PTM/Processing
Post-translational modification
N-Glycosylated.
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Sequence similarities
Belongs to the ELO family. ELOVL6 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length265
- Mass (Da)31,440
- Last updated2018-03-28 v1
- ChecksumA724DC6912230519
Keywords
- Technical term