Q9H5J4 · ELOV6_HUMAN
- ProteinVery long chain fatty acid elongase 6
- GeneELOVL6
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids265 (go to sequence)
- Protein existenceEvidence at protein level
- 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 in 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
- H+ + hexadecanoyl-CoA + malonyl-CoA = 3-oxooctadecanoyl-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.
- dodecanoyl-CoA + H+ + malonyl-CoA = 3-oxotetradecanoyl-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.
- (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.
Activity regulation
The reaction is stimulated by the presence of HSD17B12, the enzyme catalyzing the second step of the elongation cycle.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.22 μM | hexadecanoyl-CoA | 6.8 | 37 |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
0.79 pmol/min/ug | with hexadecanoyl-CoA as substrate |
Pathway
Lipid metabolism; fatty acid biosynthesis.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | endoplasmic reticulum membrane | |
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 | positive regulation of cold-induced thermogenesis | |
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
Chemistry
Names & Taxonomy
Protein names
- Recommended nameVery long chain fatty acid elongase 6
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H5J4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 34-51 | Helical | ||||
Sequence: FLFSALYAAFIFGGRHLM | ||||||
Transmembrane | 70-90 | Helical | ||||
Sequence: LAVFSIFGALRTGAYMVYILM | ||||||
Transmembrane | 111-131 | Helical | ||||
Sequence: FWAYAFVLSKAPELGDTIFII | ||||||
Transmembrane | 136-156 | Helical | ||||
Sequence: KLIFLHWYHHITVLLYSWYSY | ||||||
Transmembrane | 159-179 | Helical | ||||
Sequence: MVAGGGWFMTMNYGVHAVMYS | ||||||
Transmembrane | 197-217 | Helical | ||||
Sequence: FITLSQITQMLMGCVVNYLVF | ||||||
Transmembrane | 232-252 | Helical | ||||
Sequence: IFWSSLMYLSYLVLFCHFFFE |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 203 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000282845 | 1-265 | Very long chain fatty acid elongase 6 | |||
Sequence: MNMSVLTLQEYEFEKQFNENEAIQWMQENWKKSFLFSALYAAFIFGGRHLMNKRAKFELRKPLVLWSLTLAVFSIFGALRTGAYMVYILMTKGLKQSVCDQGFYNGPVSKFWAYAFVLSKAPELGDTIFIILRKQKLIFLHWYHHITVLLYSWYSYKDMVAGGGWFMTMNYGVHAVMYSYYALRAAGFRVSRKFAMFITLSQITQMLMGCVVNYLVFCWMQHDQCHSHFQNIFWSSLMYLSYLVLFCHFFFEAYIGKMRKTTKAE | ||||||
Glycosylation | 2 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-Glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9H5J4 | HMOX1 P09601 | 3 | EBI-12821617, EBI-2806151 | |
BINARY | Q9H5J4 | LCP2 Q13094 | 3 | EBI-12821617, EBI-346946 | |
BINARY | Q9H5J4 | RTP2 Q5QGT7 | 3 | EBI-12821617, EBI-10244780 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length265
- Mass (Da)31,376
- Last updated2001-03-01 v1
- Checksum01234E0EEF6CE341
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 10-11 | in Ref. 1; BAC11225 | ||||
Sequence: EY → KN |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK074813 EMBL· GenBank· DDBJ | BAC11225.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK027031 EMBL· GenBank· DDBJ | BAB15632.1 EMBL· GenBank· DDBJ | mRNA | ||
AC004050 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC093770 EMBL· GenBank· DDBJ | AAY40928.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001305 EMBL· GenBank· DDBJ | AAH01305.1 EMBL· GenBank· DDBJ | mRNA |