ELOVL1 (very long chain fatty acid elongase 1; 3-oxoacyl-CoA synthase ELOVL1, EC 2.3.1.199) is a multipass endoplasmic reticulum membrane enzyme of the ELO family that catalyzes the first and rate-limiting condensation step of the microsomal very-long-chain fatty acid (VLCFA) elongation cycle. It condenses a long-chain acyl-CoA with malonyl-CoA to yield a 3-oxoacyl-CoA plus CO2 and CoA; this 3-oxoacyl-CoA is subsequently reduced, dehydrated and reduced by KAR (HSD17B12), HACD1/2 and TECR to complete each two-carbon elongation. ELOVL1 is specific for saturated and monounsaturated acyl-CoA substrates and is the principal producer of C24-C26 VLCFAs (extending C22 to C24 to C26), with highest activity toward C22:0-CoA. Its VLCFA products are precursors of membrane lipids and lipid mediators, and are especially important for the synthesis of C24 sphingolipids and ceramides (coordinated with the ceramide synthase CERS2), contributing to myelin and the epidermal permeability barrier. In humans, dominant loss-of-function ELOVL1 variants (recurrent p.Ser165Phe) cause ichthyotic keratoderma with spasticity, hypomyelination and dysmorphic facies (IKSHD).
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005789 endoplasmic reticulum membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Correct localization. ELOVL1 is a multipass ER membrane enzyme and is active in the ER membrane, consistent with experimental (EXP/IDA) evidence and UniProt. Core location. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0009922 fatty acid elongase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Correct core molecular function. The GO definition of this term is exactly the ELOVL1 condensation reaction (very-long-chain acyl-CoA + malonyl-CoA -> 3-oxoacyl-CoA + CO2 + CoA; EC 2.3.1.199), the first and rate-limiting step of the elongation cycle. Directly supported by EXP/IDA evidence. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle |
| GO:0042761 very long-chain fatty acid biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: Correct core biological process. ELOVL1 is the principal elongase producing C24-C26 saturated/monounsaturated VLCFAs. Also directly supported by IDA (PMID:20166112, PMID:20937905). Supporting Evidence: PMID:20166112 We identify ELOVL1 (elongation of very-long-chain-fatty acids) as the single elongase catalysing the synthesis of both saturated VLCFA (C26:0) and mono-unsaturated VLCFA (C26:1). |
| GO:0030148 sphingolipid biosynthetic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Correct. ELOVL1-derived C24 acyl-CoAs are required for C24 sphingolipid synthesis (coordinated with CERS2). Also supported by IMP (PMID:20937905). Contributory downstream process; kept as non-core relative to the direct elongase activity. Supporting Evidence: PMID:20937905 it was essential for the production of C24 sphingolipids |
| GO:0034626 fatty acid elongation, polyunsaturated fatty acid | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: Over-annotation from phylogenetic propagation. ELOVL1 is specific for SATURATED and MONOUNSATURATED acyl-CoA substrates; PUFA elongation is the role of the ELOVL2/ELOVL5 paralogs. In substrate profiling no PUFA activity is attributed to ELOVL1. Marked as over-annotated rather than removed (IBA). Propagation Review Root cause: PROPAGATION BAD Failure modes: WRONG ORTHOLOG OR PARALOG FUNCTIONAL DIVERGENCE Sources checked: PANTHER:PTN000125390 · ELOVL family node (includes PUFA-elongating ELOVL2/ELOVL5) SUPPORTS SOURCE BUT NOT TARGET Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt Condensing enzyme that exhibits activity toward saturated and monounsaturated acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. |
| GO:0019367 fatty acid elongation, saturated fatty acid | IBA GO_REF:0000033 | ACCEPT | Summary: Correct. ELOVL1 elongates saturated VLCFAs (e.g. C22:0 to C24:0 to C26:0). Also directly supported by IDA (PMID:20166112, PMID:20937905). Core process. Supporting Evidence: PMID:19575253 ELOVL1, -3 and -6 preferably elongated the saturated fatty acyl-CoAs |
| GO:0034625 fatty acid elongation, monounsaturated fatty acid | IBA GO_REF:0000033 | ACCEPT | Summary: Correct. ELOVL1 elongates monounsaturated VLCFAs (e.g. C24:1, C26:1). Also directly supported by IDA (PMID:20166112). Core process. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt Important for saturated C24:0 and monounsaturated C24:1 sphingolipid synthesis |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000002 | MARK AS OVER ANNOTATED | Summary: Correct organelle, but less precise than the ER membrane localization (ELOVL1 is a multipass ER MEMBRANE protein). Generalization of the well-supported GO:0005789 term. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Correct core localization, consistent with UniProt and experimental evidence. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0006636 unsaturated fatty acid biosynthetic process | IEA GO_REF:0000104 | KEEP AS NON CORE | Summary: Defensible but imprecise. ELOVL1 elongates monounsaturated (not polyunsaturated) VLCFAs, so it does contribute to unsaturated fatty acid biosynthesis, but the specific terms fatty acid elongation, monounsaturated fatty acid (GO:0034625) and VLCFA biosynthetic process (GO:0042761) are better. Kept as non-core. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt Condensing enzyme that exhibits activity toward saturated and monounsaturated acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. |
| GO:0009922 fatty acid elongase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Correct core molecular function (electronic support via InterPro/UniRule/EC 2.3.1.199). Redundant with the EXP/IDA/IBA annotations to the same term. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle |
| GO:0016020 membrane | IEA GO_REF:0000120 | MARK AS OVER ANNOTATED | Summary: Too general. ELOVL1 is specifically an ER membrane protein; the generic membrane term should be replaced by endoplasmic reticulum membrane. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0019367 fatty acid elongation, saturated fatty acid | IEA GO_REF:0000120 | ACCEPT | Summary: Correct (electronic). Redundant with the IDA-supported same-term annotations. Supporting Evidence: PMID:19575253 ELOVL1, -3 and -6 preferably elongated the saturated fatty acyl-CoAs |
| GO:0030497 fatty acid elongation | IEA GO_REF:0000117 | ACCEPT | Summary: Correct high-level process (ARBA electronic). Accurate but less specific than very long-chain fatty acid biosynthetic process; retained as a valid grouping term. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt allows the addition of 2 carbons to the chain of file:human/ELOVL1/ELOVL1-uniprot.txt long- and very long-chain fatty acids (VLCFAs) per cycle |
| GO:0034625 fatty acid elongation, monounsaturated fatty acid | IEA GO_REF:0000104 | ACCEPT | Summary: Correct (electronic). Redundant with the IDA-supported same-term annotation. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt Important for saturated C24:0 and monounsaturated C24:1 sphingolipid synthesis |
| GO:0035338 long-chain fatty-acyl-CoA biosynthetic process | IEA GO_REF:0000104 | KEEP AS NON CORE | Summary: Defensible. The elongation cycle products are (very-)long-chain fatty-acyl-CoAs, so ELOVL1 contributes to long-chain fatty-acyl-CoA biosynthesis. The VLCFA-specific terms are more informative; kept as non-core. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt Reaction=a very-long-chain acyl-CoA + malonyl-CoA + H(+) = a very-long- file:human/ELOVL1/ELOVL1-uniprot.txt chain 3-oxoacyl-CoA + CO2 + CoA |
| GO:0042761 very long-chain fatty acid biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: Correct core process (electronic). Redundant with IDA/IBA same-term annotations. Supporting Evidence: PMID:20166112 We identify ELOVL1 (elongation of very-long-chain-fatty acids) as the single elongase catalysing the synthesis of both saturated VLCFA (C26:0) and mono-unsaturated VLCFA (C26:1). |
| GO:0005515 protein binding | IPI PMID:23864651 The identification of novel proteins that interact with the ... | MARK AS OVER ANNOTATED | Summary: Uninformative bare protein binding. Derived (IntAct) from a MYTH interactome screen reporting ELOVL1 among 38 candidate GLP-1R (P43220) interactors; ELOVL1 is a bystander ER enzyme in that dataset, not a GLP-1 signaling component. Not removed (IPI); marked over-annotated. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt Q9BW60; P43220: GLP1R; NbExp=3; IntAct=EBI-1050331, EBI-7466542 |
| GO:0030148 sphingolipid biosynthetic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Correct (electronic, orthology to mouse Elovl1). ELOVL1 C24-CoA production feeds C24 sphingolipid synthesis. Kept as non-core downstream process. Supporting Evidence: PMID:20937905 it was essential for the production of C24 sphingolipids |
| GO:0046513 ceramide biosynthetic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Correct (electronic, orthology). ELOVL1 supplies the >=C24 acyl-CoAs used by ceramide synthases; loss of ELOVL1 activity reduces >=C24 ceramides. Downstream contributory process; non-core. Supporting Evidence: PMID:30487246 reduced ≥C24 ceramides and sphingomyelins in patient cells |
| GO:0061436 establishment of skin barrier | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Plausible (electronic, orthology). VLCFA/ceramide products are important for the epidermal permeability barrier, and ELOVL1 loss-of-function causes ichthyosis; this is a distal physiological consequence rather than the direct molecular activity. Kept as non-core. Supporting Evidence: PMID:30487246 upregulation of modules involved in epidermal development and keratinisation |
| GO:0035338 long-chain fatty-acyl-CoA biosynthetic process | TAS Reactome:R-HSA-75876 | KEEP AS NON CORE | Summary: Defensible Reactome grouping (Synthesis of very long-chain fatty acyl-CoAs). Consistent with ELOVL1 catalysis; more specific VLCFA terms preferred. Non-core. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt Reaction=a very-long-chain acyl-CoA + malonyl-CoA + H(+) = a very-long- |
| GO:0036109 alpha-linolenic acid metabolic process | TAS Reactome:R-HSA-2046106 | KEEP AS NON CORE | Summary: Reactome places all four ELOVLs generically in the n-3 PUFA (ALA) elongation pathway. ELOVL1 is specific for saturated/monounsaturated VLCFAs and is not the principal PUFA (ALA) elongase (ELOVL2/ELOVL5), so this pathway context is peripheral for ELOVL1. Not removed (TAS); non-core. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt Condensing enzyme that exhibits activity toward saturated and monounsaturated acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. |
| GO:0043651 linoleic acid metabolic process | TAS Reactome:R-HSA-2046105 | KEEP AS NON CORE | Summary: As with the ALA term, Reactome groups all four ELOVLs into the n-6 PUFA (LA) elongation pathway. ELOVL1 acts on saturated/monounsaturated VLCFAs and is not the principal linoleic-acid/PUFA elongase; peripheral pathway context. Not removed (TAS); non-core. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt Condensing enzyme that exhibits activity toward saturated and monounsaturated acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. |
| GO:0006633 fatty acid biosynthetic process | IEA GO_REF:0000041 | KEEP AS NON CORE | Summary: Correct but high-level (UniPathway mapping). Accurate parent process; more specific VLCFA biosynthetic process is preferred. Non-core grouping. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt PATHWAY: Lipid metabolism; fatty acid biosynthesis. |
| GO:0009922 fatty acid elongase activity | EXP PMID:10970790 Cloning of a human cDNA encoding a novel enzyme involved in ... | ACCEPT | Summary: The MF term (fatty acid elongase activity) is correct for ELOVL1 and is abundantly supported by other EXP/IDA papers, so the term is accepted. However the cited reference is problematic: PMID:10970790 (Leonard et al. 2000) cloned "HELO1", a 299-aa human elongase on chromosome 6 that elongates long-chain POLYUNSATURATED fatty acids (i.e. ELOVL5), not ELOVL1 (279 aa, chromosome 1, saturated/monounsaturated VLCFAs). Per policy an experimental annotation is not removed on the basis of an abstract; the reference mis-attribution is flagged in reference_review. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle |
| GO:0005783 endoplasmic reticulum | IDA GO_REF:0000052 | MARK AS OVER ANNOTATED | Summary: Correct organelle from HPA immunofluorescence, but less precise than ER membrane (ELOVL1 is a multipass ER MEMBRANE protein). Generalization of the well-supported GO:0005789 term. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingol... | ACCEPT | Summary: Correct core localization, experimentally determined. Consistent with UniProt. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:30487246 De novo mutation in ELOVL1 causes ichthyosis, acanthosis nig... | ACCEPT | Summary: Correct core localization, experimentally determined (immunofluorescence in the IKSHD study). Consistent with UniProt. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0009922 fatty acid elongase activity | EXP PMID:19575253 Development of a high-density assay for long-chain fatty acy... | ACCEPT | Summary: Correct core molecular function. Kitazawa et al. profiled recombinant ELOVL1 elongase activity in a high-density acyl-CoA elongation assay, showing it preferentially elongates saturated fatty acyl-CoAs. Supporting Evidence: PMID:19575253 ELOVL1, -3 and -6 preferably elongated the saturated fatty acyl-CoAs |
| GO:0009922 fatty acid elongase activity | EXP PMID:20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingol... | ACCEPT | Summary: Correct core molecular function. Ohno et al. determined ELOVL1 substrate specificity by in vitro elongation assay, showing high activity toward saturated and monounsaturated C20-/C22-CoAs. Supporting Evidence: PMID:20937905 the high activity exhibited by ELOVL1 toward saturated and monounsaturated C20- and C22-CoAs |
| GO:0009922 fatty acid elongase activity | EXP PMID:29496980 Dominant ELOVL1 mutation causes neurological disorder with i... | ACCEPT | Summary: Correct core molecular function. VLCFA elongase activity of ELOVL1 was assayed by VLCFA profiling in cells expressing wild-type and IKSHD-mutant ELOVL1 (the mutant reducing C24:0-C28:0/C26:1 production). Supporting Evidence: PMID:29496980 reduced levels of FAs C24:0-C28:0 and C26:1 with the most pronounced effect for C26:0 |
| GO:0009922 fatty acid elongase activity | EXP PMID:30487246 De novo mutation in ELOVL1 causes ichthyosis, acanthosis nig... | ACCEPT | Summary: Correct core molecular function. ELOVL1 enzymatic activity was measured by a stable-isotope [13C]malonyl-CoA elongation assay; the disease mutation abrogated activity. Supporting Evidence: PMID:30487246 The mutation abrogated ELOVL1 enzymatic activity |
| GO:0005515 protein binding | IPI PMID:38422897 The 3-hydroxyacyl-CoA dehydratase 1/2 form complex with tran... | MARK AS OVER ANNOTATED | Summary: Uninformative bare protein binding. Captures the ELOVL1-TECR interaction (with/from Q9NZ01) within the ER VLCFA elongation machinery; while biologically real, the bare term is not informative and the interaction is recorded in notes/core functions. Not removed (IPI); marked over-annotated. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt Interacts with TECR (PubMed:20937905, PubMed:38422897) |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | MARK AS OVER ANNOTATED | Summary: Too general. From an NK-cell membrane proteomics dataset; consistent with ELOVL1 being an integral membrane protein but far less informative than its specific ER membrane localization. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-2046088 | ACCEPT | Summary: Correct core localization (Reactome elongation reaction). Consistent with UniProt. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-2046094 | ACCEPT | Summary: Correct core localization (Reactome elongation reaction). Consistent with UniProt. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-548800 | ACCEPT | Summary: Correct core localization (Reactome: ELOVL1,2,3,5 elongate AA-CoA and Mal-CoA). Consistent with UniProt. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005515 protein binding | IPI PMID:20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingol... | MARK AS OVER ANNOTATED | Summary: Uninformative bare protein binding (IntAct-derived interactions from the Ohno et al. study, with/from including elongation-machinery partners). The meaningful interactions (CERS2/LASS2, HSD17B12, TECR) are recorded in notes; the bare term is not informative. Not removed (IPI); over-annotated. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt Interacts with LASS2 and HSD17B12. |
| GO:0005783 endoplasmic reticulum | IDA PMID:20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingol... | MARK AS OVER ANNOTATED | Summary: Correct organelle, experimentally determined, but less precise than ER membrane (ELOVL1 is a multipass ER MEMBRANE protein). Generalization of the well-supported GO:0005789 term. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | NAS PMID:20166112 The role of ELOVL1 in very long-chain fatty acid homeostasis... | ACCEPT | Summary: Correct core localization (author statement). Consistent with UniProt. Supporting Evidence: file:human/ELOVL1/ELOVL1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0009922 fatty acid elongase activity | IDA PMID:20166112 The role of ELOVL1 in very long-chain fatty acid homeostasis... | ACCEPT | Summary: Correct core molecular function, experimentally determined. Ofman et al. showed by expression/knockdown that ELOVL1 elongates C22:0 to C26:0 and is the single elongase making C26:0/C26:1. Supporting Evidence: PMID:20166112 We identify ELOVL1 (elongation of very-long-chain-fatty acids) as the single elongase catalysing the synthesis of both saturated VLCFA (C26:0) and mono-unsaturated VLCFA (C26:1). |
| GO:0019367 fatty acid elongation, saturated fatty acid | IDA PMID:20166112 The role of ELOVL1 in very long-chain fatty acid homeostasis... | ACCEPT | Summary: Correct core process, experimentally determined. ELOVL1 elongates saturated VLCFAs (C22:0 to C26:0). Supporting Evidence: PMID:20166112 ELOVL1 knockdown reduces elongation of C22:0 to C26:0 and lowers C26:0 levels in X-ALD fibroblasts. |
| GO:0019367 fatty acid elongation, saturated fatty acid | IDA PMID:20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingol... | ACCEPT | Summary: Correct core process, experimentally determined (in vitro substrate profiling toward saturated C20-/C22-CoAs). Supporting Evidence: PMID:20937905 the high activity exhibited by ELOVL1 toward saturated and monounsaturated C20- and C22-CoAs |
| GO:0030148 sphingolipid biosynthetic process | IMP PMID:20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingol... | KEEP AS NON CORE | Summary: Correct, experimentally supported (ELOVL1 knockdown; ELOVL1 essential for C24 sphingolipid production). Downstream process fed by ELOVL1 activity; kept as non-core relative to the direct elongase MF. Supporting Evidence: PMID:20937905 it was essential for the production of C24 sphingolipids |
| GO:0034625 fatty acid elongation, monounsaturated fatty acid | IDA PMID:20166112 The role of ELOVL1 in very long-chain fatty acid homeostasis... | ACCEPT | Summary: Correct core process, experimentally determined. ELOVL1 is the single elongase producing monounsaturated C26:1. Supporting Evidence: PMID:20166112 We identify ELOVL1 (elongation of very-long-chain-fatty acids) as the single elongase catalysing the synthesis of both saturated VLCFA (C26:0) and mono-unsaturated VLCFA (C26:1). |
| GO:0042761 very long-chain fatty acid biosynthetic process | IDA PMID:20166112 The role of ELOVL1 in very long-chain fatty acid homeostasis... | ACCEPT | Summary: Correct core process, experimentally determined. ELOVL1 synthesizes C24-C26 VLCFAs. Supporting Evidence: PMID:20166112 We identify ELOVL1 (elongation of very-long-chain-fatty acids) as the single elongase catalysing the synthesis of both saturated VLCFA (C26:0) and mono-unsaturated VLCFA (C26:1). |
| GO:0042761 very long-chain fatty acid biosynthetic process | IDA PMID:20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingol... | ACCEPT | Summary: Correct core process, experimentally determined (substrate profiling; production of C24 VLCFAs/sphingolipids). Supporting Evidence: PMID:20937905 the high activity exhibited by ELOVL1 toward saturated and monounsaturated C20- and C22-CoAs |
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Download this section (compressed HTML)Q: Beyond providing C24-C26 VLCFA/sphingolipid precursors, does ELOVL1 have a scaffolding role in organizing the four-component ER elongation machinery (ELOVL-KAR-HACD-TECR)?
Q: How does the dominant p.Ser165Phe variant act (dominant-negative versus haploinsufficiency) given that ELOVL1 participates in a multi-enzyme complex?
Experiment: Reconstitute the ELOVL1/KAR/HACD/TECR elongation cycle in vitro to quantify the chain-length-dependent kcat/KM of the condensation step across C18-C26 saturated and monounsaturated acyl-CoA substrates.
Experiment: Tissue-specific conditional Elovl1 knockout (skin, oligodendrocytes) with VLCFA and sphingolipid lipidomics to dissect the myelin versus epidermal-barrier contributions.
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