ELOVL6

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005789 endoplasmic reticulum membrane	IBA GO_REF:0000033	ACCEPT	Summary: ELOVL6 is a multipass endoplasmic-reticulum membrane elongase; this location is supported. Reason: The full human ELOVL comparison in PMID:20937905 reports ER localization for all seven proteins, consistent with the target UniProt membrane topology. A parent membrane/ER term remains a correct description of the core location; breadth and duplicate evidence are not biological contradictions. This does not transfer the fly ELOVL6 mitochondrial location to human. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000125390 SUPPORTS TRANSFER Actual PTHR11157 tree places human ELOVL6 below the positive PTN000125390 IBD for this term. No on-lineage NOT/IRD was found; target self-inclusion and donor number are not objections. Target-specific biochemical scope is assessed separately in the reason. Supporting Evidence: file:human/ELOVL6/ELOVL6-primary-assessment.md Results describe ER localization for all seven proteins file:human/ELOVL6/ELOVL6-primary-assessment.md Both targets descend from PTN000125390; donor count and target self-inclusion are not objections.
GO:0009922 fatty acid elongase activity	IBA GO_REF:0000033	ACCEPT	Summary: Core molecular function. The IBA assignment of fatty acid elongase activity matches direct enzymatic evidence (EC 2.3.1.199) for human ELOVL6. Reason: This protein catalyzes the malonyl-CoA-dependent condensation step of the ER fatty-acid elongation cycle. The three later reduction/dehydration/reduction reactions are performed by other enzymes; the elongase annotation correctly identifies the target condensing activity. The source-specific scope is described in the summary and reference review. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000125390 SUPPORTS TRANSFER Actual PTHR11157 tree places human ELOVL6 below the positive PTN000125390 IBD for this term. No on-lineage NOT/IRD was found; target self-inclusion and donor number are not objections. Target-specific biochemical scope is assessed separately in the reason. Supporting Evidence: file:human/ELOVL6/ELOVL6-uniprot.txt Condensing enzyme that elongates fatty acids with file:human/ELOVL6/ELOVL6-primary-assessment.md Both targets descend from PTN000125390; donor count and target self-inclusion are not objections.
GO:0042761 very long-chain fatty acid biosynthetic process	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: ELOVL6 performs an upstream elongation step in very-long-chain fatty-acid biosynthesis. Reason: The human target descends from the positive PTN000125390 assertion. C16-to-C18 synthesis alone does not produce a GO-defined VLCFA: GO:0042761 requires more than 22 aliphatic-tail carbons. However, full PMID:20937905 Figure 1D connects the ELOVL6 C16-to-C18 step to later ELOVL-dependent C20-C24 synthesis, and Reactome R-HSA-75876 describes this same multistep route. ELOVL6 performs actual precursor-chain synthesis within it. The annotation does not require ELOVL6 to catalyze the terminal >22-producing step. Retain this downstream multistep-pathway contribution as non-core relative to the defining C16-to-C18 reaction and C18-ceramide role. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000125390 SUPPORTS TRANSFER Actual PTHR11157 tree places human ELOVL6 below the positive PTN000125390 IBD for this term. No on-lineage NOT/IRD was found; target self-inclusion and donor number are not objections. Target-specific biochemical scope is assessed separately in the reason. Supporting Evidence: file:human/ELOVL6/ELOVL6-primary-assessment.md Figure 1D maps ELOVL6's C16-to-C18 step upstream of longer-chain synthesis. Reactome:R-HSA-75876 Saturated and monounsaturated VLCFAs can be synthesized by elongation of palmitic acid synthesized de novo or derived from the diet.
GO:0030148 sphingolipid biosynthetic process	IBA GO_REF:0000033	ACCEPT	Summary: ELOVL6 synthesizes acyl-chain precursors used for ceramide and sphingolipid biosynthesis. Reason: The positive PTN000125390 ancestry is compatible with direct pathway work. Sphingolipids are not restricted to C24-C26 acyl chains: mouse PMID:31529722 identifies an Elovl6-dependent C18:0 ceramide pool and Elovl6-CerS4 association, corroborated by full Figure 5. ELOVL6 condenses the acyl precursor; CerS4 performs the subsequent amide-bond reaction. This supports conserved sphingolipid participation without equating the ortholog experiment with a direct human flux assay. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000125390 SUPPORTS TRANSFER Actual PTHR11157 tree places human ELOVL6 below the positive PTN000125390 IBD for this term. No on-lineage NOT/IRD was found; target self-inclusion and donor number are not objections. Target-specific biochemical scope is assessed separately in the reason. Supporting Evidence: PMID:31529722 Its production involves the formation of an Elovl6-ceramide synthase 4 (CerS4) complex in the endoplasmic reticulum file:human/ELOVL6/ELOVL6-primary-assessment.md The study concerns mouse Elovl6 physiology and supports ortholog-conserved sphingolipid precursor synthesis
GO:0034626 fatty acid elongation, polyunsaturated fatty acid	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Human ELOVL6 displays weak but significant polyunsaturated-substrate elongation in membrane assays. Reason: The target inherits this capacity from PTN000125390. In full PMID:20937905 Figure 1B, ELOVL6 gives significant activity over vector with C18:2 and C18:3(n-3), despite far stronger C16:0 activity. Purified proteoliposome ELOVL6 in PMID:25003994 Figure 2D strongly favors C16:0 and gives near-baseline signals for other substrates under different conditions. This qualifies magnitude and context but does not negate the positive membrane assay. Retain the biochemical capacity without asserting a dominant physiological PUFA role. The weak PUFA capacity is retained as non-core because saturated and monounsaturated C16 substrates dominate its established physiological role. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000125390 SUPPORTS TRANSFER Actual PTHR11157 tree places human ELOVL6 below the positive PTN000125390 IBD for this term. No on-lineage NOT/IRD was found; target self-inclusion and donor number are not objections. Target-specific biochemical scope is assessed separately in the reason. Supporting Evidence: file:human/ELOVL6/ELOVL6-primary-assessment.md ELOVL6 signals for C18:2 and C18:3(n-3) are significantly above vector, although far below C16:0. file:human/ELOVL6/ELOVL6-primary-assessment.md Other substrate bars are near baseline; the figure does not establish an all-conditions negative for the weak PUFA activities detected in the 2010 membrane assay.
GO:0019367 fatty acid elongation, saturated fatty acid	IBA GO_REF:0000033	ACCEPT	Summary: Core process. ELOVL6 elongates saturated C16:0 to C18:0; the IBA assignment is consistent with direct experimental evidence. Reason: Saturated C16:0 and monounsaturated C16:1 elongations are established target capacities. These classes are not mutually exclusive, and relative substrate preference is not a reason to remove a documented lower-activity capacity. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000125390 SUPPORTS TRANSFER Actual PTHR11157 tree places human ELOVL6 below the positive PTN000125390 IBD for this term. No on-lineage NOT/IRD was found; target self-inclusion and donor number are not objections. Target-specific biochemical scope is assessed separately in the reason. Supporting Evidence: PMID:25003994 The FA elongase ELOVL6 is responsible for the conversion of C16-CoAs to C18-CoAs file:human/ELOVL6/ELOVL6-primary-assessment.md Both targets descend from PTN000125390; donor count and target self-inclusion are not objections.
GO:0034625 fatty acid elongation, monounsaturated fatty acid	IBA GO_REF:0000033	ACCEPT	Summary: Supported. ELOVL6 elongates monounsaturated C16:1 (palmitoleoyl-CoA) to C18:1, as documented by the UniProt catalytic-activity block. Accurate process annotation. Reason: Saturated C16:0 and monounsaturated C16:1 elongations are established target capacities. These classes are not mutually exclusive, and relative substrate preference is not a reason to remove a documented lower-activity capacity. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000125390 SUPPORTS TRANSFER Actual PTHR11157 tree places human ELOVL6 below the positive PTN000125390 IBD for this term. No on-lineage NOT/IRD was found; target self-inclusion and donor number are not objections. Target-specific biochemical scope is assessed separately in the reason. Supporting Evidence: file:human/ELOVL6/ELOVL6-primary-assessment.md Both targets descend from PTN000125390; donor count and target self-inclusion are not objections.
GO:0005783 endoplasmic reticulum	IEA GO_REF:0000002	ACCEPT	Summary: ELOVL6 is a multipass endoplasmic-reticulum membrane elongase; this location is supported. Reason: The full human ELOVL comparison in PMID:20937905 reports ER localization for all seven proteins, consistent with the target UniProt membrane topology. A parent membrane/ER term remains a correct description of the core location; breadth and duplicate evidence are not biological contradictions. This does not transfer the fly ELOVL6 mitochondrial location to human. Supporting Evidence: file:human/ELOVL6/ELOVL6-primary-assessment.md Results describe ER localization for all seven proteins
GO:0005789 endoplasmic reticulum membrane	IEA GO_REF:0000120	ACCEPT	Summary: ELOVL6 is a multipass endoplasmic-reticulum membrane elongase; this location is supported. Reason: The full human ELOVL comparison in PMID:20937905 reports ER localization for all seven proteins, consistent with the target UniProt membrane topology. A parent membrane/ER term remains a correct description of the core location; breadth and duplicate evidence are not biological contradictions. This does not transfer the fly ELOVL6 mitochondrial location to human. Supporting Evidence: file:human/ELOVL6/ELOVL6-primary-assessment.md Results describe ER localization for all seven proteins
GO:0006636 unsaturated fatty acid biosynthetic process	IEA GO_REF:0000104	ACCEPT	Summary: ELOVL6 performs synthesis of unsaturated fatty-acyl chains. Reason: Elongation preserves the existing double bonds while extending the acyl chain. This is biosynthetic work in the unsaturated-fatty-acid pathway, not a claim that the elongase itself introduces double bonds. Broadness relative to an elongation child term does not make this role non-core.
GO:0009922 fatty acid elongase activity	IEA GO_REF:0000120	ACCEPT	Summary: Core molecular function, redundant with the experimental (EXP/IMP) and IBA annotations. Correctly derived from EC 2.3.1.199 / RHEA:32727. Reason: This protein catalyzes the malonyl-CoA-dependent condensation step of the ER fatty-acid elongation cycle. The three later reduction/dehydration/reduction reactions are performed by other enzymes; the elongase annotation correctly identifies the target condensing activity. The source-specific scope is described in the summary and reference review.
GO:0016020 membrane	IEA GO_REF:0000120	ACCEPT	Summary: ELOVL6 is a multipass endoplasmic-reticulum membrane elongase; this location is supported. Reason: The full human ELOVL comparison in PMID:20937905 reports ER localization for all seven proteins, consistent with the target UniProt membrane topology. A parent membrane/ER term remains a correct description of the core location; breadth and duplicate evidence are not biological contradictions. This does not transfer the fly ELOVL6 mitochondrial location to human. Supporting Evidence: file:human/ELOVL6/ELOVL6-primary-assessment.md Results describe ER localization for all seven proteins
GO:0019367 fatty acid elongation, saturated fatty acid	IEA GO_REF:0000120	ACCEPT	Summary: Core process, redundant with the IDA/IGI/IBA annotations to the same term. Correct. Reason: Saturated C16:0 and monounsaturated C16:1 elongations are established target capacities. These classes are not mutually exclusive, and relative substrate preference is not a reason to remove a documented lower-activity capacity.
GO:0030497 fatty acid elongation	IEA GO_REF:0000117	ACCEPT	Summary: ELOVL6 directly catalyzes fatty-acid elongation. Reason: The target performs the chain-extending condensation step. This broad process is a correct core role; the availability of more specific substrate-class terms does not make it non-core.
GO:0034625 fatty acid elongation, monounsaturated fatty acid	IEA GO_REF:0000104	ACCEPT	Summary: Supported; ELOVL6 elongates monounsaturated C16:1 to C18:1. Redundant with the IBA annotation to the same term. Correct. Reason: Saturated C16:0 and monounsaturated C16:1 elongations are established target capacities. These classes are not mutually exclusive, and relative substrate preference is not a reason to remove a documented lower-activity capacity.
GO:0035338 long-chain fatty-acyl-CoA biosynthetic process	IEA GO_REF:0000104	ACCEPT	Summary: Accurate: ELOVL6 elongation produces long-chain (C18) fatty-acyl-CoAs. Correct higher-level process; redundant with the TAS Reactome annotation. Reason: ELOVL6 catalyzes the condensation step yielding C18 intermediates and acyl-CoA products after completion of the cycle. These are long-chain species under GO definitions using 13-22 aliphatic-tail carbons. This is direct synthesis work, not an inference that C18 meets the separate very-long-chain product boundary.
GO:0042761 very long-chain fatty acid biosynthetic process	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: ELOVL6 performs an upstream elongation step in very-long-chain fatty-acid biosynthesis. Reason: The human target descends from the positive PTN000125390 assertion. C16-to-C18 synthesis alone does not produce a GO-defined VLCFA: GO:0042761 requires more than 22 aliphatic-tail carbons. However, full PMID:20937905 Figure 1D connects the ELOVL6 C16-to-C18 step to later ELOVL-dependent C20-C24 synthesis, and Reactome R-HSA-75876 describes this same multistep route. ELOVL6 performs actual precursor-chain synthesis within it. The annotation does not require ELOVL6 to catalyze the terminal >22-producing step. Retain this downstream multistep-pathway contribution as non-core relative to the defining C16-to-C18 reaction and C18-ceramide role. Supporting Evidence: file:human/ELOVL6/ELOVL6-primary-assessment.md Figure 1D maps ELOVL6's C16-to-C18 step upstream of longer-chain synthesis. Reactome:R-HSA-75876 Saturated and monounsaturated VLCFAs can be synthesized by elongation of palmitic acid synthesized de novo or derived from the diet.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: Protein interactions are supported by the HuRI dataset. Reason: Remove the generic protein-binding annotation because it does not describe a specific molecular function. The interaction evidence and source attribution are retained; this curation action does not assert that the reported association is false. The inspected evidence does not justify an informative replacement function for this particular row. Supporting Evidence: file:human/ELOVL6/ELOVL6-primary-assessment.md IntAct HuRI records verify HMOX1, LCP2 and RTP2 pairings.
GO:0120162 positive regulation of cold-induced thermogenesis	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: ELOVL6-dependent fatty-acid remodeling supports mammalian brown-adipose thermogenic adaptation. Reason: PMID:26628376 is a mouse study: Elovl6 loss prevents the normal cold-induced C18:C16 shift and reduces maximal thermogenic capacity. The enzyme performs lipid-synthesis work supporting adaptation; this is not dismissed as an unspecified knockout consequence. Relative contributions of mitochondrial lipid composition and TFR1 signaling remain unresolved. Retain the ortholog-supported tissue-specific physiological role as non-core, without calling it a direct human experiment. Supporting Evidence: PMID:26628376 the increase in the C18:C16 ratio caused by cold acclimation was almost entirely ablated by deletion of Elovl6. PMID:26628376 Additional work will be needed to elucidate the relative balance of changes in mitochondrial fatty acid composition and the TfR1-ELOVL6 signaling pathway.
GO:0035338 long-chain fatty-acyl-CoA biosynthetic process	TAS Reactome:R-HSA-75876	ACCEPT	Summary: Reactome traceable annotation for synthesis of long-chain/very-long-chain fatty-acyl-CoAs; ELOVL6 produces long-chain (C18) acyl-CoAs. Accurate higher-level process. Reason: ELOVL6 catalyzes the condensation step yielding C18 intermediates and acyl-CoA products after completion of the cycle. These are long-chain species under GO definitions using 13-22 aliphatic-tail carbons. This is direct synthesis work, not an inference that C18 meets the separate very-long-chain product boundary.
GO:0006633 fatty acid biosynthetic process	IEA GO_REF:0000041	ACCEPT	Summary: ELOVL6 catalyzes a step in fatty-acid biosynthesis. Reason: The condensation reaction extends fatty-acyl carbon skeletons and is direct synthesis work. A general pathway term remains correct and core even where a more specific elongation annotation also exists. Supporting Evidence: file:human/ELOVL6/ELOVL6-uniprot.txt Lipid metabolism; fatty acid biosynthesis
GO:0009922 fatty acid elongase activity	TAS Reactome:R-HSA-548814	ACCEPT	Summary: Core molecular function, Reactome-traceable (ELOVL3,6,7 condense palmitoyl-CoA with malonyl-CoA to 3-oxooctadecanoyl-CoA). Correct. Reason: This protein catalyzes the malonyl-CoA-dependent condensation step of the ER fatty-acid elongation cycle. The three later reduction/dehydration/reduction reactions are performed by other enzymes; the elongase annotation correctly identifies the target condensing activity. The source-specific scope is described in the summary and reference review.
GO:0005789 endoplasmic reticulum membrane	EXP PMID:20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingol...	ACCEPT	Summary: ELOVL6 is a multipass endoplasmic-reticulum membrane elongase; this location is supported. Reason: The full human ELOVL comparison in PMID:20937905 reports ER localization for all seven proteins, consistent with the target UniProt membrane topology. A parent membrane/ER term remains a correct description of the core location; breadth and duplicate evidence are not biological contradictions. This does not transfer the fly ELOVL6 mitochondrial location to human. Supporting Evidence: file:human/ELOVL6/ELOVL6-primary-assessment.md Results describe ER localization for all seven proteins
GO:0009922 fatty acid elongase activity	EXP PMID:19575253 Development of a high-density assay for long-chain fatty acy...	ACCEPT	Summary: Direct enzymatic characterization of recombinant human ELOVL6 acyl-CoA elongase activity via the Unifilter GF/C assay, with substrate profiling. Core molecular function. Reason: This protein catalyzes the malonyl-CoA-dependent condensation step of the ER fatty-acid elongation cycle. The three later reduction/dehydration/reduction reactions are performed by other enzymes; the elongase annotation correctly identifies the target condensing activity. The source-specific scope is described in the summary and reference review. Supporting Evidence: PMID:19575253 recombinantly expressed human ELOVLs (i.e., ELOVL1,-2,-3,-5 and -6) displayed appreciable assay windows
GO:0009922 fatty acid elongase activity	EXP PMID:20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingol...	ACCEPT	Summary: Direct in vitro determination of ELOVL6 substrate specificity as part of a systematic characterization of all seven mammalian ELOVLs. Core molecular function. Reason: This protein catalyzes the malonyl-CoA-dependent condensation step of the ER fatty-acid elongation cycle. The three later reduction/dehydration/reduction reactions are performed by other enzymes; the elongase annotation correctly identifies the target condensing activity. The source-specific scope is described in the summary and reference review. Supporting Evidence: PMID:20937905 mammals have seven elongases (ELOVL1-7)
GO:0009922 fatty acid elongase activity	IMP PMID:25003994 Two modes of regulation of the fatty acid elongase ELOVL6 by...	ACCEPT	Summary: Purified ELOVL6 reconstituted into proteoliposomes showed measurable condensing (elongase) activity toward C16:0-CoA (KM 1.22 uM), stimulated by KAR. Direct functional evidence for the core molecular function. Reason: This protein catalyzes the malonyl-CoA-dependent condensation step of the ER fatty-acid elongation cycle. The three later reduction/dehydration/reduction reactions are performed by other enzymes; the elongase annotation correctly identifies the target condensing activity. The source-specific scope is described in the summary and reference review. Supporting Evidence: PMID:25003994 Activity of purified ELOVL6 was enhanced by
GO:0009923 fatty acid elongase complex	IDA PMID:25003994 Two modes of regulation of the fatty acid elongase ELOVL6 by...	ACCEPT	Summary: ELOVL6 functions with KAR in the ER fatty-acid elongation machinery. Reason: Full PMID:25003994 shows purified ELOVL6/KAR co-reconstitution and stimulation of condensation even without KAR catalytic turnover, consistent with functional assembly. The authors explicitly discuss the absence of definitive physical-interaction evidence and possible detergent-micelle artifacts in earlier co-immunoprecipitations. Retain the experimental complex annotation without claiming a resolved binary interface, fixed stoichiometry or proof from colocalization alone. Supporting Evidence: file:human/ELOVL6/ELOVL6-primary-assessment.md KAR co-reconstitution stimulates condensation even without KAR catalysis; active KAR plus NADPH gives additional stimulation.
GO:0009922 fatty acid elongase activity	IGI PMID:26214738 Regulation of mitochondrial morphology and function by stear...	ACCEPT	Summary: Human ELOVL6 expression rescues fly dElovl6 lethality, supporting conserved elongase activity. The fly mutant has reduced C16-to-C18 elongation and C18:0 abundance. Reason: Full PMID:26214738 explicitly tests human ELOVL6 rescue of fly dElovl6 lethality, alongside the fly C16:0-to-C18:0 biochemical defect. This cross-species genetic evidence is appropriate for the conserved elongase/saturated-elongation function; it is not evidence that human ELOVL6 shares the fly protein localization. Supporting Evidence: PMID:26214738 their lethality is rescued by human Elovl6
GO:0019367 fatty acid elongation, saturated fatty acid	IGI PMID:26214738 Regulation of mitochondrial morphology and function by stear...	ACCEPT	Summary: Same cross-species genetic evidence establishes ELOVL6's role in elongating saturated C16:0 to C18:0. Core process annotation. Reason: Full PMID:26214738 explicitly tests human ELOVL6 rescue of fly dElovl6 lethality, alongside the fly C16:0-to-C18:0 biochemical defect. This cross-species genetic evidence is appropriate for the conserved elongase/saturated-elongation function; it is not evidence that human ELOVL6 shares the fly protein localization. Supporting Evidence: PMID:26214738 the enzyme elongating C16 fatty acids to C18
GO:0120162 positive regulation of cold-induced thermogenesis	ISS PMID:26628376 Brown Adipose Tissue Thermogenic Capacity Is Regulated by El...	KEEP AS NON CORE	Summary: ELOVL6-dependent fatty-acid remodeling supports mammalian brown-adipose thermogenic adaptation. Reason: PMID:26628376 is a mouse study: Elovl6 loss prevents the normal cold-induced C18:C16 shift and reduces maximal thermogenic capacity. The enzyme performs lipid-synthesis work supporting adaptation; this is not dismissed as an unspecified knockout consequence. Relative contributions of mitochondrial lipid composition and TFR1 signaling remain unresolved. Retain the ortholog-supported tissue-specific physiological role as non-core, without calling it a direct human experiment. Supporting Evidence: PMID:26628376 the increase in the C18:C16 ratio caused by cold acclimation was almost entirely ablated by deletion of Elovl6. PMID:26628376 Additional work will be needed to elucidate the relative balance of changes in mitochondrial fatty acid composition and the TfR1-ELOVL6 signaling pathway.
GO:0005789 endoplasmic reticulum membrane	TAS Reactome:R-HSA-1655835	ACCEPT	Summary: ELOVL6 is a multipass endoplasmic-reticulum membrane elongase; this location is supported. Reason: The full human ELOVL comparison in PMID:20937905 reports ER localization for all seven proteins, consistent with the target UniProt membrane topology. A parent membrane/ER term remains a correct description of the core location; breadth and duplicate evidence are not biological contradictions. This does not transfer the fly ELOVL6 mitochondrial location to human. Supporting Evidence: file:human/ELOVL6/ELOVL6-primary-assessment.md Results describe ER localization for all seven proteins
GO:0005789 endoplasmic reticulum membrane	TAS Reactome:R-HSA-548814	ACCEPT	Summary: ELOVL6 is a multipass endoplasmic-reticulum membrane elongase; this location is supported. Reason: The full human ELOVL comparison in PMID:20937905 reports ER localization for all seven proteins, consistent with the target UniProt membrane topology. A parent membrane/ER term remains a correct description of the core location; breadth and duplicate evidence are not biological contradictions. This does not transfer the fly ELOVL6 mitochondrial location to human. Supporting Evidence: file:human/ELOVL6/ELOVL6-primary-assessment.md Results describe ER localization for all seven proteins
GO:0005515 protein binding	IPI PMID:20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingol...	REMOVE	Summary: ELOVL6 association with CERS2 was detected in the ELOVL comparison. Reason: Remove the generic protein-binding annotation because it does not describe a specific molecular function. The interaction evidence and source attribution are retained; this curation action does not assert that the reported association is false. The inspected evidence does not justify an informative replacement function for this particular row. Supporting Evidence: file:human/ELOVL6/ELOVL6-primary-assessment.md Results describe ER localization for all seven proteins and CERS2 co-immunoprecipitation with all seven; indirect association remains possible.
GO:0005783 endoplasmic reticulum	IDA PMID:20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingol...	ACCEPT	Summary: ELOVL6 is a multipass endoplasmic-reticulum membrane elongase; this location is supported. Reason: The full human ELOVL comparison in PMID:20937905 reports ER localization for all seven proteins, consistent with the target UniProt membrane topology. A parent membrane/ER term remains a correct description of the core location; breadth and duplicate evidence are not biological contradictions. This does not transfer the fly ELOVL6 mitochondrial location to human. Supporting Evidence: file:human/ELOVL6/ELOVL6-primary-assessment.md Results describe ER localization for all seven proteins
GO:0019367 fatty acid elongation, saturated fatty acid	IDA PMID:20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingol...	ACCEPT	Summary: Direct in vitro evidence that ELOVL6 elongates saturated acyl-CoAs (C16:0 to C18:0). Core process annotation. Reason: Saturated C16:0 and monounsaturated C16:1 elongations are established target capacities. These classes are not mutually exclusive, and relative substrate preference is not a reason to remove a documented lower-activity capacity. Supporting Evidence: PMID:20937905 Very long-chain fatty acids (VLCFAs) exert a variety of cellular functions
GO:0042759 long-chain fatty acid biosynthetic process	IDA PMID:20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingol...	ACCEPT	Summary: Direct experimental evidence that ELOVL6 produces long-chain (C18) fatty acids. Accurate and core; ELOVL6's principal product (C18) is a long-chain fatty acid. Reason: ELOVL6 catalyzes the condensation step yielding C18 intermediates and acyl-CoA products after completion of the cycle. These are long-chain species under GO definitions using 13-22 aliphatic-tail carbons. This is direct synthesis work, not an inference that C18 meets the separate very-long-chain product boundary.

Gene Description

Existing Annotations Review

Core Functions

References

Suggested Questions for Experts

📚 Additional Documentation

Notes

Primary Assessment

📄 View Raw YAML