ELOVL2 is a multipass endoplasmic-reticulum membrane enzyme that catalyzes the malonyl-CoA-dependent condensation step of fatty-acid elongation. It preferentially elongates C20 and C22 polyunsaturated acyl-CoAs in the omega-3 and omega-6 pathways, including formation of C24 precursors for docosahexaenoic acid synthesis through the Sprecher pathway. Separate reductase and dehydratase enzymes complete each two-carbon elongation cycle. ELOVL2-dependent polyunsaturated acyl chains contribute to membrane lipids, including specialized sphingolipids in mammalian testis, and support retinal and reproductive physiology.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005789 endoplasmic reticulum membrane | IBA GO_REF:0000033 | ACCEPT | Summary: ELOVL2 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 ELOVL2 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/ELOVL2/ELOVL2-primary-assessment.md Results describe ER localization for all seven proteins file:human/ELOVL2/ELOVL2-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: Fatty acid elongase activity is the core molecular function of ELOVL2 (the condensation step of the elongation cycle, EC 2.3.1.199). The IBA assignment agrees with direct experimental evidence and with UniProt. 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 ELOVL2 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/ELOVL2/ELOVL2-uniprot.txt Catalyzes the first and rate-limiting reaction of the four file:human/ELOVL2/ELOVL2-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 | ACCEPT | Summary: ELOVL2 catalyzes polyunsaturated chain elongation that yields C24 products. Reason: Human ELOVL2 catalyzes C22-to-C24 PUFA elongation as well as C20-to-C22 (PMID:12371743). C24 products meet GO:0042761, whose definition requires more than 22 carbons in the aliphatic tail; C22 alone would not. The previous C22-C24 shorthand obscured this boundary. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000125390 SUPPORTS TRANSFER Actual PTHR11157 tree places human ELOVL2 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:12371743 22:4n-6 to 24:4n-6 file:human/ELOVL2/ELOVL2-primary-assessment.md C18 alone does not establish a VLCFA product; C24 clearly qualifies. |
| GO:0030148 sphingolipid biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: ELOVL2 supplies polyunsaturated acyl-chain precursors used in sphingolipid synthesis. Reason: The target inherits the positive PTN000125390 assertion. PUFA preference is compatible with sphingolipid synthesis: mammalian testis contains VLC-PUFA-bearing ceramides, and PMID:38485951 connects ELOVL2-dependent elongation to this route while distinguishing the subsequent CerS3 acyl-transfer step. This is conserved pathway participation, not a claim that ELOVL2 catalyzes ceramide synthesis or that the AdipoR2 knockout is an ELOVL2-only assay. Full PMID:20937905 also reports CERS2 association with all seven ELOVLs; its ELOVL1-focused functional result does not exclude ELOVL2. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000125390 SUPPORTS TRANSFER Actual PTHR11157 tree places human ELOVL2 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:38485951 FA elongation by elongases (such as ELOVL2, ELOVL4, and ELOVL5) file:human/ELOVL2/ELOVL2-primary-assessment.md ELOVL2 catalyzes synthesis of acyl-chain precursors, rather than being a passive substrate of ceramide synthesis. |
| GO:0034626 fatty acid elongation, polyunsaturated fatty acid | IBA GO_REF:0000033 | ACCEPT | Summary: ELOVL2 preferentially elongates polyunsaturated fatty acyl-CoAs, so "fatty acid elongation, polyunsaturated fatty acid" is a correct and specific core process. Also supported by direct experimental evidence (IDA). Reason: Human ELOVL2 expression directly supports C20/C22 polyunsaturated elongation (PMID:12371743); full PMID:20937905 assays corroborate strong C20:4-CoA elongation. Polyunsaturated means at least two carbon-carbon double bonds; preference does not by itself establish absence of other substrate classes. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000125390 SUPPORTS TRANSFER Actual PTHR11157 tree places human ELOVL2 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/ELOVL2/ELOVL2-uniprot.txt polyunsaturated very long chain fatty acid (C20- and C22-PUFA) file:human/ELOVL2/ELOVL2-primary-assessment.md Both targets descend from PTN000125390; donor count and target self-inclusion are not objections. |
| GO:0019367 fatty acid elongation, saturated fatty acid | IBA GO_REF:0000033 | UNDECIDED | Summary: ELOVL2 saturated elongation remains unresolved against the positive inherited/family assertion. Reason: The actual human target descends from the positive ancestral IBD. Full PMID:20937905 Figure 1B shows no significant ELOVL2 signal over vector for tested saturated C16-C26 substrates or C18:1, in contrast to strong C20:4 activity. This is a concrete target-specific assay limitation, but a finite panel, especially one monounsaturated substrate, does not establish universal loss across each substrate class. PMID:19575253 reports preference, not categorical exclusion; its full tables remain inaccessible. A focused neutral review is requested before deciding whether the ancestral class-level capacity should be retained or rejected. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN000125390 UNRESOLVED The target actually descends from the positive PTN000125390 assertion. Human substrate-panel results raise a specific capacity question; neither donor count nor PUFA preference alone resolves whether this ancestral activity was retained. Supporting Evidence: file:human/ELOVL2/ELOVL2-primary-assessment.md ELOVL2 has no significant signal above vector on the tested saturated C16-C26 or C18:1 substrates; the finite panel cannot exclude every substrate or condition. PMID:19575253 preferentially elongated the polyunsaturated fatty acyl-CoAs |
| GO:0034625 fatty acid elongation, monounsaturated fatty acid | IBA GO_REF:0000033 | UNDECIDED | Summary: ELOVL2 monounsaturated elongation remains unresolved against the positive inherited/family assertion. Reason: The actual human target descends from the positive ancestral IBD. Full PMID:20937905 Figure 1B shows no significant ELOVL2 signal over vector for tested saturated C16-C26 substrates or C18:1, in contrast to strong C20:4 activity. This is a concrete target-specific assay limitation, but a finite panel, especially one monounsaturated substrate, does not establish universal loss across each substrate class. PMID:19575253 reports preference, not categorical exclusion; its full tables remain inaccessible. A focused neutral review is requested before deciding whether the ancestral class-level capacity should be retained or rejected. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN000125390 UNRESOLVED The target actually descends from the positive PTN000125390 assertion. Human substrate-panel results raise a specific capacity question; neither donor count nor PUFA preference alone resolves whether this ancestral activity was retained. Supporting Evidence: file:human/ELOVL2/ELOVL2-primary-assessment.md ELOVL2 has no significant signal above vector on the tested saturated C16-C26 or C18:1 substrates; the finite panel cannot exclude every substrate or condition. PMID:19575253 preferentially elongated the polyunsaturated fatty acyl-CoAs |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000002 | ACCEPT | Summary: ELOVL2 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/ELOVL2/ELOVL2-primary-assessment.md Results describe ER localization for all seven proteins |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000120 | ACCEPT | Summary: ELOVL2 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/ELOVL2/ELOVL2-primary-assessment.md Results describe ER localization for all seven proteins |
| GO:0006636 unsaturated fatty acid biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: ELOVL2 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. Supporting Evidence: file:human/ELOVL2/ELOVL2-uniprot.txt Lipid metabolism; polyunsaturated fatty acid biosynthesis. |
| GO:0009922 fatty acid elongase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Correct core molecular function (EC 2.3.1.199 / RHEA:32727), redundant with the experimental EXP/IDA annotations. 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: file:human/ELOVL2/ELOVL2-uniprot.txt EC=2.3.1.199 |
| GO:0016020 membrane | IEA GO_REF:0000120 | ACCEPT | Summary: ELOVL2 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/ELOVL2/ELOVL2-primary-assessment.md Results describe ER localization for all seven proteins |
| GO:0019367 fatty acid elongation, saturated fatty acid | IEA GO_REF:0000002 | UNDECIDED | Summary: ELOVL2 saturated elongation remains unresolved against the positive inherited/family assertion. Reason: The actual human target descends from the positive ancestral IBD. Full PMID:20937905 Figure 1B shows no significant ELOVL2 signal over vector for tested saturated C16-C26 substrates or C18:1, in contrast to strong C20:4 activity. This is a concrete target-specific assay limitation, but a finite panel, especially one monounsaturated substrate, does not establish universal loss across each substrate class. PMID:19575253 reports preference, not categorical exclusion; its full tables remain inaccessible. A focused neutral review is requested before deciding whether the ancestral class-level capacity should be retained or rejected. Supporting Evidence: file:human/ELOVL2/ELOVL2-primary-assessment.md ELOVL2 has no significant signal above vector on the tested saturated C16-C26 or C18:1 substrates; the finite panel cannot exclude every substrate or condition. PMID:19575253 preferentially elongated the polyunsaturated fatty acyl-CoAs |
| GO:0030497 fatty acid elongation | IEA GO_REF:0000117 | ACCEPT | Summary: ELOVL2 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. Supporting Evidence: file:human/ELOVL2/ELOVL2-uniprot.txt reactions that constitute the long-chain fatty acids elongation cycle. |
| GO:0034626 fatty acid elongation, polyunsaturated fatty acid | IEA GO_REF:0000120 | ACCEPT | Summary: Correct core process; redundant with the experimental IDA annotations of the same term. Reason: Human ELOVL2 expression directly supports C20/C22 polyunsaturated elongation (PMID:12371743); full PMID:20937905 assays corroborate strong C20:4-CoA elongation. Polyunsaturated means at least two carbon-carbon double bonds; preference does not by itself establish absence of other substrate classes. Supporting Evidence: file:human/ELOVL2/ELOVL2-uniprot.txt polyunsaturated very long chain fatty acid (C20- and C22-PUFA) |
| GO:0042761 very long-chain fatty acid biosynthetic process | IEA GO_REF:0000120 | ACCEPT | Summary: ELOVL2 catalyzes polyunsaturated chain elongation that yields C24 products. Reason: Human ELOVL2 catalyzes C22-to-C24 PUFA elongation as well as C20-to-C22 (PMID:12371743). C24 products meet GO:0042761, whose definition requires more than 22 carbons in the aliphatic tail; C22 alone would not. The previous C22-C24 shorthand obscured this boundary. Supporting Evidence: PMID:12371743 22:4n-6 to 24:4n-6 file:human/ELOVL2/ELOVL2-primary-assessment.md C18 alone does not establish a VLCFA product; C24 clearly qualifies. |
| 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/ELOVL2/ELOVL2-primary-assessment.md The IntAct HuRI records verify FXYD6, IFITM3, MALL and TMEM218 pairings. |
| GO:0035338 long-chain fatty-acyl-CoA biosynthetic process | TAS Reactome:R-HSA-75876 | ACCEPT | Summary: ELOVL2 directly performs long-chain fatty-acyl-CoA biosynthesis. Reason: Its C20-to-C22 PUFA cycle produces long-chain acyl-CoAs within the live GO:0035338 boundary of 13-22 aliphatic-tail carbons. C22-to-C24 elongation separately supplies very-long-chain products. Both pathway scopes can apply; this is direct chemical synthesis, not a merely downstream consequence. Supporting Evidence: PMID:12371743 the conversion of 20:4n-6 to 22:4n-6 file:human/ELOVL2/ELOVL2-primary-assessment.md GO:0035338 and GO:0042759 use 13-22 tail carbons for long-chain species. |
| GO:0036109 alpha-linolenic acid metabolic process | TAS Reactome:R-HSA-2046106 | ACCEPT | Summary: ELOVL2 performs elongation steps within alpha-linolenic-acid-derived omega-3 metabolism. Reason: Reactome R-HSA-2046106 explicitly includes 20:5(n-3)-to-22:5(n-3)-to-24:5(n-3) synthesis in the ALA pathway; human ELOVL2 performs these steps (PMID:12371743). Direct use of free ALA is not required for participation in its multistep metabolic pathway. The live GO definition misdescribes ALA as omega-6/C18H32O2; source ID and label are preserved, while the biological interpretation follows ALA/omega-3 chemistry. Supporting Evidence: Reactome:R-HSA-2046106 18:3(n-3)--> 18:4(n-3)-->20:4(n-3)-->20:5(n-3)-->22:5(n-3)-->24:5(n-3)-->24:6(n-3)-->22:6(n-3). PMID:12371743 20:5n-3 to 22:5n-3 |
| GO:0043651 linoleic acid metabolic process | TAS Reactome:R-HSA-2046105 | ACCEPT | Summary: ELOVL2 performs elongation steps within linoleic-acid-derived omega-6 metabolism. Reason: Reactome R-HSA-2046105 places the C20:4-to-C22:4-to-C24:4 reactions in the linoleic acid pathway; human ELOVL2 catalyzes those elongations. The enzyme does actual synthesis work in the pathway despite not being the first enzyme acting on free dietary linoleate. Supporting Evidence: Reactome:R-HSA-2046105 20:3(n-6)-->20:4(n-6)-->22:4(n-6)-->24:4(n-6)-->24:5(n-6)-->22:5(n-6). PMID:12371743 22:4n-6 to 24:4n-6 |
| GO:0009922 fatty acid elongase activity | EXP PMID:10970790 Cloning of a human cDNA encoding a novel enzyme involved in ... | ACCEPT | Summary: Fatty-acid elongase activity is independently established for human ELOVL2; exact scope of this older source remains incompletely verified. Reason: PMID:10970790 foregrounds the 299-residue HELO1 clone. Its accessible abstract does not establish the scope of all full-text experiments or the basis of this Reactome EXP assertion. The prior confident WRONG_IDENTIFIER judgment is withdrawn rather than inferring misattribution from the abstract. The molecular function itself is directly supported for ELOVL2 by PMID:12371743 and PMID:20937905. Supporting Evidence: PMID:12371743 The open reading frame of the human clone (ELOVL2) encodes a 296-amino acid peptide |
| GO:0009922 fatty acid elongase activity | TAS Reactome:R-HSA-2046083 | ACCEPT | Summary: Reactome TAS for the elongase condensation reaction (elongation of arachidonyl-CoA). Correct core molecular function; redundant with the experimental annotations. 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: file:human/ELOVL2/ELOVL2-uniprot.txt EC=2.3.1.199 |
| GO:0009922 fatty acid elongase activity | TAS Reactome:R-HSA-2046090 | ACCEPT | Summary: Reactome TAS for an ELOVL2 elongation reaction (docosapentaenoyl-CoA -> tetracosapentaenoyl-CoA). Correct core molecular function; redundant with the experimental annotations. 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: file:human/ELOVL2/ELOVL2-uniprot.txt EC=2.3.1.199 |
| GO:0009922 fatty acid elongase activity | TAS Reactome:R-HSA-2046095 | ACCEPT | Summary: Reactome TAS for an ELOVL2 elongation reaction (docosatetraenoyl-CoA -> tetracosatetraenoyl-CoA). Correct core molecular function; redundant with the experimental annotations. 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: file:human/ELOVL2/ELOVL2-uniprot.txt EC=2.3.1.199 |
| GO:0009922 fatty acid elongase activity | TAS Reactome:R-HSA-2046100 | ACCEPT | Summary: Reactome TAS for an ELOVL2 elongation reaction (eicosapentaenoyl-CoA -> docosapentaenoyl-CoA). Correct core molecular function; redundant with the experimental annotations. 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: file:human/ELOVL2/ELOVL2-uniprot.txt EC=2.3.1.199 |
| GO:0005789 endoplasmic reticulum membrane | EXP PMID:20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingol... | ACCEPT | Summary: ELOVL2 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/ELOVL2/ELOVL2-primary-assessment.md Results describe ER localization for all seven proteins |
| GO:0009922 fatty acid elongase activity | EXP PMID:11734209 Activity of human Delta5 and Delta6 desaturases on multiple ... | ACCEPT | Summary: Human ELOVL2 elongase activity is established; this coexpression paper has limited accessible construct detail. Reason: PMID:11734209 describes sequential PUFA elongations in yeast coexpressing human elongase/desaturase genes, but the abstract does not identify every construct. It is inappropriate to infer the exact ELOVL2 assay merely from product chain length. Retain the curator assertion for the independently established activity, with this source-specific limitation. Supporting Evidence: PMID:11734209 Yeast co-expressing human elongase and desaturase genes PMID:12371743 The open reading frame of the human clone (ELOVL2) encodes a 296-amino acid peptide |
| GO:0009922 fatty acid elongase activity | EXP PMID:19575253 Development of a high-density assay for long-chain fatty acy... | ACCEPT | Summary: Experimental support: comprehensive substrate profiling showed ELOVL2 (and ELOVL5) preferentially elongated polyunsaturated fatty acyl-CoAs. Correct 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 preferentially elongated the polyunsaturated 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: Experimental support: Ohno et al. determined the precise substrate specificities of all ELOVLs (including ELOVL2) by in-vitro elongase assays. Correct 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 we determined the precise substrate specificities of all the |
| GO:0005515 protein binding | IPI PMID:38422897 The 3-hydroxyacyl-CoA dehydratase 1/2 form complex with tran... | UNDECIDED | Summary: The curated ELOVL2-TECR interaction is compatible with the elongation machinery. Reason: The curated interaction is not contradicted, but the accessible evidence does not expose the target-specific assay needed to choose a more informative molecular function. Leave this row unresolved pending source inspection; generic protein binding is not accepted as a functional synthesis, and lack of accessible assay detail is not evidence that the interaction is false. Supporting Evidence: file:human/ELOVL2/ELOVL2-uniprot.txt Interacts with TECR |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-2046083 | ACCEPT | Summary: ELOVL2 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/ELOVL2/ELOVL2-primary-assessment.md Results describe ER localization for all seven proteins |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-2046088 | ACCEPT | Summary: ELOVL2 is a multipass endoplasmic-reticulum membrane elongase; this location is supported. Reason: The cached Reactome reaction summary names ELOVL5 for the associated C18-PUFA step, so it is not direct proof that ELOVL2 catalyzes that reaction. The asserted term here is ER-membrane localization, independently established for ELOVL2 in full PMID:20937905. Retain the correct location and flag the reaction-context limitation without manufacturing a catalytic annotation. Supporting Evidence: file:human/ELOVL2/ELOVL2-primary-assessment.md Results describe ER localization for all seven proteins |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-2046090 | ACCEPT | Summary: ELOVL2 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/ELOVL2/ELOVL2-primary-assessment.md Results describe ER localization for all seven proteins |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-2046094 | ACCEPT | Summary: ELOVL2 is a multipass endoplasmic-reticulum membrane elongase; this location is supported. Reason: The cached Reactome reaction summary names ELOVL5 for the associated C18-PUFA step, so it is not direct proof that ELOVL2 catalyzes that reaction. The asserted term here is ER-membrane localization, independently established for ELOVL2 in full PMID:20937905. Retain the correct location and flag the reaction-context limitation without manufacturing a catalytic annotation. Supporting Evidence: file:human/ELOVL2/ELOVL2-primary-assessment.md Results describe ER localization for all seven proteins |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-2046095 | ACCEPT | Summary: ELOVL2 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/ELOVL2/ELOVL2-primary-assessment.md Results describe ER localization for all seven proteins |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-2046100 | ACCEPT | Summary: ELOVL2 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/ELOVL2/ELOVL2-primary-assessment.md Results describe ER localization for all seven proteins |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-548800 | ACCEPT | Summary: ELOVL2 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/ELOVL2/ELOVL2-primary-assessment.md Results describe ER localization for all seven proteins |
| GO:0034626 fatty acid elongation, polyunsaturated fatty acid | IDA PMID:20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingol... | ACCEPT | Summary: Direct experimental evidence (in-vitro substrate specificity of ELOVLs) for ELOVL2 involvement in polyunsaturated fatty acid elongation. Correct core process. Reason: Human ELOVL2 expression directly supports C20/C22 polyunsaturated elongation (PMID:12371743); full PMID:20937905 assays corroborate strong C20:4-CoA elongation. Polyunsaturated means at least two carbon-carbon double bonds; preference does not by itself establish absence of other substrate classes. Supporting Evidence: PMID:20937905 we determined the precise substrate specificities of all the |
| 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: ELOVL2 catalyzes polyunsaturated chain elongation that yields C24 products. Reason: Human ELOVL2 catalyzes C22-to-C24 PUFA elongation as well as C20-to-C22 (PMID:12371743). C24 products meet GO:0042761, whose definition requires more than 22 carbons in the aliphatic tail; C22 alone would not. The previous C22-C24 shorthand obscured this boundary. Supporting Evidence: PMID:12371743 22:4n-6 to 24:4n-6 file:human/ELOVL2/ELOVL2-primary-assessment.md C18 alone does not establish a VLCFA product; C24 clearly qualifies. |
| GO:0005515 protein binding | IPI PMID:20937905 ELOVL1 production of C24 acyl-CoAs is linked to C24 sphingol... | REMOVE | Summary: ELOVL2 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/ELOVL2/ELOVL2-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: ELOVL2 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/ELOVL2/ELOVL2-primary-assessment.md Results describe ER localization for all seven proteins |
| GO:0009922 fatty acid elongase activity | IDA PMID:12371743 Identification and expression of mammalian long-chain PUFA e... | ACCEPT | Summary: Direct experimental evidence: yeast expression of the human ELOVL2 ORF elongated 20- and 22-carbon PUFA (20:4n-6->22:4n-6, 22:4n-6->24:4n-6, 20:5n-3->22:5n-3, 22:5n-3->24:5n-3). This is the defining core molecular function of ELOVL2. 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:12371743 the conversion of 20:4n-6 to 22:4n-6, 22:4n-6 to 24:4n-6, 20:5n-3 to 22:5n-3, |
| GO:0034626 fatty acid elongation, polyunsaturated fatty acid | IDA PMID:12371743 Identification and expression of mammalian long-chain PUFA e... | ACCEPT | Summary: Direct experimental evidence that ELOVL2 elongates 20- and 22-carbon polyunsaturated fatty acids. Correct core process. Reason: Human ELOVL2 expression directly supports C20/C22 polyunsaturated elongation (PMID:12371743); full PMID:20937905 assays corroborate strong C20:4-CoA elongation. Polyunsaturated means at least two carbon-carbon double bonds; preference does not by itself establish absence of other substrate classes. Supporting Evidence: PMID:12371743 involved in the elongation of both 20- and 22-carbon long-chain PUFA |
| GO:0042761 very long-chain fatty acid biosynthetic process | IDA PMID:12371743 Identification and expression of mammalian long-chain PUFA e... | ACCEPT | Summary: ELOVL2 catalyzes polyunsaturated chain elongation that yields C24 products. Reason: Human ELOVL2 catalyzes C22-to-C24 PUFA elongation as well as C20-to-C22 (PMID:12371743). C24 products meet GO:0042761, whose definition requires more than 22 carbons in the aliphatic tail; C22 alone would not. The previous C22-C24 shorthand obscured this boundary. Supporting Evidence: PMID:12371743 22:4n-6 to 24:4n-6 file:human/ELOVL2/ELOVL2-primary-assessment.md C18 alone does not establish a VLCFA product; C24 clearly qualifies. |
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Download this section (compressed HTML)Q: Do full quantitative human ELOVL2 assays or well-resolved ortholog data support saturated or monounsaturated elongation outside the finite negative panel in PMID:20937905 Figure 1B? Resolve retained ancestral capacity versus target-specific loss without treating substrate preference as exclusivity.
Q: Can GO:0036109 be corrected to describe alpha-linolenic acid as omega-3 C18H30O2, rather than the current omega-6/C18H32O2 text? The source term ID/label and ALA-pathway annotation are retained.
Q: Can curator/full-text follow-up clarify the exact ELOVL2 experimental basis for PMID:10970790 and PMID:11734209 and the ELOVL5 reaction-context location rows? Independent ELOVL2 activity/localization remains well supported.
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