Elovl7

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005789 endoplasmic reticulum membrane	IBA GO_REF:0000033	ACCEPT	Summary: IBA from the ELOVL family node PTN000125390; ER membrane localization is shared across ELO-family condensing enzymes. Elovl7 is a multi-pass ER membrane protein with a C-terminal di-lysine ER retention motif, and the elongation cycle it initiates is ER-bound; the purified enzyme requires reconstitution into a lipid bilayer for activity. Reason: Previously KEEP_AS_NON_CORE. The ER membrane is the site where Elovl7 performs its core condensing activity, not peripheral context, so it is accepted as the core location (matching the acceptance of the primary localization in other enzyme reviews). Supporting Evidence: UniProtKB:D4ADY9 SUBCELLULAR LOCATION: Endoplasmic reticulum membrane UniProtKB:D4ADY9 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. file:rat/Elovl7/Elovl7-deep-research-falcon.md Mammalian ELOVL7 is a membrane-embedded elongase associated with the endoplasmic reticulum (ER).
GO:0030148 sphingolipid biosynthetic process	IBA GO_REF:0000033	MARK AS OVER ANNOTATED	Summary: This IBA annotation propagates a sphingolipid biosynthesis role across the ELOVL family, but ELOVL7's measured substrate preference argues against a dedicated sphingolipid (ceramide) role for this paralog. Sphingolipids characteristically incorporate very-long-chain fatty acids (C22-C26 and longer), whereas purified ELOVL7 is most active toward C18 acyl-CoAs over a C16-C20 range and shows little or no activity toward C22-C26 saturated acyl-CoAs. The VLCFAs destined for sphingolipid/ceramide synthesis are predominantly produced by other ELOVL paralogs (e.g., ELOVL1/ELOVL4). This is therefore best treated as a family-level over-annotation rather than a specific ELOVL7 function. Reason: The IBA-propagated sphingolipid biosynthesis role does not match ELOVL7's C16-C20 (C18-preferring) substrate specificity; the long-chain substrates characteristic of sphingolipids are elongated mainly by other ELOVL paralogs. Propagation Review Root cause: PROPAGATION BAD Failure modes: WRONG ORTHOLOG OR PARALOG FUNCTIONAL DIVERGENCE Sources checked: PANTHER:PTN000125390 · PANTHER:PTN000125390 SUPPORTS SOURCE BUT NOT TARGET In the current PTHR11157 PAINT slice the GO:0030148 IBD at this deep family node is seeded exclusively by sphingolipid-dedicated members - human ELOVL1 (Q9BW60), a mouse Elovl member, two budding-yeast ELO genes and two Candida CGD entries - with no ELOVL7 ortholog among the seeds. Those members elongate the C22-C26 substrates that sphingolipids incorporate; ELOVL7's measured C16-C20 (C18-preferring) range means the sphingolipid role does not follow for the rat gene, even though the same node correctly anchors the elongase activity and elongation-process IBDs that Elovl7 does inherit (GO:0009922, GO:0019367, GO:0034625, GO:0034626 - the latter three seeded in part by rat RGD members). Supporting Evidence: UniProtKB:D4ADY9 Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. file:rat/Elovl7/Elovl7-deep-research-falcon.md In purified-enzyme assays (reconstituted into proteoliposomes), mammalian ELOVL7 shows activity toward C16–C20 acyl‑CoA substrates, with the highest activity toward C18 substrates, and comparatively little/no activity toward longer saturated substrates (e.g., C22–C26 saturated acyl‑CoAs) under the tested conditions.
GO:0034626 fatty acid elongation, polyunsaturated fatty acid	IBA GO_REF:0000033	ACCEPT	Summary: Elovl7 is a very-long-chain fatty acid elongase 7; the fatty acid elongation, polyunsaturated fatty acid annotation is supported by the fetched UniProt/GOA evidence (IBA, GO_REF:0000033) and represents a core or direct activity/process. Falcon deep research directly corroborates a PUFA elongation role, noting the highest measured activity toward the polyunsaturated C18:3(n-3) and C18:3(n-6) acyl-CoA substrates. Reason: Elovl7 performs the condensing step of this elongation process itself; the substrate class named by the term is among those the enzyme elongates (C16-C20 saturated, monounsaturated and polyunsaturated acyl-CoAs, highest for C18:3). Supporting Evidence: UniProtKB:D4ADY9 Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. file:rat/Elovl7/Elovl7-deep-research-falcon.md In purified-enzyme assays (reconstituted into proteoliposomes), mammalian ELOVL7 shows activity toward C16–C20 acyl‑CoA substrates, with the highest activity toward C18 substrates
GO:0019367 fatty acid elongation, saturated fatty acid	IBA GO_REF:0000033	ACCEPT	Summary: Elovl7 is a very-long-chain fatty acid elongase 7; the fatty acid elongation, saturated fatty acid annotation is supported by the fetched UniProt/GOA evidence (IBA, GO_REF:0000033) and represents a core or direct activity/process. Reason: Elovl7 performs the condensing step of this elongation process itself; the substrate class named by the term is among those the enzyme elongates (C16-C20 saturated, monounsaturated and polyunsaturated acyl-CoAs, highest for C18:3). Supporting Evidence: UniProtKB:D4ADY9 Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. file:rat/Elovl7/Elovl7-deep-research-falcon.md In purified-enzyme assays (reconstituted into proteoliposomes), mammalian ELOVL7 shows activity toward C16–C20 acyl‑CoA substrates, with the highest activity toward C18 substrates
GO:0034625 fatty acid elongation, monounsaturated fatty acid	IBA GO_REF:0000033	ACCEPT	Summary: Elovl7 is a very-long-chain fatty acid elongase 7; the fatty acid elongation, monounsaturated fatty acid annotation is supported by the fetched UniProt/GOA evidence (IBA, GO_REF:0000033) and represents a core or direct activity/process. Reason: Elovl7 performs the condensing step of this elongation process itself; the substrate class named by the term is among those the enzyme elongates (C16-C20 saturated, monounsaturated and polyunsaturated acyl-CoAs, highest for C18:3). Supporting Evidence: UniProtKB:D4ADY9 Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. file:rat/Elovl7/Elovl7-deep-research-falcon.md Review-level synthesis indicates that ELOVL3 and ELOVL7 can elongate saturated and unsaturated C16–C22 acyl‑CoAs, with highest activities toward C18-CoAs
GO:0005783 endoplasmic reticulum	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: The endoplasmic reticulum annotation is plausible for Elovl7 but should be kept as non-core context rather than used to define the gene product function. Reason: Correct but less specific than endoplasmic reticulum membrane (GO:0005789), which is the accepted core location. Supporting Evidence: UniProtKB:D4ADY9 SUBCELLULAR LOCATION: Endoplasmic reticulum membrane UniProtKB:D4ADY9 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.
GO:0005789 endoplasmic reticulum membrane	IEA GO_REF:0000120	ACCEPT	Summary: UniRule/SubCell-based ER membrane assignment for the multi-pass ELO-family condensing enzyme. Elovl7 is a multi-pass ER membrane protein with a C-terminal di-lysine ER retention motif, and the elongation cycle it initiates is ER-bound; the purified enzyme requires reconstitution into a lipid bilayer for activity. Reason: Previously KEEP_AS_NON_CORE. The ER membrane is the site where Elovl7 performs its core condensing activity, not peripheral context, so it is accepted as the core location (matching the acceptance of the primary localization in other enzyme reviews). Supporting Evidence: UniProtKB:D4ADY9 SUBCELLULAR LOCATION: Endoplasmic reticulum membrane UniProtKB:D4ADY9 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. file:rat/Elovl7/Elovl7-deep-research-falcon.md Mammalian ELOVL7 is a membrane-embedded elongase associated with the endoplasmic reticulum (ER).
GO:0006636 unsaturated fatty acid biosynthetic process	IEA GO_REF:0000104	KEEP AS NON CORE	Summary: The unsaturated fatty acid biosynthetic process annotation is plausible for Elovl7 but should be kept as non-core context rather than used to define the gene product function. Reason: Elovl7 elongates unsaturated C18 acyl-CoAs, so it contributes to unsaturated fatty acid biosynthesis, but the elongation-specific child terms (GO:0034625, GO:0034626) are the informative process terms. Supporting Evidence: UniProtKB:D4ADY9 Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. UniProtKB:D4ADY9 Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA.
GO:0008610 lipid biosynthetic process	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: The lipid biosynthetic process annotation is plausible for Elovl7 but should be kept as non-core context rather than used to define the gene product function. Reason: The annotation is compatible with Elovl7 biology but is broader or more contextual than the core molecular function. GOA no longer carries this row (retired). Supporting Evidence: UniProtKB:D4ADY9 FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle.
GO:0009922 fatty acid elongase activity	IEA GO_REF:0000120	ACCEPT	Summary: Elovl7 is a very-long-chain fatty acid elongase 7; the fatty acid elongase activity annotation is supported by the fetched UniProt/GOA evidence (IEA, GO_REF:0000120) and represents a core or direct activity/process. This is the core molecular function. Falcon deep research corroborates that ELOVL7 is the condensing (3-ketoacyl-CoA synthase, EC 2.3.1.199) enzyme catalyzing the first, rate-limiting step of microsomal fatty-acid elongation. Reason: Fatty acid elongase (3-ketoacyl-CoA synthase) activity is the defining activity of Elovl7 and is the core molecular function. Supporting Evidence: UniProtKB:D4ADY9 FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. file:rat/Elovl7/Elovl7-deep-research-falcon.md Biochemical characterization of mammalian ELOVL7 demonstrates that it catalyzes the condensation of an acyl‑CoA (fatty acyl donor) with malonyl‑CoA (two-carbon donor) to yield a 3‑ketoacyl‑CoA
GO:0016020 membrane	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: The membrane annotation is plausible for Elovl7 but should be kept as non-core context rather than used to define the gene product function. Reason: Correct but uninformative parent of the accepted endoplasmic reticulum membrane location. Supporting Evidence: UniProtKB:D4ADY9 SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
GO:0019367 fatty acid elongation, saturated fatty acid	IEA GO_REF:0000120	ACCEPT	Summary: Elovl7 is a very-long-chain fatty acid elongase 7; the fatty acid elongation, saturated fatty acid annotation is supported by the fetched UniProt/GOA evidence (IEA, GO_REF:0000120) and represents a core or direct activity/process. Reason: Elovl7 performs the condensing step of this elongation process itself; the substrate class named by the term is among those the enzyme elongates (C16-C20 saturated, monounsaturated and polyunsaturated acyl-CoAs, highest for C18:3). Supporting Evidence: UniProtKB:D4ADY9 Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. file:rat/Elovl7/Elovl7-deep-research-falcon.md In purified-enzyme assays (reconstituted into proteoliposomes), mammalian ELOVL7 shows activity toward C16–C20 acyl‑CoA substrates, with the highest activity toward C18 substrates
GO:0034625 fatty acid elongation, monounsaturated fatty acid	IEA GO_REF:0000104	ACCEPT	Summary: Elovl7 is a very-long-chain fatty acid elongase 7; the fatty acid elongation, monounsaturated fatty acid annotation is supported by the fetched UniProt/GOA evidence (IEA, GO_REF:0000104) and represents a core or direct activity/process. Reason: Elovl7 performs the condensing step of this elongation process itself; the substrate class named by the term is among those the enzyme elongates (C16-C20 saturated, monounsaturated and polyunsaturated acyl-CoAs, highest for C18:3). Supporting Evidence: UniProtKB:D4ADY9 Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. file:rat/Elovl7/Elovl7-deep-research-falcon.md Review-level synthesis indicates that ELOVL3 and ELOVL7 can elongate saturated and unsaturated C16–C22 acyl‑CoAs, with highest activities toward C18-CoAs
GO:0034626 fatty acid elongation, polyunsaturated fatty acid	IEA GO_REF:0000120	ACCEPT	Summary: Elovl7 is a very-long-chain fatty acid elongase 7; the fatty acid elongation, polyunsaturated fatty acid annotation is supported by the fetched UniProt/GOA evidence (IEA, GO_REF:0000120) and represents a core or direct activity/process. Reason: Elovl7 performs the condensing step of this elongation process itself; the substrate class named by the term is among those the enzyme elongates (C16-C20 saturated, monounsaturated and polyunsaturated acyl-CoAs, highest for C18:3). Supporting Evidence: UniProtKB:D4ADY9 Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. file:rat/Elovl7/Elovl7-deep-research-falcon.md In purified-enzyme assays (reconstituted into proteoliposomes), mammalian ELOVL7 shows activity toward C16–C20 acyl‑CoA substrates, with the highest activity toward C18 substrates
GO:0035338 long-chain fatty-acyl-CoA biosynthetic process	IEA GO_REF:0000104	KEEP AS NON CORE	Summary: The long-chain fatty-acyl-CoA biosynthetic process annotation is plausible for Elovl7 but should be kept as non-core context rather than used to define the gene product function. Reason: Each Elovl7-initiated cycle converts a C16-C20 acyl-CoA into an acyl-CoA two carbons longer, so long-chain acyl-CoA biosynthesis is a fair description of the output, but it is broader than the elongation terms that capture the activity. Supporting Evidence: UniProtKB:D4ADY9 FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. UniProtKB:D4ADY9 Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA.
GO:0042761 very long-chain fatty acid biosynthetic process	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: The very long-chain fatty acid biosynthetic process annotation is plausible for Elovl7 but should be kept as non-core context rather than used to define the gene product function. Reason: GO defines a very long-chain fatty acid as having more than 22 carbons. Elovl7 is most active on C18 substrates and has little or no activity on C22:0-C26:0-CoAs, so its products are mainly C20-C22; it can supply precursors for VLCFA synthesis but is not a major VLCFA-producing elongase. Kept as non-core rather than removed because UniProt states it may contribute to VLCFA production. Supporting Evidence: UniProtKB:D4ADY9 May participate in the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. UniProtKB:D4ADY9 Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. file:rat/Elovl7/Elovl7-deep-research-falcon.md In purified-enzyme assays (reconstituted into proteoliposomes), mammalian ELOVL7 shows activity toward C16–C20 acyl‑CoA substrates, with the highest activity toward C18 substrates
GO:0006633 fatty acid biosynthetic process	IEA GO_REF:0000041	KEEP AS NON CORE	Summary: The fatty acid biosynthetic process annotation is plausible for Elovl7 but should be kept as non-core context rather than used to define the gene product function. Reason: Correct but general (UniPathway mapping); the specific elongation terms are the informative process annotations. Supporting Evidence: UniProtKB:D4ADY9 PATHWAY: Lipid metabolism; fatty acid biosynthesis. UniProtKB:D4ADY9 FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle.
GO:0005789 endoplasmic reticulum membrane	ISO GO_REF:0000121	ACCEPT	Summary: ISO from human ELOVL7 (UniProtKB:A1L3X0). Elovl7 is a multi-pass ER membrane protein with a C-terminal di-lysine ER retention motif, and the elongation cycle it initiates is ER-bound; the purified enzyme requires reconstitution into a lipid bilayer for activity. Reason: Previously KEEP_AS_NON_CORE. The ER membrane is the site where Elovl7 performs its core condensing activity, not peripheral context, so it is accepted as the core location (matching the acceptance of the primary localization in other enzyme reviews). Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:A1L3X0 · ELOVL7 SUPPORTS TRANSFER Human ELOVL7 donor; ER membrane localization of the ELOVL7 condensing enzyme is conserved, and the rat protein carries the same multi-pass topology and C-terminal di-lysine motif. Supporting Evidence: UniProtKB:D4ADY9 SUBCELLULAR LOCATION: Endoplasmic reticulum membrane UniProtKB:D4ADY9 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. file:rat/Elovl7/Elovl7-deep-research-falcon.md Mammalian ELOVL7 is a membrane-embedded elongase associated with the endoplasmic reticulum (ER).
GO:0009922 fatty acid elongase activity	ISO GO_REF:0000121	ACCEPT	Summary: Elovl7 is a very-long-chain fatty acid elongase 7; the fatty acid elongase activity annotation is supported by the fetched UniProt/GOA evidence (ISO, GO_REF:0000121) and represents a core or direct activity/process. Reason: Orthology transfer from human ELOVL7 (UniProtKB:A1L3X0), whose condensing activity was characterized biochemically; the rat protein is a 1:1 ortholog with the same ELO-family catalytic architecture. Supporting Evidence: UniProtKB:D4ADY9 FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. UniProtKB:D4ADY9 Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs.
GO:0019367 fatty acid elongation, saturated fatty acid	ISO GO_REF:0000121	ACCEPT	Summary: Elovl7 is a very-long-chain fatty acid elongase 7; the fatty acid elongation, saturated fatty acid annotation is supported by the fetched UniProt/GOA evidence (ISO, GO_REF:0000121) and represents a core or direct activity/process. Reason: Elovl7 performs the condensing step of this elongation process itself; the substrate class named by the term is among those the enzyme elongates (C16-C20 saturated, monounsaturated and polyunsaturated acyl-CoAs, highest for C18:3). Supporting Evidence: UniProtKB:D4ADY9 Also active toward C20:4-, C18:0-, C18:1-, C18:2- and C16:0-CoAs, and weakly toward C20:0-CoA. file:rat/Elovl7/Elovl7-deep-research-falcon.md In purified-enzyme assays (reconstituted into proteoliposomes), mammalian ELOVL7 shows activity toward C16–C20 acyl‑CoA substrates, with the highest activity toward C18 substrates
GO:0005783 endoplasmic reticulum	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: The endoplasmic reticulum annotation is plausible for Elovl7 but should be kept as non-core context rather than used to define the gene product function. Reason: Correct but less specific than endoplasmic reticulum membrane (GO:0005789), which is the accepted core location. Supporting Evidence: UniProtKB:D4ADY9 SUBCELLULAR LOCATION: Endoplasmic reticulum membrane UniProtKB:D4ADY9 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.
GO:0034626 fatty acid elongation, polyunsaturated fatty acid	ISO GO_REF:0000121	ACCEPT	Summary: Elovl7 is a very-long-chain fatty acid elongase 7; the fatty acid elongation, polyunsaturated fatty acid annotation is supported by the fetched UniProt/GOA evidence (ISO, GO_REF:0000121) and represents a core or direct activity/process. Reason: Elovl7 performs the condensing step of this elongation process itself; the substrate class named by the term is among those the enzyme elongates (C16-C20 saturated, monounsaturated and polyunsaturated acyl-CoAs, highest for C18:3). Supporting Evidence: UniProtKB:D4ADY9 Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs. file:rat/Elovl7/Elovl7-deep-research-falcon.md In purified-enzyme assays (reconstituted into proteoliposomes), mammalian ELOVL7 shows activity toward C16–C20 acyl‑CoA substrates, with the highest activity toward C18 substrates
GO:0042761 very long-chain fatty acid biosynthetic process	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: The very long-chain fatty acid biosynthetic process annotation is plausible for Elovl7 but should be kept as non-core context rather than used to define the gene product function. Reason: GO defines a very long-chain fatty acid as having more than 22 carbons. Elovl7 is most active on C18 substrates and has little or no activity on C22:0-C26:0-CoAs, so its products are mainly C20-C22; it can supply precursors for VLCFA synthesis but is not a major VLCFA-producing elongase. Kept as non-core rather than removed because UniProt states it may contribute to VLCFA production. Supporting Evidence: UniProtKB:D4ADY9 May participate in the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. UniProtKB:D4ADY9 Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. file:rat/Elovl7/Elovl7-deep-research-falcon.md In purified-enzyme assays (reconstituted into proteoliposomes), mammalian ELOVL7 shows activity toward C16–C20 acyl‑CoA substrates, with the highest activity toward C18 substrates
GO:0009922 fatty acid elongase activity	IBA GO_REF:0000033	ACCEPT	Summary: IBA from the ELOVL family node PTN000125390, seeded by experimentally characterized ELOVL members across animals, fungi and plants, including human ELOVL7 (UniProtKB:A1L3X0). Fatty acid elongase (3-ketoacyl-CoA synthase) activity is the ancestral and conserved activity of the ELO family, and rat Elovl7 is a canonical member. Reason: Core conserved activity; the node placement is sound and there is no evidence of divergence in rat Elovl7. Supporting Evidence: UniProtKB:D4ADY9 FUNCTION: Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. UniProtKB:D4ADY9 Condensing enzyme with higher activity toward C18 acyl-CoAs, especially C18:3(n-3) acyl-CoAs and C18:3(n-6)-CoAs.
GO:0042761 very long-chain fatty acid biosynthetic process	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: IBA from the ELOVL family node PTN000125390. VLCFA (more than 22 carbons) biosynthesis is the ancestral role of the ELO family, but ELOVL7 itself is C18-preferring with little or no activity on C22:0-C26:0-CoAs. Reason: Consistent with the IEA and ISO rows for the same term. The family-level assertion is not wrong for Elovl7, which can feed precursors into VLCFA synthesis, but its own products are mainly C20-C22, so VLCFA biosynthesis is not its core process. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000125390 · PANTHER:PTN000125390 SUPPORTS TRANSFER ELO-family node whose seeds include VLCFA-producing elongases; the term transfers to Elovl7 only as a contributory, non-core process given its C16-C20 substrate range. Supporting Evidence: UniProtKB:D4ADY9 May participate in the production of saturated and polyunsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. UniProtKB:D4ADY9 Little or no activity toward C22:0-, C24:0-, or C26:0-CoAs. file:rat/Elovl7/Elovl7-deep-research-falcon.md In purified-enzyme assays (reconstituted into proteoliposomes), mammalian ELOVL7 shows activity toward C16–C20 acyl‑CoA substrates, with the highest activity toward C18 substrates

Gene Description

Existing Annotations Review

Core Functions

ER membrane fatty acid elongase (3-ketoacyl-CoA synthase) that catalyzes the rate-limiting condensation step of the microsomal elongation cycle, preferring C18 acyl-CoAs (especially C18:3) and elongating saturated, monounsaturated and polyunsaturated C16-C20 substrates.

References

Deep Research

Falcon

📚 Additional Documentation

Notes

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