TECR

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0102758 very-long-chain enoyl-CoA reductase activity	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (PANTHER PTN000059180) propagation of the core VLCFA enoyl-CoA reductase activity. This is the correct and best-supported molecular function for TECR and is directly backed by experimental IDA/IMP annotations (PMID:12482854, PMID:24220030). Supporting Evidence: file:human/TECR/TECR-uniprot.txt This enzyme reduces the trans-2,3-enoyl- file:human/TECR/TECR-uniprot.txt CoA fatty acid intermediate to an acyl-CoA that can be further
GO:0005783 endoplasmic reticulum	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Phylogenetic assignment of ER localization, consistent with experimental IDA evidence (PMID:12482854, PMID:24220030) that TECR is an ER enzyme. The more specific and accurate location is ER membrane; retained as correct but the endoplasmic reticulum membrane term is preferred. Supporting Evidence: file:human/TECR/TECR-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
GO:0006665 sphingolipid metabolic process	IBA GO_REF:0000033	ACCEPT	Summary: TECR participates in sphingolipid metabolism both by supplying VLCFAs used as the acyl chain of sphingolipids and by catalyzing the saturation step of the S1P degradation pathway. Phylogenetic call is consistent with the experimental IMP annotation (PMID:25049234). Core process. Supporting Evidence: PMID:25049234 TER is involved in both the production of VLCFAs used in the fatty acid moiety of sphingolipids as well as in the degradation of the sphingosine moiety of sphingolipids via S1P.
GO:0042761 very long-chain fatty acid biosynthetic process	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic propagation of the VLCFA biosynthetic process, the core biological role of TECR as the fourth-step reductase of the elongation cycle. Directly supported by experimental IDA/IMP (PMID:12482854, PMID:24220030). Core process. Supporting Evidence: file:human/TECR/TECR-uniprot.txt allows the addition of 2
GO:0005789 endoplasmic reticulum membrane	IEA GO_REF:0000044	ACCEPT	Summary: Electronic mapping from the UniProt subcellular-location keyword to ER membrane. Correct and matches experimental IDA/EXP evidence (PMID:12482854, PMID:24220030); TECR is a multi-pass ER membrane protein. Core location. Supporting Evidence: file:human/TECR/TECR-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
GO:0006629 lipid metabolic process	IEA GO_REF:0000002	MARK AS OVER ANNOTATED	Summary: InterPro2GO electronic annotation to a very general lipid metabolism term. Not incorrect but far less informative than the specific VLCFA biosynthetic process and sphingolipid metabolic process terms already annotated. Over-annotated (redundant generalization). Reason: Subsumed by the more specific, experimentally supported biological-process terms (very long-chain fatty acid biosynthetic process, sphingolipid metabolic process).
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors	IEA GO_REF:0000002	MARK AS OVER ANNOTATED	Summary: InterPro2GO electronic annotation to the general CH-CH-donor oxidoreductase parent. Correct branch but a direct is_a parent of the specific, experimentally supported very-long-chain enoyl-CoA reductase activity (GO:0102758). Over-annotated (redundant generalization). Reason: Direct parent of the specific MF term GO:0102758 already annotated with experimental (IDA/IMP) evidence.
GO:0019166 trans-2-enoyl-CoA reductase (NADPH) activity	IEA GO_REF:0000116	ACCEPT	Summary: Rhea-based electronic annotation of the trans-2-enoyl-CoA reductase (NADPH) activity, matching the enzyme's EC 1.3.1.93 catalytic activity and the several Rhea reactions listed in UniProt. Correct molecular function (a parent/sibling of the VLCFA-specific term GO:0102758). Accept. Supporting Evidence: file:human/TECR/TECR-uniprot.txt very-long-chain (2E)-enoyl-CoA + NADPH + H(+); Xref=Rhea:RHEA:14473,
GO:0102758 very-long-chain enoyl-CoA reductase activity	IEA GO_REF:0000120	ACCEPT	Summary: Automated (Rhea/EC) electronic annotation of the core VLCFA enoyl-CoA reductase activity, redundant with and confirmed by the experimental IDA/IMP annotations to the same term. Accept as the core molecular function. Supporting Evidence: file:human/TECR/TECR-uniprot.txt EC=1.3.1.93
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	MARK AS OVER ANNOTATED	Summary: Bare protein binding from a large-scale interactome map (with HACD2 as the recorded partner). The interaction with HACD2 is biologically meaningful (part of the VLCFA elongase complex), but the GO:0005515 term itself is uninformative; the functional detail is captured by the complex/interaction description and by the MF/BP terms. Over-annotated per curation policy. Reason: Uninformative bare protein binding; the meaningful partner (HACD2) is captured in core-function complex membership rather than GO:0005515.
GO:0005515 protein binding	IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma...	MARK AS OVER ANNOTATED	Summary: Bare protein binding from a nuclear histone crosslinking-MS interactome study (recorded partner HACD2). Uninformative term; likely a proximity/XL capture in the large nuclear interactome dataset. Over-annotated per curation policy (not removed, as it is an IPI). Reason: Uninformative bare protein binding from a proteome-scale crosslinking-MS dataset; no specific functional MF is conveyed.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	MARK AS OVER ANNOTATED	Summary: Bare protein binding from the HuRI reference binary interactome (many recorded partners, including HACD1/HACD2 and ELOVL4). Individual Y2H hits are uninformative as a bare GO:0005515; biologically relevant partners are captured in the complex/interaction descriptions. Over-annotated per curation policy. Reason: Uninformative bare protein binding from a high-throughput binary interactome; functional partners captured elsewhere.
GO:0005515 protein binding	IPI PMID:38422897 The 3-hydroxyacyl-CoA dehydratase 1/2 form complex with tran...	MARK AS OVER ANNOTATED	Summary: Bare protein binding underpinned by the biochemically validated HACD1/2 and ELOVL interactions that form the VLCFA elongase machinery. The interaction is real and important, but the GO:0005515 term is uninformative; the specific complex membership (with HACD1/2) is the informative representation and is captured in core functions. Reason: Bare protein binding; the informative content (HACD1/2-TECR complex, ELOVL interactions) is represented via complex membership, not GO:0005515.
GO:0035338 long-chain fatty-acyl-CoA biosynthetic process	TAS Reactome:R-HSA-75876	KEEP AS NON CORE	Summary: Reactome pathway assignment (Synthesis of very long-chain fatty acyl-CoAs) to long-chain fatty-acyl-CoA biosynthesis. Accurate description of the elongation product TECR helps generate; consistent with the fatty acid elongation / VLCFA biosynthesis core processes. Keep as non-core (the more specific VLCFA biosynthetic process is the primary process term). Supporting Evidence: Reactome:R-HSA-75876 reduced with NADPH to yield a fatty acyl-CoA two carbons longer than the starting one.
GO:0006633 fatty acid biosynthetic process	IEA GO_REF:0000041	MARK AS OVER ANNOTATED	Summary: UniPathway-mapping electronic annotation to the general fatty acid biosynthetic process. Correct but subsumed by the more specific, experimentally supported very long-chain fatty acid biosynthetic process. Over-annotated (redundant generalization). Reason: General parent of the specific very long-chain fatty acid biosynthetic process term already annotated experimentally.
GO:0006665 sphingolipid metabolic process	IEA GO_REF:0000041	ACCEPT	Summary: UniPathway-mapping electronic annotation to sphingolipid metabolic process, redundant with and confirmed by the experimental IMP annotation (PMID:25049234). Core process. Supporting Evidence: PMID:25049234 TER is involved in both the production of VLCFAs used in the fatty acid moiety of sphingolipids as well as in the degradation of the sphingosine moiety of sphingolipids via S1P.
GO:0017099 very-long-chain fatty acyl-CoA dehydrogenase activity	TAS Reactome:R-HSA-548831	MODIFY	Summary: Reactome models the TECR-catalyzed reaction (trans-octadec-2-enoyl-CoA + NADPH -> stearoyl-CoA + NADP) in the reverse "dehydrogenate" direction and maps it to a dehydrogenase molecular function. Physiologically TECR is a reductase (NADPH-consuming), catalyzing the fourth reductive step of elongation; the dehydrogenase MF misrepresents the enzyme's biological direction. Modify to the correct reductase MF (GO:0102758). Not removed (TAS; same catalytic activity written in the reverse direction). Reason: Same chemistry as the enzyme's reductase activity but assigned in the reverse (dehydrogenase) direction; the physiological function is NADPH-dependent enoyl-CoA reduction. Proposed replacements: very-long-chain enoyl-CoA reductase activity Supporting Evidence: Reactome:R-HSA-548831 Trans-2,3-enoyl-CoA reductase (TECR) catalyzes the reaction of trans-octadec-2-enoyl-CoA and NADPH + H+ to form stearoyl-CoA and NADP+.
GO:0005783 endoplasmic reticulum	IDA GO_REF:0000052	KEEP AS NON CORE	Summary: Immunofluorescence (HPA) IDA localizing TECR to the endoplasmic reticulum, consistent with all other evidence. Correct; the ER membrane term is the more precise location. Keep (compartment correct). Supporting Evidence: file:human/TECR/TECR-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
GO:0005789 endoplasmic reticulum membrane	EXP PMID:24220030 Mutation for nonsyndromic mental retardation in the trans-2-...	ACCEPT	Summary: Experimental localization of TECR to the ER membrane (the P182L characterization study reported no effect of the variant on subcellular localization, i.e. the enzyme remains ER-membrane resident). Core location. Supporting Evidence: file:human/TECR/TECR-uniprot.txt no effect on subcellular localization;
GO:0102758 very-long-chain enoyl-CoA reductase activity	IDA PMID:12482854 Identification of two mammalian reductases involved in the t...	ACCEPT	Summary: Direct biochemical assay (Moon & Horton 2003) identifying and characterizing TECR/TER as the mammalian trans-2,3-enoyl-CoA reductase of the elongation cascade. This is the primary experimental anchor for the core molecular function. Supporting Evidence: PMID:12482854 the identification and characterization of two mammalian enzymes that catalyze the 3-ketoacyl-CoA and trans-2,3-enoyl-CoA reduction reactions in long and very long chain fatty acid elongation
GO:0005783 endoplasmic reticulum	IDA PMID:24220030 Mutation for nonsyndromic mental retardation in the trans-2-...	KEEP AS NON CORE	Summary: Experimental IDA localization to the ER (P182L characterization study). Correct compartment; the ER membrane term is the more precise location. Keep. Supporting Evidence: file:human/TECR/TECR-uniprot.txt no effect on subcellular localization;
GO:0042761 very long-chain fatty acid biosynthetic process	IMP PMID:24220030 Mutation for nonsyndromic mental retardation in the trans-2-...	ACCEPT	Summary: IMP: the P182L mutant enzyme impairs VLCFA synthesis, demonstrating TECR's requirement in very long-chain fatty acid biosynthesis. Core process. Supporting Evidence: PMID:24220030 thereby impairing VLCFA synthesis
GO:0102758 very-long-chain enoyl-CoA reductase activity	IMP PMID:24220030 Mutation for nonsyndromic mental retardation in the trans-2-...	ACCEPT	Summary: IMP: the disease P182L mutant shows reduced trans-2-enoyl-CoA reductase activity, confirming that TECR enables the VLCFA enoyl-CoA reductase activity. Core molecular function. Supporting Evidence: PMID:24220030 TER P182L mutant enzyme exhibits reduced trans-2-enoyl-CoA reductase activity
GO:0006665 sphingolipid metabolic process	IMP PMID:25049234 Dual functions of the trans-2-enoyl-CoA reductase TER in the...	ACCEPT	Summary: IMP (TER-knockdown HeLa; yeast TSC13 complementation) demonstrating TER's dual involvement in sphingolipid metabolism, including the S1P degradation saturation step. Core process. Supporting Evidence: PMID:25049234 TER is involved in both the production of VLCFAs used in the fatty acid moiety of sphingolipids as well as in the degradation of the sphingosine moiety of sphingolipids via S1P.
GO:0005634 nucleus	HDA PMID:21630459 Proteomic characterization of the human sperm nucleus.	KEEP AS NON CORE	Summary: High-throughput mass-spectrometry detection of TECR in a purified sperm-nucleus proteome catalog. TECR is a multi-pass ER membrane enzyme; this is a proteomics catalog entry, not evidence of a nuclear function. Keep as non-core (not a functional site). Reason: Detection in a large-scale sperm-nuclear proteome catalog; no functional role in the nucleus is implied for this ER membrane enzyme. Supporting Evidence: PMID:21630459 403 different proteins have been identified from the isolated sperm nuclei.
GO:0005789 endoplasmic reticulum membrane	TAS Reactome:R-HSA-548831	ACCEPT	Summary: Reactome TAS localization to the ER membrane, consistent with the experimental evidence. Core location (redundant with the IDA/EXP ER membrane annotations). Supporting Evidence: file:human/TECR/TECR-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
GO:0005789 endoplasmic reticulum membrane	IDA PMID:12482854 Identification of two mammalian reductases involved in the t...	ACCEPT	Summary: Direct experimental localization (Moon & Horton 2003) of TECR to the ER membrane in transfected cells, established alongside the enzymatic characterization. Core location. Supporting Evidence: Reactome:R-HSA-548831 localization to the endoplasmic reticulum membrane was established in studies
GO:0030497 fatty acid elongation	IDA PMID:12482854 Identification of two mammalian reductases involved in the t...	ACCEPT	Summary: Direct experimental evidence that TECR catalyzes the final reductive step of the two-carbon fatty acyl elongation cycle. Core biological process. Supporting Evidence: file:human/TECR/TECR-uniprot.txt Catalyzes the last of the four reactions of
GO:0042761 very long-chain fatty acid biosynthetic process	IDA PMID:12482854 Identification of two mammalian reductases involved in the t...	ACCEPT	Summary: Direct experimental evidence for TECR's role in producing long- and very-long-chain fatty acids via elongation. Core biological process (redundant with the IMP annotation from PMID:24220030). Supporting Evidence: file:human/TECR/TECR-uniprot.txt participates in the production of VLCFAs of different chain

Gene Description

Existing Annotations Review

Core Functions

NADPH-dependent reduction of the trans-2,3-enoyl-CoA (very-long-chain (2E)-enoyl-CoA) intermediate to the fully saturated acyl-CoA, the fourth and final step of the microsomal fatty-acid elongation cycle, occurring at the ER membrane.

Cofactor binding: TECR uses NADPH as the physiological reductant for the enoyl-CoA reduction reaction (NADP(+) is released).

References

📚 Additional Documentation

Notes

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