Gsta2

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005829 cytosol	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: cytosol is retained as useful context for Gsta2, but it is not the defining core function (IBA, GO_REF:0000033). Reason: cytosol records where Gsta2 has been observed, but localization does not define the gene product's primary activity. Supporting Evidence: UniProtKB:P04903 SUBCELLULAR LOCATION: Cytoplasm. file:rat/Gsta2/Gsta2-deep-research-falcon.md Alpha-class GSTs, including GSTA2-like proteins, belong to the cytosolic GST family (distinct from microsomal and mitochondrial GSTs), indicating a primarily cytosolic intracellular site of action.
GO:0004364 glutathione transferase activity	IBA GO_REF:0000033	ACCEPT	Summary: Gsta2's glutathione conjugation of electrophilic endogenous and xenobiotic substrates supports retaining glutathione transferase activity as a direct annotation (IBA, GO_REF:0000033). Reason: glutathione transferase activity is a specific catalytic activity matching Gsta2's documented role in glutathione conjugation of electrophilic endogenous and xenobiotic substrates. Supporting Evidence: UniProtKB:P04903 Reaction=RX + glutathione = an S-substituted glutathione + a halide anion + H(+) file:rat/Gsta2/Gsta2-deep-research-falcon.md Cytosolic glutathione S-transferases (GSTs) are multifunctional detoxification enzymes whose canonical reaction is conjugation of reduced glutathione (GSH) to electrophilic xenobiotic and endogenous substrates, increasing solubility and facilitating downstream excretion (e.g., via mercapturic acid pathways).
GO:0006749 glutathione metabolic process	IBA GO_REF:0000033	ACCEPT	Summary: Gsta2's glutathione conjugation of electrophilic endogenous and xenobiotic substrates supports retaining glutathione metabolic process as a direct annotation (IBA, GO_REF:0000033). Reason: glutathione metabolic process is a direct metabolic process expected from Gsta2's documented role in glutathione conjugation of electrophilic endogenous and xenobiotic substrates. Supporting Evidence: UniProtKB:P04903 Reaction=RX + glutathione = an S-substituted glutathione + a halide anion + H(+) file:rat/Gsta2/Gsta2-deep-research-falcon.md Cytosolic glutathione S-transferases (GSTs) are multifunctional detoxification enzymes whose canonical reaction is conjugation of reduced glutathione (GSH) to electrophilic xenobiotic and endogenous substrates, increasing solubility and facilitating downstream excretion (e.g., via mercapturic acid pathways).
GO:0006805 xenobiotic metabolic process	IBA GO_REF:0000033	ACCEPT	Summary: Gsta2's glutathione conjugation of electrophilic endogenous and xenobiotic substrates supports retaining xenobiotic metabolic process as a direct annotation (IBA, GO_REF:0000033). Reason: xenobiotic metabolic process is a direct metabolic process expected from Gsta2's documented role in glutathione conjugation of electrophilic endogenous and xenobiotic substrates. Supporting Evidence: UniProtKB:P04903 FUNCTION: Catalyzes the conjugation of glutathione to a large variety of electrophilic compounds. file:rat/Gsta2/Gsta2-deep-research-falcon.md Rat Gsta2 is inducible in liver by xenobiotic exposure (PFOA), consistent with a phase II detoxification/xenobiotic-response role.
GO:0004364 glutathione transferase activity	IEA GO_REF:0000120	ACCEPT	Summary: Gsta2's glutathione conjugation of electrophilic endogenous and xenobiotic substrates supports retaining glutathione transferase activity as a direct annotation (IEA, GO_REF:0000120). Reason: glutathione transferase activity is a specific catalytic activity matching Gsta2's documented role in glutathione conjugation of electrophilic endogenous and xenobiotic substrates. Supporting Evidence: UniProtKB:P04903 Reaction=RX + glutathione = an S-substituted glutathione + a halide anion + H(+)
GO:0005737 cytoplasm	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: cytoplasm is retained as useful context for Gsta2, but it is not the defining core function (IEA, GO_REF:0000044). Reason: cytoplasm records where Gsta2 has been observed, but localization does not define the gene product's primary activity. Supporting Evidence: UniProtKB:P04903 FUNCTION: Catalyzes the conjugation of glutathione to a large variety of electrophilic compounds. file:rat/Gsta2/Gsta2-deep-research-falcon.md Alpha-class GSTs, including GSTA2-like proteins, belong to the cytosolic GST family (distinct from microsomal and mitochondrial GSTs), indicating a primarily cytosolic intracellular site of action.
GO:0005829 cytosol	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: cytosol is retained as useful context for Gsta2, but it is not the defining core function (ISO, GO_REF:0000121; donor mouse Gsta1, MGI:MGI:1095417). Reason: cytosol records where Gsta2 has been observed, but localization does not define the gene product's primary activity. The donor is mouse Gsta1 (MGI:MGI:1095417), a cluster-level rather than strict one-to-one alpha-class match, but the cytosolic location is independently established for rat GSTA2 by direct assay (IDA, PMID:17112229) and by the UniProt subcellular location. Supporting Evidence: UniProtKB:P04903 SUBCELLULAR LOCATION: Cytoplasm. UniProtKB:P04903 SUBCELLULAR LOCATION: Cytoplasm.
GO:0061771 response to caloric restriction	ISO GO_REF:0000121	MARK AS OVER ANNOTATED	Summary: response to caloric restriction is treated as over-annotation because it reflects context or consequence rather than Gsta2's direct role (ISO, GO_REF:0000121). Reason: response to caloric restriction reflects exposure, expression, phenotype, or downstream pathway context rather than the direct Gsta2 role in glutathione conjugation of electrophilic endogenous and xenobiotic substrates. Propagation Review Root cause: PROPAGATION BAD Failure modes: WRONG ORTHOLOG OR PARALOG CONTEXT OR TISSUE MISMATCH Sources checked: MGI:MGI:1095417 · mouse Gsta1 SUPPORTS SOURCE BUT NOT TARGET Rodent alpha-class GST genes are an expanded cluster rather than a 1:1 orthologue set, so RGD's mouse-to-rat ISO here is cluster-level. Verifiable in Gsta2-goa.tsv itself: two different mouse donors, Gsta1 (MGI:MGI:1095417) and Gsta2 (MGI:MGI:95863), both seed ISO onto this one rat gene, so the mapping RGD applied is many-to-one rather than 1:1. Independently of that, the donor term records a dietary/physiological expression response rather than a Gsta2 activity, which is the primary reason it does not transfer.
GO:0004364 glutathione transferase activity	ISS GO_REF:0000024	ACCEPT	Summary: Gsta2's glutathione conjugation of electrophilic endogenous and xenobiotic substrates supports retaining glutathione transferase activity as a direct annotation (ISS, GO_REF:0000024). Reason: glutathione transferase activity is a specific catalytic activity matching Gsta2's documented role in glutathione conjugation of electrophilic endogenous and xenobiotic substrates. The similarity donor is mouse Gsta2 (UniProtKB:P10648), from which the rat UniProt FUNCTION statement is itself transferred; the activity is the class-defining catalysis of all alpha-class GSTs. Supporting Evidence: UniProtKB:P04903 Reaction=RX + glutathione = an S-substituted glutathione + a halide anion + H(+) UniProtKB:P04903 FUNCTION: Catalyzes the conjugation of glutathione to a large variety of electrophilic compounds.
GO:0005739 mitochondrion	ISO GO_REF:0000121	MARK AS OVER ANNOTATED	Summary: mitochondrion is treated as over-annotation; it derives only from ISO transfer from an RGD ortholog and conflicts with the cytosolic-family assignment of alpha-class GSTs (ISO, GO_REF:0000121). Reason: The mitochondrion localization rests solely on ISO transfer from a rodent ortholog (RGD) and is contradicted by falcon deep research, which assigns alpha-class GSTs (including GSTA2-like proteins) to the cytosolic GST family, explicitly distinct from mitochondrial GSTs. This weak, ortholog-inferred localization is best flagged as over-annotation rather than retained as valid localization context. Propagation Review Root cause: PROPAGATION BAD Failure modes: COMPARTMENT OR COMPLEX MISMATCH WRONG ORTHOLOG OR PARALOG Sources checked: MGI:MGI:1095417 · mouse Gsta1 SUPPORTS SOURCE BUT NOT TARGET Cluster-level ISO transfer across the expanded rodent alpha-class family. UniProt records only "SUBCELLULAR LOCATION - Cytoplasm" for P04903, and alpha-class GSTs are the cytosolic branch of the GST superfamily, distinct from the mitochondrial (kappa) and microsomal (MAPEG) branches, so the compartment does not transfer regardless of how good the orthology assignment is. Supporting Evidence: file:rat/Gsta2/Gsta2-deep-research-falcon.md Alpha-class GSTs, including GSTA2-like proteins, belong to the cytosolic GST family (distinct from microsomal and mitochondrial GSTs), indicating a primarily cytosolic intracellular site of action.
GO:0004364 glutathione transferase activity	ISO GO_REF:0000121	ACCEPT	Summary: Gsta2's glutathione conjugation of electrophilic endogenous and xenobiotic substrates supports retaining glutathione transferase activity as a direct annotation (ISO, GO_REF:0000121). Reason: glutathione transferase activity is a specific catalytic activity matching Gsta2's documented role in glutathione conjugation of electrophilic endogenous and xenobiotic substrates. Its donor is mouse Gsta1 (MGI:MGI:1095417); the mouse Gsta2 donor (MGI:MGI:95863) seeds a separate, otherwise identical row. Unlike the compartment and stimulus-response ISO annotations from the same donors, it transfers safely, because glutathione transferase activity is the defining, conserved activity of every member of the rodent alpha-class cluster and does not depend on resolving which mouse gene is the true 1:1 orthologue. GOA additionally carries a direct annotation for this activity on the target (IDA, PMID:17112229, assigned by CAFA), although that paper characterises adduction of the protein rather than assaying catalysis. Propagation Review Root cause: NO FAILURE CORE Sources checked: MGI:MGI:1095417 · mouse Gsta1 SUPPORTS TRANSFER Cluster-level donor, but the transferred term is the class-defining catalytic activity shared by all alpha-class GSTs, so imprecise orthology within the cluster does not make the transfer unsafe. Supporting Evidence: UniProtKB:P04903 Reaction=RX + glutathione = an S-substituted glutathione + a halide anion + H(+) UniProtKB:P04903 FUNCTION: Catalyzes the conjugation of glutathione to a large variety of electrophilic compounds.
GO:0035731 dinitrosyl-iron complex binding	IPI PMID:17197701 Electrostatic association of glutathione transferase to the ...	KEEP AS NON CORE	Summary: dinitrosyl-iron complex binding is retained as useful context for Gsta2, but it is not the defining core function (IPI, PMID:17197701). Reason: dinitrosyl-iron complex binding records substrate, cofactor, or quaternary-structure context for Gsta2, but the curated core function is glutathione conjugation of electrophilic endogenous and xenobiotic substrates. Supporting Evidence: PMID:17197701 The discovery that the dinitrosyl-diglutathionyl-iron complex binds tightly to Alpha class GSTs in rat hepatocytes
GO:0009617 response to bacterium	ISO GO_REF:0000121	MARK AS OVER ANNOTATED	Summary: response to bacterium is treated as over-annotation because it reflects context or consequence rather than Gsta2's direct role (ISO, GO_REF:0000121). Reason: response to bacterium reflects exposure, expression, phenotype, or downstream pathway context rather than the direct Gsta2 role in glutathione conjugation of electrophilic endogenous and xenobiotic substrates. Propagation Review Root cause: PROPAGATION BAD Failure modes: WRONG ORTHOLOG OR PARALOG CONTEXT OR TISSUE MISMATCH Sources checked: MGI:MGI:1095417 · mouse Gsta1 SUPPORTS SOURCE BUT NOT TARGET Donor annotation captures an expression/exposure response in mouse Gsta1, and the term describes stimulus context rather than the glutathione-conjugation activity of the target. Alpha-class GST induction is member- and species-specific, so it does not transfer across this expanded cluster.
GO:0004364 glutathione transferase activity	IDA PMID:17112229 Site-specific arylation of rat glutathione s-transferase A1 ...	ACCEPT	Summary: Gsta2's glutathione conjugation of electrophilic endogenous and xenobiotic substrates supports retaining glutathione transferase activity as a direct annotation (IDA, PMID:17112229). Reason: glutathione transferase activity is a specific catalytic activity matching Gsta2's documented role in glutathione conjugation of electrophilic endogenous and xenobiotic substrates. The PMID:17112229 quote shows GSTA1/A2 as targets of bromobenzoquinone arylation rather than establishing catalysis; the catalytic activity itself is independently documented by the UniProt CATALYTIC ACTIVITY record, and the IDA row is retained by deferral to the RGD curator (who read the full text). Supporting Evidence: UniProtKB:P04903 Reaction=RX + glutathione = an S-substituted glutathione + a halide anion + H(+) PMID:17112229 Here we report that treatment of rats with bromobenzene results in the site-specific modification of Cys-111 in cytosolic glutathione transferase subunits A1 and A2 by bromobenzoquinone.
GO:0005829 cytosol	IDA PMID:17112229 Site-specific arylation of rat glutathione s-transferase A1 ...	KEEP AS NON CORE	Summary: cytosol is retained as useful context for Gsta2, but it is not the defining core function (IDA, PMID:17112229). Reason: cytosol records where Gsta2 has been observed, but localization does not define the gene product's primary activity. Supporting Evidence: PMID:17112229 Here we report that treatment of rats with bromobenzene results in the site-specific modification of Cys-111 in cytosolic glutathione transferase subunits A1 and A2 by bromobenzoquinone.
GO:0042178 xenobiotic catabolic process	IDA PMID:17112229 Site-specific arylation of rat glutathione s-transferase A1 ...	ACCEPT	Summary: Gsta2's glutathione conjugation of electrophilic endogenous and xenobiotic substrates supports retaining xenobiotic catabolic process as a direct annotation (IDA, PMID:17112229). Reason: xenobiotic catabolic process is a direct metabolic process expected from Gsta2's documented role in glutathione conjugation of electrophilic endogenous and xenobiotic substrates. The PMID:17112229 quote shows GSTA1/A2 as targets of bromobenzoquinone arylation rather than establishing the conjugation chemistry; the xenobiotic-conjugation function is independently documented by the UniProt FUNCTION record, and the IDA row is retained by deferral to the RGD curator (who read the full text). Supporting Evidence: UniProtKB:P04903 FUNCTION: Catalyzes the conjugation of glutathione to a large variety of electrophilic compounds. PMID:17112229 Here we report that treatment of rats with bromobenzene results in the site-specific modification of Cys-111 in cytosolic glutathione transferase subunits A1 and A2 by bromobenzoquinone.
GO:0043295 glutathione binding	IDA PMID:17112229 Site-specific arylation of rat glutathione s-transferase A1 ...	KEEP AS NON CORE	Summary: glutathione binding is retained as useful context for Gsta2, but it is not the defining core function (IDA, PMID:17112229). Reason: glutathione binding records substrate, cofactor, or quaternary-structure context for Gsta2, but the curated core function is glutathione conjugation of electrophilic endogenous and xenobiotic substrates. Supporting Evidence: PMID:17112229 glutathione transferase, a well known and abundant BB-target protein, was isolated from liver cytosol of rats treated with 14 C-BB using a GSH-agarose affinity column
GO:0030855 epithelial cell differentiation	ISO GO_REF:0000121	MARK AS OVER ANNOTATED	Summary: epithelial cell differentiation is treated as over-annotation because it reflects context or consequence rather than Gsta2's direct role (ISO, GO_REF:0000121). Reason: epithelial cell differentiation reflects exposure, expression, phenotype, or downstream pathway context rather than the direct Gsta2 role in glutathione conjugation of electrophilic endogenous and xenobiotic substrates. Falcon frames Gsta2 in epithelial/liver contexts as a highly inducible oxidative-stress marker rather than a driver of differentiation. Propagation Review Root cause: PROPAGATION BAD Failure modes: ROLE CONFLATION CONTEXT OR TISSUE MISMATCH Sources checked: UniProtKB:P09210 · human GSTA2 SUPPORTS SOURCE BUT NOT TARGET The human donor is a genuine GSTA2 orthologue, but the donor term reflects differentiation-associated expression of an alpha-class GST in epithelium rather than a role for the enzyme in driving differentiation; transferring it recasts a detoxification enzyme as a differentiation effector. Supporting Evidence: file:rat/Gsta2/Gsta2-deep-research-falcon.md This situates Gsta2 as a highly responsive marker in oxidative-stress-associated hepatic pathophysiology.
GO:0035634 response to stilbenoid	ISO GO_REF:0000121	MARK AS OVER ANNOTATED	Summary: response to stilbenoid is treated as over-annotation because it reflects context or consequence rather than Gsta2's direct role (ISO, GO_REF:0000121). Reason: response to stilbenoid reflects exposure, expression, phenotype, or downstream pathway context rather than the direct Gsta2 role in glutathione conjugation of electrophilic endogenous and xenobiotic substrates. Falcon shows Gsta2 is an ARE/Nrf2-regulated, electrophile/oxidant-inducible gene, so such "response to X" terms reflect inducible expression context rather than a direct molecular function. Propagation Review Root cause: PROPAGATION BAD Failure modes: ROLE CONFLATION WRONG ORTHOLOG OR PARALOG Sources checked: MGI:MGI:1095417 · mouse Gsta1 SUPPORTS SOURCE BUT NOT TARGET Donor term records ARE/Nrf2-mediated transcriptional induction by a stilbenoid, i.e. the gene is a target of the response rather than an executor of it, and which alpha-class member is induced by a given inducer is member-specific. Supporting Evidence: file:rat/Gsta2/Gsta2-deep-research-falcon.md A specific ARE sequence is reported for rat GSTA2: TAAtgGTGACaaaGCA, and the review provides the ARE core motif (e.g., TGACnnnGC) and consensus patterns used to identify functional AREs. This supports that rat Gsta2 is an ARE-regulated gene, consistent with oxidative/electrophile-inducible expression.
GO:0004364 glutathione transferase activity	ISO GO_REF:0000121	ACCEPT	Summary: Glutathione transferase activity transferred by orthology from mouse Gsta2 (MGI:MGI:95863); donor-split duplicate of the mouse-Gsta1-donor ISO row and accepted on the same grounds. Reason: The donor is mouse Gsta2 (MGI:MGI:95863), which also seeds ISO rows onto rat Gsta1, so the mapping is cluster-level rather than a demonstrated one-to-one orthology. Glutathione transferase activity is nevertheless the class-defining catalytic activity of every alpha-class GST and is what the rat UniProt entry records for P04903, so the transfer is safe regardless of which mouse gene is the true orthologue. Propagation Review Root cause: NO FAILURE CORE Sources checked: MGI:MGI:95863 · mouse Gsta2 SUPPORTS TRANSFER Same cluster-level caveat as MGI:MGI:1095417 and no more precise, but the transferred term is the class-defining catalytic activity, so the imprecision does not make it unsafe. GOA also carries a direct annotation for this activity on the target (IDA, PMID:17112229, CAFA), though that paper characterises adduction rather than assaying catalysis. Supporting Evidence: UniProtKB:P04903 FUNCTION: Catalyzes the conjugation of glutathione to a large variety of electrophilic compounds.
GO:0005739 mitochondrion	ISO GO_REF:0000121	MARK AS OVER ANNOTATED	Summary: Mitochondrion transferred by orthology from mouse Gsta2 (MGI:MGI:95863); donor-split duplicate of the mouse-Gsta1-donor mitochondrion row and marked as over-annotation on the same grounds. Reason: The donor is mouse Gsta2 (MGI:MGI:95863), a cluster-level donor that seeds the same term set onto both rat Gsta1 and rat Gsta2. No rat experiment places GSTA2 in mitochondria; UniProt records only a cytoplasmic location for P04903, and the best-documented mitochondrial alpha-class GST in rat is GSTA4-4 rather than GSTA2. The compartment claim therefore overshoots what is known for the target. Propagation Review Root cause: PROPAGATION BAD Failure modes: COMPARTMENT OR COMPLEX MISMATCH WRONG ORTHOLOG OR PARALOG Sources checked: MGI:MGI:95863 · mouse Gsta2 SUPPORTS SOURCE BUT NOT TARGET Shares the symbol with the target, but this same mouse donor seeds ISO onto both rat Gsta1 and rat Gsta2 for the identical five terms (GO:0005739, GO:0005829, GO:0004364, GO:0009617, GO:0035634; compare Gsta1-goa.tsv with Gsta2-goa.tsv). One mouse gene feeding two rat genes the same term set is cluster-level transfer, not the demonstrated 1:1 orthology that would license a compartment assignment. Supporting Evidence: UniProtKB:P04903 SUBCELLULAR LOCATION: Cytoplasm. file:rat/Gsta2/Gsta2-deep-research-falcon.md Alpha-class GSTs, including GSTA2-like proteins, belong to the cytosolic GST family (distinct from microsomal and mitochondrial GSTs), indicating a primarily cytosolic intracellular site of action.
GO:0005829 cytosol	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: Cytosol transferred by orthology from mouse Gsta2 (MGI:MGI:95863); donor-split duplicate of the mouse-Gsta1-donor cytosol row, kept as non-core localization context. Reason: The donor is mouse Gsta2 (MGI:MGI:95863), a cluster-level alpha-class donor, but the cytosolic location is independently established for rat GSTA2 by direct assay (IDA, PMID:17112229) and by the UniProt subcellular location, so the transfer is correct in outcome. Localization does not define the core activity. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: MGI:MGI:95863 · mouse Gsta2 SUPPORTS TRANSFER Cluster-level donor, but cytosolic location is shared by every alpha-class GST and is confirmed for rat GSTA2 itself by direct assay, so the transferred claim holds for the target. Supporting Evidence: UniProtKB:P04903 SUBCELLULAR LOCATION: Cytoplasm. PMID:17112229 Here we report that treatment of rats with bromobenzene results in the site-specific modification of Cys-111 in cytosolic glutathione transferase subunits A1 and A2 by bromobenzoquinone.
GO:0005829 cytosol	ISO GO_REF:0000121	KEEP AS NON CORE	Summary: Cytosol transferred by orthology from human GSTA2 (UniProtKB:P09210); donor-split duplicate of the mouse-donor cytosol rows, kept as non-core localization context. Reason: The donor is human GSTA2 (P09210). Cytosolic location is shared by all alpha-class GSTs and is independently established for rat GSTA2 by direct assay (IDA, PMID:17112229) and by the UniProt subcellular location, so the transfer is correct. Localization does not define the core activity. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P09210 · human GSTA2 SUPPORTS TRANSFER Human GSTA2 is a cytosolic alpha-class GST; the location is confirmed for rat GSTA2 by direct assay, so the transferred claim holds for the target. Supporting Evidence: UniProtKB:P04903 SUBCELLULAR LOCATION: Cytoplasm. PMID:17112229 Here we report that treatment of rats with bromobenzene results in the site-specific modification of Cys-111 in cytosolic glutathione transferase subunits A1 and A2 by bromobenzoquinone.
GO:0009617 response to bacterium	ISO GO_REF:0000121	MARK AS OVER ANNOTATED	Summary: Response to bacterium transferred by orthology from mouse Gsta2 (MGI:MGI:95863); donor-split duplicate of the mouse-Gsta1-donor row and marked as over-annotation on the same grounds. Reason: The donor is mouse Gsta2 (MGI:MGI:95863). The donor term records an expression change under bacterial challenge in mouse; induction of an alpha-class GST is member- and species-specific, has not been shown for rat Gsta2, and in any case describes stimulus context rather than the glutathione-conjugation activity of the enzyme. Propagation Review Root cause: PROPAGATION BAD Failure modes: WRONG ORTHOLOG OR PARALOG CONTEXT OR TISSUE MISMATCH Sources checked: MGI:MGI:95863 · mouse Gsta2 SUPPORTS SOURCE BUT NOT TARGET This same donor seeds ISO onto both rat Gsta1 and rat Gsta2 for the identical five terms (GO:0005739, GO:0005829, GO:0004364, GO:0009617, GO:0035634), so the shared symbol reflects cluster-level transfer rather than the demonstrated 1:1 orthology that a stimulus-response term would require.
GO:0035634 response to stilbenoid	ISO GO_REF:0000121	MARK AS OVER ANNOTATED	Summary: Response to stilbenoid transferred by orthology from mouse Gsta2 (MGI:MGI:95863); donor-split duplicate of the mouse-Gsta1-donor row and marked as over-annotation on the same grounds. Reason: The donor is mouse Gsta2 (MGI:MGI:95863). The donor term records transcriptional induction by a stilbenoid in mouse; which alpha-class member is induced by a given inducer is member-specific, stilbenoid induction has not been shown for rat Gsta2, and the term describes inducible expression rather than a Gsta2 activity. Propagation Review Root cause: PROPAGATION BAD Failure modes: ROLE CONFLATION WRONG ORTHOLOG OR PARALOG Sources checked: MGI:MGI:95863 · mouse Gsta2 SUPPORTS SOURCE BUT NOT TARGET This same donor seeds ISO onto both rat Gsta1 and rat Gsta2 for the identical five terms (GO:0005739, GO:0005829, GO:0004364, GO:0009617, GO:0035634), so the shared symbol reflects cluster-level transfer; the transferred term is again an inducible-expression observation rather than a Gsta2 activity.
GO:0047066 phospholipid-hydroperoxide glutathione peroxidase activity	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Phospholipid-hydroperoxide glutathione peroxidase activity transferred by sequence similarity from human GSTA2 (UniProtKB:P09210), whose recombinant enzyme reduces phosphatidylcholine and phosphatidylethanolamine hydroperoxides with high catalytic efficiency. Kept as a genuine but secondary alpha-class activity. Reason: The donor is human GSTA2 (P09210), for which selenium-independent glutathione peroxidase activity toward phospholipid hydroperoxides was measured directly on the purified recombinant enzyme (PMID:10395737). This peroxidase activity is a conserved property of the alpha-class active site and is plausible for rat GSTA2, but it has not been measured on the purified rat enzyme and the rat UniProt entry does not record it, and it is a side activity of the same glutathione-binding site rather than the defining conjugation function. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P09210 · human GSTA2 SUPPORTS TRANSFER The donor's phospholipid-hydroperoxide peroxidase activity is experimentally measured (IDA, PMID:10395737) and is a conserved alpha-class property of the shared active site; plausible for rat GSTA2 though not yet measured on the rat enzyme. Supporting Evidence: PMID:10395737 Both isozymes had remarkably high peroxidase activity toward fatty acid hydroperoxides, phospholipid hydroperoxides, and cumene hydroperoxide. PMID:10395737 the catalytic efficiency of hGSTA2-2 for PC-hydroperoxide and PE-hydroperoxide was 317.5 and 353 s-1 mM-1, respectively file:rat/Gsta2/Gsta2-deep-research-falcon.md alpha-class GSTs are described as having additional activities, including selenium-independent glutathione peroxidase-like activity and reduction of organic hydroperoxides
GO:0098869 cellular oxidant detoxification	IEA GO_REF:0000108	KEEP AS NON CORE	Summary: Cellular oxidant detoxification inferred electronically from the phospholipid-hydroperoxide glutathione peroxidase activity (GO:0047066) annotation; retained as non-core context, following the status of that activity. Reason: This row is a mechanical inter-ontology inference from GO:0047066, which is itself kept as a genuine but secondary alpha-class activity transferred from human GSTA2. Reduction of lipid hydroperoxides by alpha-class GSTs does contribute to oxidant defence in liver, but for rat GSTA2 the core role is electrophile conjugation, so the process is kept as non-core. Supporting Evidence: PMID:10395737 Both isozymes had remarkably high peroxidase activity toward fatty acid hydroperoxides, phospholipid hydroperoxides, and cumene hydroperoxide. PMID:10395737 These results show that the alpha-class GSTs contribute a major portion of GPx activity toward lipid hydroperoxides in human liver.

Gene Description

Existing Annotations Review

Core Functions

References

Suggested Questions for Experts

Suggested Experiments

Deep Research

Falcon

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Notes

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