PRDX4 encodes peroxiredoxin-4, a typical 2-Cys thioredoxin-dependent peroxidase that reduces hydrogen peroxide and organic hydroperoxides. It is cotranslationally translocated to and retained mainly in the endoplasmic reticulum, with a smaller cytoplasmic fraction that has been linked to redox modulation of NF-kappaB signaling. Its core annotation is thioredoxin-dependent peroxiredoxin/peroxidase activity in peroxide detoxification and redox homeostasis, not generic protein binding.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: cytosol localization is supported for a smaller PRDX4 pool, including the cytoplasmic fraction implicated in NF-kappaB redox modulation. Reason: Although the endoplasmic reticulum is the dominant core location, UniProt and experimental literature support a cytoplasmic fraction. The term is therefore valid, with ER retained as the primary localization. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. Note=A small fraction of the protein is cytoplasmic. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report emphasizes ER localization as primary while noting additional cytosolic or secreted/extracellular PRDX4 contexts. |
| GO:0006979 response to oxidative stress | IBA GO_REF:0000033 | ACCEPT | Summary: response to oxidative stress is supported by PRDX4 peroxide-reducing activity and its role in cellular redox protection. Reason: PRDX4 directly detoxifies hydroperoxides through the thioredoxin system, so these redox and peroxide catabolic process annotations are appropriate biological-process summaries. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report summarizes PRDX4 as a typical 2-Cys peroxiredoxin that reduces H2O2 and other hydroperoxides and supports ER redox/proteostasis biology. |
| GO:0008379 thioredoxin peroxidase activity | IBA GO_REF:0000033 | ACCEPT | Summary: thioredoxin peroxidase activity accurately captures PRDX4 catalysis as a thioredoxin-dependent 2-Cys peroxiredoxin that reduces hydroperoxides. Reason: This is the core molecular function of PRDX4 and is supported by both the original thioredoxin peroxidase study and structural/catalytic analysis. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt Reaction=a hydroperoxide + [thioredoxin]-dithiol = an alcohol + [thioredoxin]-disulfide + H2O; EC=1.11.1.24. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report summarizes PRDX4 as a typical 2-Cys peroxiredoxin that reduces H2O2 and other hydroperoxides and supports ER redox/proteostasis biology. |
| GO:0042744 hydrogen peroxide catabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: hydrogen peroxide catabolic process is supported by PRDX4 peroxide-reducing activity and its role in cellular redox protection. Reason: PRDX4 directly detoxifies hydroperoxides through the thioredoxin system, so these redox and peroxide catabolic process annotations are appropriate biological-process summaries. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report summarizes PRDX4 as a typical 2-Cys peroxiredoxin that reduces H2O2 and other hydroperoxides and supports ER redox/proteostasis biology. |
| GO:0045454 cell redox homeostasis | IBA GO_REF:0000033 | ACCEPT | Summary: cell redox homeostasis is supported by PRDX4 peroxide-reducing activity and its role in cellular redox protection. Reason: PRDX4 directly detoxifies hydroperoxides through the thioredoxin system, so these redox and peroxide catabolic process annotations are appropriate biological-process summaries. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report summarizes PRDX4 as a typical 2-Cys peroxiredoxin that reduces H2O2 and other hydroperoxides and supports ER redox/proteostasis biology. |
| GO:0005783 endoplasmic reticulum | IBA GO_REF:0000033 | ACCEPT | Summary: Endoplasmic reticulum localization is a core location for PRDX4. UniProt states that PRDX4 is cotranslationally translocated to and retained within the ER. Reason: This is the most informative cellular component for PRDX4 and matches the enzyme biology as the ER-localized peroxiredoxin. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. Note=Cotranslationally translocated to and retained within the endoplasmic reticulum. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report summarizes PRDX4 as localized mainly to the endoplasmic reticulum, with ER luminal targeting and retention through oxidoreductase/chaperone interactions. |
| GO:0098869 cellular oxidant detoxification | IEA GO_REF:0000120 | ACCEPT | Summary: cellular oxidant detoxification is supported by PRDX4 peroxide-reducing activity and its role in cellular redox protection. Reason: PRDX4 directly detoxifies hydroperoxides through the thioredoxin system, so these redox and peroxide catabolic process annotations are appropriate biological-process summaries. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report summarizes PRDX4 as a typical 2-Cys peroxiredoxin that reduces H2O2 and other hydroperoxides and supports ER redox/proteostasis biology. |
| GO:0004601 peroxidase activity | IEA GO_REF:0000043 | MARK AS OVER ANNOTATED | Summary: peroxidase activity is compatible with PRDX4 biology but is a broad parent or less-informative activity compared with the specific thioredoxin-dependent peroxiredoxin annotations already present. Reason: The precise MF terms GO:0140824/GO:0051920/GO:0008379 better represent PRDX4. Broad antioxidant/peroxidase/oxidoreductase terms add little specificity. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt PRDX4 is annotated as a thiol-specific peroxidase that reduces hydrogen peroxide and organic hydroperoxides. |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: cytoplasm localization is supported for a smaller PRDX4 pool, including the cytoplasmic fraction implicated in NF-kappaB redox modulation. Reason: Although the endoplasmic reticulum is the dominant core location, UniProt and experimental literature support a cytoplasmic fraction. The term is therefore valid, with ER retained as the primary localization. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. Note=A small fraction of the protein is cytoplasmic. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report emphasizes ER localization as primary while noting additional cytosolic or secreted/extracellular PRDX4 contexts. |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000120 | ACCEPT | Summary: Endoplasmic reticulum localization is a core location for PRDX4. UniProt states that PRDX4 is cotranslationally translocated to and retained within the ER. Reason: This is the most informative cellular component for PRDX4 and matches the enzyme biology as the ER-localized peroxiredoxin. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. Note=Cotranslationally translocated to and retained within the endoplasmic reticulum. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report summarizes PRDX4 as localized mainly to the endoplasmic reticulum, with ER luminal targeting and retention through oxidoreductase/chaperone interactions. |
| GO:0016209 antioxidant activity | IEA GO_REF:0000120 | MARK AS OVER ANNOTATED | Summary: antioxidant activity is compatible with PRDX4 biology but is a broad parent or less-informative activity compared with the specific thioredoxin-dependent peroxiredoxin annotations already present. Reason: The precise MF terms GO:0140824/GO:0051920/GO:0008379 better represent PRDX4. Broad antioxidant/peroxidase/oxidoreductase terms add little specificity. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt PRDX4 is annotated as a thiol-specific peroxidase that reduces hydrogen peroxide and organic hydroperoxides. |
| GO:0016491 oxidoreductase activity | IEA GO_REF:0000120 | MARK AS OVER ANNOTATED | Summary: oxidoreductase activity is compatible with PRDX4 biology but is a broad parent or less-informative activity compared with the specific thioredoxin-dependent peroxiredoxin annotations already present. Reason: The precise MF terms GO:0140824/GO:0051920/GO:0008379 better represent PRDX4. Broad antioxidant/peroxidase/oxidoreductase terms add little specificity. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt PRDX4 is annotated as a thiol-specific peroxidase that reduces hydrogen peroxide and organic hydroperoxides. |
| GO:0051920 peroxiredoxin activity | IEA GO_REF:0000002 | ACCEPT | Summary: peroxiredoxin activity accurately captures PRDX4 catalysis as a thioredoxin-dependent 2-Cys peroxiredoxin that reduces hydroperoxides. Reason: This is the core molecular function of PRDX4 and is supported by both the original thioredoxin peroxidase study and structural/catalytic analysis. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt Reaction=a hydroperoxide + [thioredoxin]-dithiol = an alcohol + [thioredoxin]-disulfide + H2O; EC=1.11.1.24. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report summarizes PRDX4 as a typical 2-Cys peroxiredoxin that reduces H2O2 and other hydroperoxides and supports ER redox/proteostasis biology. |
| GO:0140824 thioredoxin-dependent peroxiredoxin activity | IEA GO_REF:0000120 | ACCEPT | Summary: thioredoxin-dependent peroxiredoxin activity accurately captures PRDX4 catalysis as a thioredoxin-dependent 2-Cys peroxiredoxin that reduces hydroperoxides. Reason: This is the core molecular function of PRDX4 and is supported by both the original thioredoxin peroxidase study and structural/catalytic analysis. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt Reaction=a hydroperoxide + [thioredoxin]-dithiol = an alcohol + [thioredoxin]-disulfide + H2O; EC=1.11.1.24. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report summarizes PRDX4 as a typical 2-Cys peroxiredoxin that reduces H2O2 and other hydroperoxides and supports ER redox/proteostasis biology. |
| GO:0005515 protein binding | IPI PMID:17644091 Peroxiredoxin-4 interacts with and regulates the thromboxane... | MARK AS OVER ANNOTATED | Summary: Generic protein binding from interactome evidence does not describe the specific PRDX4 molecular function. Reason: PRDX4 has biologically relevant partners and oligomerization, but GO:0005515 is too vague. Specific terms for peroxiredoxin activity and identical protein binding capture the supported function better. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt The curated function describes thioredoxin-dependent peroxidase activity; interaction rows are partner lists rather than specific functional annotations. |
| GO:0005515 protein binding | IPI PMID:21057456 Recycling of peroxiredoxin IV provides a novel pathway for d... | MARK AS OVER ANNOTATED | Summary: Generic protein binding from interactome evidence does not describe the specific PRDX4 molecular function. Reason: PRDX4 has biologically relevant partners and oligomerization, but GO:0005515 is too vague. Specific terms for peroxiredoxin activity and identical protein binding capture the supported function better. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt The curated function describes thioredoxin-dependent peroxidase activity; interaction rows are partner lists rather than specific functional annotations. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | MARK AS OVER ANNOTATED | Summary: Generic protein binding from interactome evidence does not describe the specific PRDX4 molecular function. Reason: PRDX4 has biologically relevant partners and oligomerization, but GO:0005515 is too vague. Specific terms for peroxiredoxin activity and identical protein binding capture the supported function better. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt The curated function describes thioredoxin-dependent peroxidase activity; interaction rows are partner lists rather than specific functional annotations. |
| GO:0005515 protein binding | IPI PMID:25959826 Quantitative interaction proteomics of neurodegenerative dis... | MARK AS OVER ANNOTATED | Summary: Generic protein binding from interactome evidence does not describe the specific PRDX4 molecular function. Reason: PRDX4 has biologically relevant partners and oligomerization, but GO:0005515 is too vague. Specific terms for peroxiredoxin activity and identical protein binding capture the supported function better. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt The curated function describes thioredoxin-dependent peroxidase activity; interaction rows are partner lists rather than specific functional annotations. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | MARK AS OVER ANNOTATED | Summary: Generic protein binding from interactome evidence does not describe the specific PRDX4 molecular function. Reason: PRDX4 has biologically relevant partners and oligomerization, but GO:0005515 is too vague. Specific terms for peroxiredoxin activity and identical protein binding capture the supported function better. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt The curated function describes thioredoxin-dependent peroxidase activity; interaction rows are partner lists rather than specific functional annotations. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MARK AS OVER ANNOTATED | Summary: Generic protein binding from interactome evidence does not describe the specific PRDX4 molecular function. Reason: PRDX4 has biologically relevant partners and oligomerization, but GO:0005515 is too vague. Specific terms for peroxiredoxin activity and identical protein binding capture the supported function better. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt The curated function describes thioredoxin-dependent peroxidase activity; interaction rows are partner lists rather than specific functional annotations. |
| GO:0005829 cytosol | IEA GO_REF:0000107 | ACCEPT | Summary: cytosol localization is supported for a smaller PRDX4 pool, including the cytoplasmic fraction implicated in NF-kappaB redox modulation. Reason: Although the endoplasmic reticulum is the dominant core location, UniProt and experimental literature support a cytoplasmic fraction. The term is therefore valid, with ER retained as the primary localization. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. Note=A small fraction of the protein is cytoplasmic. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report emphasizes ER localization as primary while noting additional cytosolic or secreted/extracellular PRDX4 contexts. |
| GO:0042802 identical protein binding | IEA GO_REF:0000107 | ACCEPT | Summary: Identical protein binding is supported by PRDX4 homodimerization and decamer formation, which are part of its 2-Cys peroxiredoxin catalytic assembly. Reason: Unlike generic protein binding, identical protein binding is mechanistically informative for PRDX4 because catalysis uses a dimeric interface and oxidized PRDX4 forms disulfide-linked homodimers/decamers. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers assemble to form a ring-like decamer. |
| GO:0005783 endoplasmic reticulum | IDA GO_REF:0000052 | ACCEPT | Summary: Endoplasmic reticulum localization is a core location for PRDX4. UniProt states that PRDX4 is cotranslationally translocated to and retained within the ER. Reason: This is the most informative cellular component for PRDX4 and matches the enzyme biology as the ER-localized peroxiredoxin. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. Note=Cotranslationally translocated to and retained within the endoplasmic reticulum. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report summarizes PRDX4 as localized mainly to the endoplasmic reticulum, with ER luminal targeting and retention through oxidoreductase/chaperone interactions. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: cytosol localization is supported for a smaller PRDX4 pool, including the cytoplasmic fraction implicated in NF-kappaB redox modulation. Reason: Although the endoplasmic reticulum is the dominant core location, UniProt and experimental literature support a cytoplasmic fraction. The term is therefore valid, with ER retained as the primary localization. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. Note=A small fraction of the protein is cytoplasmic. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report emphasizes ER localization as primary while noting additional cytosolic or secreted/extracellular PRDX4 contexts. |
| GO:0060090 molecular adaptor activity | EXP PMID:21916849 Structural insights into the peroxidase activity and inactiv... | MODIFY | Summary: The cited structural study supports PRDX4 peroxidase catalysis, oligomerization, and overoxidation sensitivity, but it does not establish molecular adaptor activity as a distinct molecular function. Reason: The biological evidence should be captured with a catalytic peroxiredoxin term rather than adaptor or sequestering activity. The best replacement is the specific thioredoxin-dependent peroxiredoxin activity term already supported by the same catalytic mechanism. Proposed replacements: thioredoxin-dependent peroxiredoxin activity Supporting Evidence: PMID:21916849 Prx4 exhibits a toroid-shaped decamer constructed of five catalytic dimers. |
| GO:0140313 molecular sequestering activity | IDA PMID:21916849 Structural insights into the peroxidase activity and inactiv... | MODIFY | Summary: The cited structural study supports PRDX4 peroxidase catalysis, oligomerization, and overoxidation sensitivity, but it does not establish molecular sequestering activity as a distinct molecular function. Reason: The biological evidence should be captured with a catalytic peroxiredoxin term rather than adaptor or sequestering activity. The best replacement is the specific thioredoxin-dependent peroxiredoxin activity term already supported by the same catalytic mechanism. Proposed replacements: thioredoxin-dependent peroxiredoxin activity Supporting Evidence: PMID:21916849 Prx4 exhibits a toroid-shaped decamer constructed of five catalytic dimers. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-6798748 | KEEP AS NON CORE | Summary: extracellular region reflects secretory or extracellular detection/pathway context for PRDX4 rather than the main site of its curated peroxidase function. Reason: PRDX4 is an ER/secretory-pathway peroxiredoxin, so extracellular or granule-lumen pathway placements can be retained as non-core context while ER remains the primary location. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt PRDX4 is cotranslationally translocated to and retained within the endoplasmic reticulum. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report notes PRDX4 can be secreted/extracellular and has been detected in extracellular vesicle datasets, supporting non-core secretory/extracellular context. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-6800434 | KEEP AS NON CORE | Summary: extracellular region reflects secretory or extracellular detection/pathway context for PRDX4 rather than the main site of its curated peroxidase function. Reason: PRDX4 is an ER/secretory-pathway peroxiredoxin, so extracellular or granule-lumen pathway placements can be retained as non-core context while ER remains the primary location. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt PRDX4 is cotranslationally translocated to and retained within the endoplasmic reticulum. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report notes PRDX4 can be secreted/extracellular and has been detected in extracellular vesicle datasets, supporting non-core secretory/extracellular context. |
| GO:0034774 secretory granule lumen | TAS Reactome:R-HSA-6798748 | KEEP AS NON CORE | Summary: secretory granule lumen reflects secretory or extracellular detection/pathway context for PRDX4 rather than the main site of its curated peroxidase function. Reason: PRDX4 is an ER/secretory-pathway peroxiredoxin, so extracellular or granule-lumen pathway placements can be retained as non-core context while ER remains the primary location. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt PRDX4 is cotranslationally translocated to and retained within the endoplasmic reticulum. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report notes PRDX4 can be secreted/extracellular and has been detected in extracellular vesicle datasets, supporting non-core secretory/extracellular context. |
| GO:1904813 ficolin-1-rich granule lumen | TAS Reactome:R-HSA-6800434 | KEEP AS NON CORE | Summary: ficolin-1-rich granule lumen reflects secretory or extracellular detection/pathway context for PRDX4 rather than the main site of its curated peroxidase function. Reason: PRDX4 is an ER/secretory-pathway peroxiredoxin, so extracellular or granule-lumen pathway placements can be retained as non-core context while ER remains the primary location. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt PRDX4 is cotranslationally translocated to and retained within the endoplasmic reticulum. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report notes PRDX4 can be secreted/extracellular and has been detected in extracellular vesicle datasets, supporting non-core secretory/extracellular context. |
| GO:0005634 nucleus | HDA PMID:21630459 Proteomic characterization of the human sperm nucleus. | KEEP AS NON CORE | Summary: nucleus comes from high-throughput proteomic detection and is not the main functional location of PRDX4. Reason: Retain the observation as non-core because proteomic localization can reflect cargo or context-specific detection. It should not displace the ER/cytoplasmic peroxiredoxin localization. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt The curated subcellular location is cytoplasm and endoplasmic reticulum, with ER retention noted as the main localization. |
| GO:0070062 extracellular exosome | HDA PMID:19199708 Proteomic analysis of human parotid gland exosomes by multid... | KEEP AS NON CORE | Summary: extracellular exosome comes from high-throughput proteomic detection and is not the main functional location of PRDX4. Reason: Retain the observation as non-core because proteomic localization can reflect cargo or context-specific detection. It should not displace the ER/cytoplasmic peroxiredoxin localization. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt The curated subcellular location is cytoplasm and endoplasmic reticulum, with ER retention noted as the main localization. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report notes PRDX4 can be secreted/extracellular and has been detected in extracellular vesicle datasets, supporting non-core secretory/extracellular context. |
| GO:0007252 I-kappaB phosphorylation | TAS PMID:9388242 Regulatory role for a novel human thioredoxin peroxidase in ... | MODIFY | Summary: PRDX4 modulates I-kappaB-alpha phosphorylation through redox regulation but is not the kinase that phosphorylates I-kappaB. Reason: The evidence supports regulation of I-kappaB phosphorylation, not execution of phosphorylation. The annotation should be moved to a regulatory BP term. Proposed replacements: regulation of I-kappaB phosphorylation Supporting Evidence: PMID:9388242 AOE372 defines a redox pathway that specifically regulates NF-kappaB activity via a modulation of IkappaB-alpha phosphorylation in the cytoplasm. |
| GO:0008379 thioredoxin peroxidase activity | TAS PMID:9388242 Regulatory role for a novel human thioredoxin peroxidase in ... | ACCEPT | Summary: thioredoxin peroxidase activity accurately captures PRDX4 catalysis as a thioredoxin-dependent 2-Cys peroxiredoxin that reduces hydroperoxides. Reason: This is the core molecular function of PRDX4 and is supported by both the original thioredoxin peroxidase study and structural/catalytic analysis. Supporting Evidence: file:human/PRDX4/PRDX4-uniprot.txt Reaction=a hydroperoxide + [thioredoxin]-dithiol = an alcohol + [thioredoxin]-disulfide + H2O; EC=1.11.1.24. file:human/PRDX4/PRDX4-deep-research-falcon.md Falcon report summarizes PRDX4 as a typical 2-Cys peroxiredoxin that reduces H2O2 and other hydroperoxides and supports ER redox/proteostasis biology. |
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Download this section (compressed HTML)Q: Which PRDX4 pools act in ER peroxide detoxification versus cytoplasmic NF-kappaB redox modulation?
Suggested experts: redox biologists, ER protein folding specialists
Q: Under which physiological conditions is PRDX4 secreted or detected in granule/exosome compartments?
Suggested experts: secretory pathway specialists, proteomics experts
Experiment: Measure ER and cytosolic peroxide handling after PRDX4 knockout and compartment-targeted rescue.
Hypothesis: ER-localized PRDX4 is the dominant contributor to ER peroxide detoxification while a smaller cytosolic pool affects NF-kappaB redox signaling.
Type: Compartment-specific redox assay
Experiment: Test PRDX4 dimer/decamer interface mutants for peroxidase activity and overoxidation sensitivity in cells.
Hypothesis: PRDX4 oligomeric assembly is required for efficient thioredoxin-dependent peroxidase activity and controls susceptibility to overoxidation.
Type: Oligomerization mutant analysis
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