All five annotation rows (two GOA and three earlier NEW proposals) were re-reviewed. Both GST activity and glutathione-metabolism propagation remain MARK_AS_OVER_ANNOTATED as physiological assignments, while residual in-vitro catalysis is acknowledged. Existing OpenScientist and Falcon reports are incorporated with their mechanistic findings and limitations, without duplicate runs.
The full text of PMID:27499004 says: "Only one of them, named OctS4, could be expressed and purified to homogeneity." It then identifies Q108F as the crystallized mutant. Thus the 0.24 s−1 kinetics, GSH protection and 5B7C structure are evidence from a close homolog, not direct OCTS1 experiments. The earlier NEW GSH-binding proposal is now ISS rather than IDA, with the inference explicit. PMID:8827456 reports native octopus S-crystallin residual kinetics; that does not establish a physiologically important OCTS1 detoxification activity.
Visual perception passes the structural-participation test: the protein contributes the lens refractive material. A QuickGO comparator query on 2026-09-20 returned CRYAA IMP annotations (PMID:14512969, PMID:9467006) and CRYBA1 IBA/NAS annotations (PMID:8999933), demonstrating the same role is annotated to this process. No additional process term was proposed.
Corrected local-file quotations or matched supporting text to its claim where applicable. Missing-assay caveats remain in reasons rather than serving as positive support. Annotation actions are unchanged.