X2JE45 is native PC (799 aa) of FBgn0028916, distinct from PB/Q7KT91 (948 aa), PD/X2J9U5 (946 aa), and PE/X2JAF7 (923 aa). All two GOA rows attached to the exact accession are reviewed. The benchmark did not accidentally substitute a foreign sequence.
The reproducible analysis finds PC residues 29–799 identical to PB residues 178–948, with catalytic E362/D575 retained. Both independent MAFFT strategies recover those sites. The alteration overlaps the N-terminal GH116 domain, which is a specific reason to investigate native PC activity rather than simply accept or reject a family-derived name.
PMID:25344605(https://doi.org/10.1074/jbc.M114.593376) experimentally establishes human E527/D677 as the catalytic pair. Its abstract is cached; the primary full-text search result supplies the precise residue designation. PMID:33261081(https://pmc.ncbi.nlm.nih.gov/articles/PMC7761373/) is cached with full text and reports: “Thus, all human GBA2 isoforms were expressed but only isoform 1 clearly hydrolyzed the MUG substrate.” The tested N-terminal human alterations are not the same as PC. They demonstrate the importance of considering the whole isoform, not that PC must be inactive. The broad glycosyl-hydrolase prediction is UNC for this sequence.
The ancillary ProtNLM name points to non-lysosomal glucosylceramidase and its locations to ER/Golgi membranes. These are reasonable family-context leads for the longer protein, but their PC-specific relevance depends on protein folding and localization; mammalian bile-acid metabolism is not transferred to a fly protein. The original name, scores, locations and donors remain intact in CG33090-predictions-source.json.
Falcon completed in 343.06 seconds and was inspected. It independently identified the human isoform-activity study PMID:33261081 as relevant, but did not compare the exact 799-residue native PC sequence with the longer fly PB product. Its broad family-level glycosidase discussion is therefore supplemented by the explicit native-isoform analysis. The unresolved verdict concerns this target's altered N-terminal architecture, not an automatic demand for direct fly assays before accepting conserved functions.