GBA2 is a nonlysosomal glucosylceramidase. Its single core function is GlcCer hydrolysis and catabolism; substrate-transfer capacity and downstream cytoskeletal/developmental outcomes are distinguished from that role.
The manual experimental synthesis provides original article links, section locators, species/construct details and assay limits. It separates the directly measured GalCer-analog hydrolysis result from its unresolved physiological relevance, and distinguishes ER/Golgi ortholog observations from human cell-surface activity.
The selected human expression, mouse knockout, sterol-exchange and localization experiments are organized in the synthesis. The normal caches for PMID:17080196 and PMID:32144204 contain abstracts, although selected original full-text sections were independently accessible. The cache flags remain truthful; they do not erase the separate original reading. Other reference assessments distinguish complete main text from selected sections, and available-but-unread portions from inaccessible material.
The natural human products are Q9HCG7-1 (927 residues), Q9HCG7-2 (877) and Q9HCG7-3 (640). Direct FASTAs match the official alternative-sequence reconstructions. Sequence identity alone does not establish equivalent activity or localization; historical mouse/human reagents are not automatically mapped to every natural product.
The actual PTHR12654 tree and alignment place the exact 927-residue target at AN28/PTN002489239. Beta-glucosidase activity descends from AN2/PTN000291742 and CNS development from AN15/PTN000291746. Target self-donor support is legitimate, and no retained negative record blocks those target paths.
The reviewed human UniProt record independently curates GalCer hydrolysis, bile-acid glucosyl transfer and reported plasma-membrane localization with publication-linked evidence. Three short record anchors are placed once in the review; related contexts link to the same record without repeating excerpts. These curated statements complement the original assay reading and do not prove universal topology or physiological GalCer clearance. The purified-human-enzyme abstract of PMID:9111029 also directly supports bile-acid glucoside cleavage, with its negative GlcCer result confined to those assay conditions.
The proposed GO:0016139 → GO:0016137 → GO:0005975 refinement was checked against official typed paths. No is_a/part_of path to GO:0005975 was returned. The first edge is present, but that does not establish the second. Carbohydrate chemistry and glycoside catabolism therefore retain their individual evidence; no unverified hierarchical replacement is made.
The compact evidence table retains all 53 original contexts, including two distinct source-ID/date pairs collapsed by the genuine 51-key seed. They remain original annotations, with explicit actual-native/final joins; no synthetic NEW rows are introduced. There are 26 ACCEPT, 18 KEEP_AS_NON_CORE, 7 MODIFY, 1 MARK_AS_OVER_ANNOTATED and 1 UNDECIDED decisions. The smooth-ER uncertainty remains source-specific.
The eight prior publication excerpts remain unchanged, and three concise UniProt anchors are added with source hashes, line ranges and generated record sections. The synthesis retains its separately located original-source excerpt. Quotes are not repeated across paired original contexts. All 24 scientific source objects remain unchanged. Historical acquisition coordinates and completed parent validation are preserved in the evidence table. The current amendment passed default validation, strict GOA matching, computed-status and record-section checks without annotation advisories. Status remains COMPLETE. The queue remains suspended until renewed review and CI are read.