## ATP6V0A2
- **UniProt:** Q9Y487 · **batch:** proteostasis-batch-2026-06-03 · **review status:** COMPLETE
- **PN placement:** two ALP rows — `ALP|Pre-initiation autophagy signaling|mTORC1 pathway, upstream|Nutrient sensing|V0 lysosomal v-ATPase proton pump component` and `ALP|Lysosomal catabolism|Regulation of lysosomal environment|Lysosomal acidification|V0 lysosomal v-ATPase proton pump component` ; **PN-node mapping:** V0 subtype leaves `mapped/ok_for_propagation` → GO:0046610 (lysosomal V0 domain) and GO:0033179 (V0 domain); Lysosomal-acidification type `mapped/ok_for_propagation` → GO:0007042; mTORC1/nutrient-sensing ancestors `no_mapping`; Pre-initiation class `context_only/too_broad` (GO:0010506).
- **Consistency:** Consistent. Notes, review, PN row, and PN-node mapping all converge on the V0-sector lysosomal V-ATPase identity. The review adds exactly the three projected terms at their mapped levels and explicitly declines to promote the broader nutrient-sensing/autophagy context. No contradictions.
- **PN story / NEW pressure:** The lysosomal-specific terms were genuinely absent from ATP6V0A2 GOA (which had only broader GO:0007035 vacuolar acidification and GO:0033179/GO:0000220 V0-domain). Review adds GO:0007042 lysosomal lumen acidification (NEW) and GO:0046610 lysosomal V0 domain (NEW). I verified both are real, non-obsolete GO terms via OLS. These are defensible ADDs (more specific children of existing annotations), supported by V0-subunit identity plus lysosomal-membrane proteomics (PMID:17897319). The PN nutrient-sensing/mTORC1 story correctly does NOT generate a NEW term — review leaves it as a suggested_question/experiment only.
- **Mapping strategy:** No change warranted. Subtype-level `ok_for_propagation` and the conservative `no_mapping`/`context_only` ancestors are right; broad mTORC1 container is correctly not propagated (matches TOMM20/HSPA8 "too broad" precedent).
- **Evidence alignment:** Divergent by design. PN cites review-article titles (mTORC1, SEA/GATOR, V-ATPase structure, neurodegeneration); the review's load-bearing PMIDs are independent primary/structural sources (16415858 ARNO endosome, 33065002 human V-ATPase cryo-EM, 32001091, 17897319 lysosomal proteomics, 28296633 iron/HIF). Only the V-ATPase-structure theme overlaps conceptually.
- **Verdict:** Consistent; both lysosomal NEW terms are verified real, defensible ADDs; PN nutrient-sensing context correctly not propagated. No edits required.