## ATG2B
- **UniProt:** Q96BY7 · **batch:** proteostasis-batch-2026-06-03 · **review status:** COMPLETE
- **PN placement:** `ALP|Autophagophore initiation and elongation|Regulation of autophagophore membrane composition|ATG2-WIPI complex component` ; **PN-node mapping:** type-leaf `mapped`, `ok_for_propagation_to_go` → GO:0062079 ATG2-ATG18 complex (verified real, OLS); goa_status=more_specific_than_existing_goa.
- **Consistency:** Fully consistent. Deep research/notes, review YAML, PN annotation, and PN-node mapping all converge on ATG2B as a WDR45/WIPI4-associated lipid-transfer/membrane-tethering protein of the ATG2-WIPI complex. The review explicitly adds GO:0062079 as a NEW annotation, citing it as "the conservative way to use the PN projection." No contradictions.
- **PN story / NEW pressure:** PN asserts ATG2-WIPI complex membership not previously in GOA. This is a real term, directly supported by ATG2B-WDR45 structural/biochemical evidence (PMID:28820312, 20562859). Review correctly ADDED it (action: NEW, part_of, IDA). Core molecular function (GO:0120013 lipid transfer activity) and process (autophagosome assembly via MODIFY of GO:0006914) are independently captured. Verdict: PN story is correctly captured/ADDED — well-aligned, no over-reach.
- **Mapping strategy:** Gene supports the existing node mapping rather than changing it; projected component term is narrower than (and complementary to) the review's MF/BP terms — an appropriate complex-membership refinement, not a broad over-propagation.
- **Evidence alignment:** Strong overlap. PN cites Mizushima reviews plus the ATG2A-WIPI4/PNAS structural work and the lipid-droplet paper (PMID:22219374); review uses the same PMID:22219374 plus PMID:28820312 (ATG2B-WDR45 architecture) and PMID:31721365 (ATG2B lipid transfer) for the complex/MF claims. Convergent evidence base.
- **Verdict:** Consistent; PN ATG2-ATG18 complex projection correctly ADDED as NEW. No edits required.