Identity verified: UniProt Q9FG74 "Serine/threonine-protein kinase D6PK", OrderedLocusNames At5g55910.
Deep research: falcon failed (Edison API 429, 2026-10-05).
This dated audit supersedes conflicting earlier shorthand. All 40 original annotation payloads, including qualifiers and inherited NEW rows, were retained exactly. Every row was reconsidered against the target biology and cited sources. Actual Falcon and fallback provider attempts failed; the orchestration logs are preserved in .cache/module-audit-logs/auxin-polar-fetch/provider-publication-results.json. Existing provider reports, where present, served only as discovery aids. Manual primary-source inspection and normally fetched caches support the decisions below. No provider report was fabricated.
D6PK is a PIN-activating serine/threonine kinase with basal plasma-membrane recruitment. Direct transport activation and native polar localization are distinct from a general PIN polarity-switch mechanism. PMID:24948515 oocyte assays identify tested carrier/kinase pairs; no all-PIN combinatorial inference is made. Full PMID:38278951 adds CXX(X)P S-acylation and PDK1-dependent recruitment/phosphorylation mechanism; these are not merely transplanted PID properties.
ATP binding is core catalytic substrate recognition. Phosphatidylinositol phosphate and phosphatidic-acid binding contribute to membrane recruitment. The actual public Fig.5 image and caption for PMID:27251533 were inspected at https://www.nature.com/articles/nplants2015162/figures/5 (normal caption cache retained); GST-D6PK lipid-strip binding is compared with GST control. Positive in-vitro binding to less physiologically established lipids, including PIP3, is retained non-core rather than declared false because native plant abundance is uncertain. This does not manufacture a native PIP3 signaling pathway. PMID:27836964 supports the polybasic domain; full publisher retrieval was unavailable, so details beyond the abstract are not newly claimed from it.
Nucleus IBA/ISM remain UNDECIDED; membrane recruitment is not a nuclear exclusion experiment. PTN000682243 is retained from the original assertion, with unavailable target-resolved ancestral placement disclosed rather than invented. The inherited NEW regulation-of-auxin-polar-transport annotation is retained. General cell-periphery/basal-region/kinase terms are refined to supported membrane or catalytic terms; no root-organelle narrowing is used.
Final actions: 18 ACCEPT, 9 KEEP_AS_NON_CORE, 6 MODIFY, 1 NEW, 4 REMOVE, 2 UNDECIDED. This panel contains no negated source rows; there are no manufactured NOT assertions. Exact-row payload proof and focused validation are recorded in .cache/module-audit-logs/auxin-polar-six-*. Reciprocal scientific consultation with the parallel annotation reviewer confirmed source-specific localization, integral binding and substrate-assay distinctions.