Falcon deep research succeeded on the second attempt (IFT74-deep-research-falcon.md; first run timed out at 600 s with no available fallback; rerun with --timeout 2400). It agrees that IFT74's direct molecular role is tubulin binding with IFT81 plus IFT-B organization, and adds 2023 patient studies (Bakey et al., Fassad et al.; not cached) showing an exon-2 (first 40 residues) deletion that separates IFT-B association from tubulin/microtubule binding [file:human/IFT74/IFT74-deep-research-falcon.md "Selected IFT-B subunits, including IFT81, still co-precipitated with exon-2-deleted IFT74, whereas the deleted protein bound microtubules much less effectively in vitro."], with very short motile airway cilia and skeletal ciliopathy. This strengthens beta-tubulin binding as the core MF and supports keeping motile cilium as a correct location.
HPA v25: Basal body (Supported), Centriolar satellite (Supported); main locations Basal body, Centriolar satellite, Golgi apparatus. HPA makes no primary-cilium (shaft) call for IFT74, whereas the module places IFT74 in anterograde trains along the axoneme. This is not a contradiction: IFT-B subunits are concentrated at the ciliary base and only sparsely distributed in moving trains, so antibody sensitivity favours the base; the atlas also stresses cell-type and single-cilium heterogeneity PMID:41005307. GO_REF:0000052 rows: ciliary basal body (ACCEPT), centriolar satellite and Golgi (KEEP_AS_NON_CORE). Core functions agree with the module role "IFT-B core; tubulin binding".
Every IFT-B subunit annotated from PMID:26980730 (Katoh et al. 2016, an IFT-B architecture paper) carries an IDA to GO:0030991 intraciliary transport particle A. This contradicts the paper's own content (which supports the GO:0030992 IFT-B IPI rows from the same paper) and the established biochemistry. Marked REMOVE as a genuinely contradicted claim (likely batch term-selection error), not as second-guessing assay data.