WDPCP is a CPLANE ciliary scaffold with an independent actin/septin/polarity role. Mouse microscopy and perturbation establish ciliary-base, cytoplasmic actin and focal-adhesion pools. Recombinant structural work demonstrates individual WDPCP phosphoinositide binding in its C-terminal tail. The full2016paper explicitly reports human WDPCP variants and relevant digit/tongue/palate phenotypes.
The horse N-terminal difference resembles the approximately35-residue human extension relative to mouse reported in the structure. The conserved scaffold supports broad ciliary/cytoskeletal predictions. A separate nine-residue deletion affects the lipid-binding tail; disorder does not imply that deletion is functionally irrelevant, and exact lipid affinity remains unresolved.
The reproducible alignment, source paths and hashes are in the paired comparison. Current UniProt sequences have not been proven identical to the original ProtNLM input sequences. Sequence anomalies are therefore recorded as model/transfer limitations, not as proven wrong-input pipeline errors.
Distinguish transition-zone/base localization from the axonemal shaft. Test the tail deletion before transferring quantitative phosphoinositide affinity.
Every seeded annotation receives a current assessment. UNDECIDED marks unresolved source-specific or biological evidence; these are initial reviews rather than a claim that every original experimental assay has been independently reproduced or verified. The human Edison report is retained as a research synthesis and source-finding aid; decisive YAML excerpts cite primary publications, source records or reproducible analysis. The validator advisory to cite the deep-research file is deliberately not satisfied by citing AI prose as biological proof.