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.
ProtNLM2 output was not consulted. Sources: cached full texts of PMID:24302887 (mouse Wdpcp Cys40), PMID:27158779 (CPLANE, Xenopus/mouse/human genetics), PMID:35427153 (CPLANE cryo-EM and lipid binding), PMID:20671153 (Xenopus Fritz, the donor of the ISS rows), the UniProt record, PANTHER PTHR13667 PAINT/entries files, and the falcon deep-research file, which was used only to find sources.
O95876 is the reviewed, canonical Swiss-Prot entry (isoform 1, 746 aa). It is not a fragment or an alternative gene model. UniProt cautions that Met-1 or Met-34 may be the initiator. That fits the structure paper: "Compared to mouse, the human Wdpcp has an N-terminal extension of ~35 residues that is not resolved in the map" PMID:35427153. Mouse Q8C456 is 722 aa, Xenopus Q32NR9 708 aa. The WD repeats (326-414) and the PIP-binding C-terminal tail (last ~60 residues) are both present.
PANTHER puts human WDPCP, mouse Wdpcp (Q8C456), rat (B1WC10) and Xenopus (Q32NR9) in the same subfamily, PTHR13667:SF5. The four PAINT IBDs (cilium organization, nervous system development, axonemal basal plate, establishment of protein localization) sit at the bilaterian node PTN001007408, seeded from MGI and Xenopus (plus fly fritz for nervous system development). That justifies transferring the mouse and Xenopus experimental functions. The family review interpro/panther/PTHR13667/PTHR13667-review.yaml agrees with SF5 placement. It lists no mouse representative, but there is no disagreement.
Mouse Wdpcp (Q8C456, MGI:2144467) is a same-subfamily (SF5) ortholog and the PAINT seed. It is the best-characterized ortholog (Cys40 mutant, CPLANE structure with lipid mapping). There is no mouse review in the repo.
No module covers CPLANE. modules/bbsome.yaml mentions WDPCP/BBS15 only to place it out of scope.