Claudin and membrane-domain mappings are consistent with a structural tight-junction protein; the broad membrane term can be made compartment-specific.

O88552 is mouse Cldn2. Its direct junctional, adhesion and self-association annotations provide genuine family-transfer grounding rather than a mistaken Cldn14 identity.

The original PTN000243505 and all descendant identifiers are retained. Current experimental compartment records corroborate the curated transfer, without reconstructing historical ancestral placement.

Combined Cldn14 ortholog, Ensembl, domain and subcellular-location mappings are concordant with target junctional and plasma membrane evidence.

The exact CLDN14 supplement row reports ER/PM for the human NM_012130/AAG60052 ORF in HEK293T cells; Figure 4 shows ER-marker overlap. This is tagged overexpression localization, not a demonstrated ER-specific function.

Exact positive CLDN14 pairs with MAL, CTXN3 and PLLP occur in three two-hybrid configurations each. Pairwise retesting and sequence verification support the screen records; native tissue mechanisms are not established for these pairs.

The human CLDN14 terminal ten-residue peptide binds specific PDZ-domain fragments in holdup assays. The literal records resolve 20 partners and 61 positives; domain preparations and fragment assays do not establish all full-length native complexes.

The complete original paper identifies YAP WW-domain binding to WBP proline-rich ligands using fusion-protein and mutational assays. It does not support the CLDN14 tight-junction assembly attribution.

Mouse CLDN14 associates with human CLDN16 in membrane two-hybrid and coimmunoprecipitation assays and reduces cation permeability in LLC-PK1 models. Mouse renal expression responds to calcium-sensing regulation; the older oligomer interpretation is retained at that assay scope.

CLDN14 forms a barrier in claudin-deficient MDCKII cells and participates in CLDN19-containing strands that replace CLDN16. Tagged cell models distinguish cis/trans organization, and mouse kidney studies support changing junctional composition. The inspected supplement does not identify the CLDN14 transgene species.

The authentic abstract reports deafness and hair-cell degeneration in Cldn14-null mice, alongside increased epithelial resistance and reduced cation permeability after claudin-14 expression. These phenotypes contextualize the barrier without creating a separate developmental process assertion.

The authentic abstract identifies CLDN14 mutations in recessive human deafness and reports mouse inner-ear expression. It does not supply a fully inspected human protein assay.

The authentic abstract reports calcium-independent cell aggregation for claudin-1, -2 and -3 transfectants. Current mouse Cldn2 GOA contains the direct adhesion annotation; full assay Methods remain inaccessible.

Selected full Methods and Results establish claudin-2 homopolymers and paired strands in mouse L cells, with selective heterotypic compatibility. These are donor-family experiments, not direct human CLDN14 assays.

Endogenous CLDN14 is restricted to an apical subdomain of mammalian cochlear junctions. Mouse organ-of-Corti cDNA-derived GFP-claudin-14 forms parallel fibrils in COS-7 cells without recruiting the tested catenins; the native opposing-cell partner remains unresolved.

The authentic abstract reports that wild-type claudin-14 forms tight junctions in L-M fibroblasts whereas deafness-associated V85D and G101R variants fail in distinct ways. Full Methods and exact construct-product mapping were not recovered.