InterPro-based family, transporter and membrane mappings identify CLC transport biology but do not by themselves distinguish a channel from a coupled chloride/proton exchanger.

The original ISS annotation names rat Clcn4 P51794; its current experimental early-endosome record is authenticated separately from the human sorting experiments.

Current source records authenticate the PAINT nodes and experimental descendant grounding. Historical family-tree, MSA and IBD reconstruction is unavailable; target self-inclusion is legitimate, not circular.

Specific UniProt subcellular-location mappings correspond to distinct ER, early, late, lysosomal and recycling membrane contexts.

Current ARBA00026476 conditions match target sets 1 and 9; its channel output is refined using direct exchange evidence.

The recovered abstract reports an acid-activated outward current from a human skeletal-muscle clone expressed in CHO cells. That positive observation is preserved while later direct proton assays resolve the exchange mechanism.

Full-length tagged human ClC-4 localizes with ER markers and fractions in HEK293 cells; separate mouse-brain fractionation is concordant. The early N-terminal retention model is distinguished from later partner-dependent sorting and CBS-linker results.

Human G544R ClC-4 has greatly reduced oocyte current, with human HeLa localization and construct controls examined. Proton coupling is not directly measured by that experiment.

Human variant oocyte-current measurements support altered transport. Mouse neuronal knockdown/rescue and knockout morphology are separate evidence and do not establish another molecular activity.

Human WT and variant ClC-4 show ER localization in COS-7 cells and variant-dependent oocyte currents; most tested variants reduce current, whereas Asp15Asn is WT-like. Structural interpretation uses an algal model.

Human long ClC-4 associates with mouse ClC-3 splice variants, which determine endolysosomal versus recycling targeting. Unpartnered long protein accumulates in the ER; the tested short form is poorly expressed and lacks measured currents under these conditions.

The systematic human binary-interaction screen includes an exact positive CLCN4–ABHD5 pair in three literal two-hybrid records. General orthogonal validation of the dataset is not automatically assigned to this pair.

The original cloning study describes a predicted 760-residue protein homologous to voltage-gated chloride channels; the recovered abstract does not demonstrate coupled proton transport.

The P51793 target is an alternative catalyst-set member for endosomal chloride/proton exchange, not a transported solute or an obligate CLCN4/5/6 complex.

The broad ion-transport pathway contains the explicit CLC exchange reaction and its endosome-membrane P51793 entity.

Independent surface-pH experiments identify ClC-4/5 proton export; the authentic abstract supports exchange, while the original full Methods were not recovered.

Voltage-clamp and pH measurements directly show ClC-4-dependent proton transport against its gradient. Mutant and channel controls distinguish coupling; the reported stoichiometry estimate is rough rather than a precise 2:1 determination.

TMEM9-family proteins affect CLC transporter abundance and inhibit transport. Human ClC-4 association and targeted ClC-3 transport-dead/ClC-4 vacuolization assays supply target evidence; numerous other assays concern ClC-3 or ClC-5 and are kept separate.

Human ClC-4 disease variants alter transport with mouse ClC-3c in voltage- and pH-dependent ways. Some effects differ from the corresponding homomer currents, limiting simple loss-of-function classifications.

Mouse Clcn4 loss changes hippocampal network activity with regional specificity. The proposed downstream channel-trafficking model remains a hypothesis rather than an additional demonstrated human ClC-4 activity.