InterPro associations identify CLC transport domains; direct coupling evidence makes chloride:proton antiporter activity more informative than broad channel/transporter labels.

The exact PAINT node and descendant identifiers are preserved. Current experimental grounding corroborates several assertions, while historical tree/MSA placement remains uninspected.

Subcellular-location mappings are considered with independent target localization, retaining endosomal, Golgi and surface contexts separately.

Human Protein Atlas target records support Golgi and plasma membrane locations, with a cytosolic signal in U-2 OS cells. Selected images were viewed; these are cell-line observations.

Rat P51796 is Clcn5. The ortholog transfer is biologically concordant with direct human endosomal membrane localization.

ARBA00026476 currently reaches the target through two condition sets. The other two current rule snapshots do not reconstruct their historical target route; that is not evidence of biological absence.

Combined ortholog/domain mappings are genuine source assertions. Mechanistic or compartment refinements use independently established human target evidence.

Human fetal/postnatal kidney and mouse development studies establish renal membrane and segmental distribution. Fetal human staining is less polarized; detailed mouse apical observations are not relabeled as human experiments.

Purified human C-terminal domains directly bind ATP, ADP and AMP and show weak self-association. Nucleotide-binding-site mutations change currents in an uncoupled E211A background, whereas wild-type-background currents remain unchanged.

Official Table 1 positively detects human placental ClC5 with seven peptides, but its adjusted enrichment P value is 1. Detection and significant lysosomal enrichment are distinct conclusions.

Human ClC-5 tail and KIF3B constructs associate in multiple assays. KIF3B affects surface abundance and uptake differently in HEK293 and polarized opossum kidney cells; ClC-5 is not assigned kinesin motor activity.

The authentic abstract describes YTS-cell membrane proteomics, but the exact ClC-5 target result and peptides remain inaccessible.

The complete abstract connects human CLCN5 variants with renal disorders and reduced oocyte currents. It does not independently establish proton coupling or provide the unrecovered full assay details.

P51795 is an alternative catalyst-set member for chloride/proton exchange in the endosome membrane; the set does not assert an obligate CLCN4/5/6 complex.

The broad pathway includes the explicit CLC exchange reaction and target entity, supporting a chloride-specific transmembrane process.

ClC-5-dependent proton flux, gradient tests and uncoupling mutants distinguish exchange from passive chloride conduction. The original stoichiometry estimate is rough rather than a precise universal cycle count.

Mouse E211A knock-in uncouples chloride conduction from proton exchange. Renal endocytic defects persist despite normal bulk ATP-driven vesicle acidification, separating coupled exchange from a simple shunt-conductance model.

Human ClC-5 expressed in HEK293 cells contributes a bafilomycin-insensitive vesicular acidification component, with transport mutants as controls. Separate opossum-cell knockdown and a proposed proton-entry model are kept at their assay scope.

Human ClC-5 constructs in oocytes support direct chloride/proton transport measurements; epithelial-cell localization distinguishes wild-type endosomal/surface pools from mutant retention. Apparent stoichiometry is calculated from transport energetics.

TMEM9-family partners associate with and regulate human ClC-5 in heterologous systems, while mouse renal experiments distinguish TMEM9B-dependent transporter stability. Tagged constructs and other CLC-family controls are not treated as interchangeable.