AQP10 is an aquaglyceroporin that forms homotetrameric transmembrane channels mediating water and glycerol transport across cell membranes along osmotic gradients 1. Among aquaglyceroporins, AQP10 exhibits unique pH-gated glycerol transport activity, being more active at acidic pH 123. AQP10 is permeable to glycerol, water, urea, and boric acid 45. In humans, AQP10 is expressed selectively in the small intestine (duodenum and jejunum), with two isoforms showing distinct subcellular localizations: one in capillary endothelium and another in gastro-entero-pancreatic endocrine cells 6. AQP10 likely plays central roles in glycerol efflux during triglyceride hydrolysis in adipocytes and glycerol uptake by enterocytes, processes stimulated at acidic pH 123. In the digestive system, AQP10 participates in glycerol metabolism, though its specific functions remain incompletely characterized 7. Notably, AQP10 is a pseudogene in mice, limiting translational research models 8. Evolutionary analysis reveals that ray-finned fish AQP10 paralogs have secondarily reduced urea and boric acid permeability while retaining water and glycerol transport 5.