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Proteins/UNIPROT:Q96PS8
Aquaglyceroporins form homotetrameric transmembrane channels, with each monomer independently mediating glycerol and water transport across the plasma membrane along their osmotic gradient. Could also be permeable to urea. Among aquaglyceroporins, it exhibits a unique pH-gated glycerol transport activity, being more active at acidic pH. It most likely plays a central role in the efflux of glycerol formed during triglyceride hydrolysis in adipocytes and in glycerol uptake by enterocytes, as both processes occur and are stimulated at acidic pH..
Function from UniProtKB (Q96PS8), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
12 statements
12 statements · 5 reference databases · Subject: AQP10 · Sources: Bgee, Human Protein Atlas, Human-GEM, Reactome, Rhea
5 reactions
3 names
Resolves to: AQP10
Reaction pageReversibleBalancedextracellular space, cytosol
Human-GEM MAR09890CC BY 4.0Reference data
Transported by AQP7B or AQP12B or AQP7 or AQP9 or AQP8 or AQP1 or MIP or AQP2 or AQP5 or AQP4 or CLDN15 or CLDN2 and 5 more alternatives
Reaction pageDirection not assertedBalanced
Rhea RHEA:29667CC BY 4.0Reference data
Transported by AQP7B or AQP7 or AQP9 or AQP1 or AQP2 or AQP11 or AQP3 or AQP10
Reaction pageDirection not assertedBalanced
Rhea RHEA:29675CC BY 4.0Reference data
Transported by AQP7 or AQP9 or SLC14A1 or SLC14A2 or AQP3 or AQP10
Reaction pageDirection not assertedBalanced
Rhea RHEA:32799CC BY 4.0Reference data