Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).


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Aquaporins and aquaglyceroporins are membrane channels that allow the permeation of water and certain other small solutes across the cell membrane. Since the isolation and cloning of the first aquaporin (AQP1) [3], 12 additional members of the family have been identified, although little is known about the functional properties of two of these (AQP11; Q8NBQ7 and AQP12A; Q8IXF9). The other 11 aquaporins can be divided into two families (aquaporins and aquaglyceroporins) depending on whether they are permeable to glycerol [2]. One or more members of this family of proteins have been found to be expressed in almost all tissues of the body. Individual AQP subunits have six transmembrane domains with an inverted symmetry between the first three and last three domains [1]. Functional AQPs exist as tetramers but, unusually, each subunit contains a separate pore, so each channel has four pores.


AQP0 Show summary »

AQP1 Show summary »

AQP2 Show summary »

AQP3 Show summary »

AQP4 Show summary »

AQP5 Show summary »

AQP6 Show summary »

AQP7 Show summary »

AQP8 Show summary »

AQP9 Show summary »

AQP10 Show summary »

Further reading

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How to cite this family page

Database page citation:

Aquaporins. Accessed on 24/07/2014. IUPHAR/BPS Guide to PHARMACOLOGY,

Concise Guide to PHARMACOLOGY citation:

Alexander SPH, Benson HE, Faccenda E, Pawson AJ, Sharman JL, Catterall WA, Spedding M, Peters JA and Harmar AJ, CGTP Collaborators. (2013) The Concise Guide to PHARMACOLOGY 2013/14: Ion Channels. Br J Pharmacol. 170: 1607–1651.