Family

Aquaporin 6 (IPR023254)

Short name: Aquaporin_6

Family relationships

Description

Aquaporins are water channels, present in both higher and lower organisms, that belong to the major intrinsic protein family. Most aquaporins are highly selective for water, though some also facilitate the movement of small uncharged molecules such as glycerol [PMID: 15340377]. In higher eukaryotes these proteins play diverse roles in the maintenance of water homeostasis, indicating that membrane water permeability can be regulated independently of solute permeability. In microorganisms however, many of which do not contain aquaporins, they do not appear to play such a broad role. Instead, they assist specific microbial lifestyles within the environment, e.g. they confer protection against freeze-thaw stress and may help maintain water permeability at low temperatures [PMID: 16406529]. The regulation of aquaporins is complex, including transcriptional, post-translational, protein-trafficking and channel-gating mechanisms that are frequently distinct for each family member.

Structural studies show that aquaporins are present in the membrane as tetramers, though each monomer contains its own channel [PMID: 11780053, PMID: 15377788, PMID: 14691544]. The monomer has an overall "hourglass" structure made up of three structural elements: an external vestibule, an internal vestibule, and an extended pore which connects the two vestibules. Substrate selectivity is conferred by two mechanisms. Firstly, the diameter of the pore physically limits the size of molecules that can pass through the channel. Secondly, specific amino acids within the molecule regulate the preference for hydrophobic or hydrophilic substrates.

Aquaporin-6 forms a water-specific channel [PMID: 10318966] that participates in distinct physiological functions, such as glomerular filtration, tubular endocytosis and acid-base metabolism. It is found in the kidney and gastrointestinal tract [PMID: 19811639], and is also localised in the inner ear of mammals [PMID: 17318586]. It is a pH-regulated anion channel [PMID: 19096784], and has been found to bind calmodulin in a calcium-dependent manner, possibly providing a vital clue to its physiological role in the kidney [PMID: 19336226].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PRINTS