Anoctamin (ANO), also known as transmembrane member 16 (TMEM16), is a class of transport proteins, detected in all eukaryotes. There are 10 members of anoctamin family in vertebrates (ANO1-10). The anoctamin proteins are highly hydrophobic and possess a similar structure with eight transmembrane domains, and one re-entry loop that consists of the NH2 and COOH termini protruding into the cytosol. They exert an essential role in ion transport. ANO1 and ANO2 function as Ca2+-activated Cl- channels (CaCCs) in many tissues, involved in transmembrane ion transport, smooth muscle contraction, olfaction, phototransduction, nociception, and control of neuronal excitability. Besides, other members of anoctamin family may be involved in phospholipid scrambling and/or ion channels. Studies have been indicated that ANO6 and ANO7 can produce chloride currents, and ANO6 may be a major regulator for phosphatidylserine translocation from the inner to the outer leaflet of the plasma membrane. Mutations in anoctamin genes may be associated with genetic diseases, such as cancer, cervical dystonia, gnathodyaphyseal dysplasia, Scott syndrome, cerebellar ataxia.
Among these 10 anoctamin proteins, ANO1 and ANO2 have been studied extensively so far. However, the studies of other members of anoctamin family are relatively lacking and their biological roles have not been elucidated completely. The following table shows the detailed descriptions of 10 anoctamin proteins.
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