Anoctamin-6 (ANO6, TMEM16F) is a member of the Anoctamin chloride channel family. This family includes 10 proteins: ANO1-ANO10 that are encoded by the conserved TMEM16A-K genes. Anoctamin-6 acts as calcium (Ca²⁺)-activated chloride (Cl⁻) channel. It generates an outwardly rectifying Cl⁻ current when activated by a large increase in local intracellular Ca²⁺ concentrations¹_. ANO6 structure includes eight transmembrane domains and cytosolic amino- and carboxyl termini. There is a high sequence identity in the putative transmembrane domains and more divergent in other regions^2,3.

ANO6 has also been shown to operate as a Ca²⁺-activated phospholipid scramblase resulting in movement of phosphatidylserine from the inner to the outer leaflet of the plasma membrane bilayer. ANO6 is also involved in bone mineralization, cell volume regulation, cell proliferation and apoptosis^1,2. ANO6 is expressed in cyst-forming epithelial cells together with ANO1.

A mutation in the ANO6 gene is linked to Scott Syndrome, a rare inherited bleeding disorder, characterized by altered Ca²⁺-dependent platelet signaling with defective phosphatidylserine exposure and microparticle formation. Deletion of ANO6 in mice shows reduced skeleton size, skeletal deformities, and mineralization defects^4,5.