Anoctamin-6 (ANO6)

Anoctamin-6 (ANO6), also known as transmembrane protein 16F (TMEM16F), is a **dual-function membrane protein** that acts as both a *small-conductance calcium-activated nonselective cation (SCAN) channel* and a *calcium-activated phospholipid scramblase*[1][3][4]. ANO6 mediates the Ca2+-dependent externalization of phosphatidylserine on the cell surface, an essential process for platelet procoagulant activity, membrane repair, and various forms of cell–cell fusion including roles in viral infection and bone mineralization[1][2][3][4]. Mutations or loss of function in ANO6 cause **Scott syndrome**, a rare inherited bleeding disorder due to defective phospholipid scrambling in platelets[2][3]. ANO6 is distinguished from canonical chloride-selective anoctamin family members (like ANO1/TMEM16A) by its dual activity as an ion channel and phospholipid scramblase. As a potential target, it is of interest in disorders of hemostasis, inflammatory processes, and viral syncytia (e.g., COVID-19)[2][3]. No drugs are currently approved that target ANO6 directly, but it remains under active investigation as a therapeutic target and biomarker candidate.

Other names

ANO6TMEM16FSCAN channelDKFZp313M0720Small-conductance calcium-activated nonselective cation channelTransmembrane protein 16FBDPLT7SCTSanoctamin-6small-conductance calcium-activated nonselective cation channelsmall conductance calcium activated nonselective cation channeltransmembrane protein 16F[2][4]

Modulation of ANO6's calcium-activated phospholipid scramblase activity or cation channel function alters phosphatidylserine exposure and thus can affect blood coagulation, cell death, or fusion events[1][3].