1.A.17.1.26
Anoctamin-10 or TMEM16K of 660 aas and 9 or 10 TMSs.  In the presence of Ca²⁺, TMEM16K directly binds Ca²⁺ to form a stable complex (Ishihara et al. 2016). In the absence of Ca²⁺, TMEM16K and TMEM16F (TC# 1.A.17.1.4) aggregate, suggesting that their structures are stabilized by Ca²⁺.  Mutagenesis of acidic residues in TMEM16K's cytoplasmic and transmembrane regions identified five residues that are critical for binding Ca²⁺. These residues are well conserved between TMEM16F and 16K, and point mutations of these residues in TMEM16F reduced its ability to support Ca²⁺-dependent phospholipid scrambling (Ishihara et al. 2016). Phosphatidyl serine in the ER of mammalian cells is predominantly localized to the cytoplasmic leaflet, but TMEM16K directly or indirectly mediates Ca²⁺-dependent phospholipid scrambling (Tsuji et al. 2019). Ano10 plays roles in cell division, migration, apoptosis, cell signalling, and developmental processes (Chrysanthou et al. 2022).  There is structural heterogeneity within the ion and lipid channel of TMEM16F (Ye et al. 2024).  It coordinates organ morphogenesis in the urochordate notochord (Liang et al. 2024).