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Enkurin is a novel calmodulin- and TRPC channel-binding protein first identified in sperm, where it colocalizes with TRPC1, TRPC2, and TRPC5 channels but not TRPC3[1]. It carries three distinct protein interaction domains: a C-terminal region essential for channel interaction, an IQ motif that binds calmodulin in a Ca²⁺-dependent manner, and a proline-rich N-terminus that associates with SH3 domain proteins (such as the p85 subunit of PI3K)[1]. Enkurin is thought to function as an adaptor, localizing Ca²⁺-sensitive signaling machinery to TRPC channels, thereby facilitating calcium-mediated signal transduction—particularly in mammalian sperm, where it is involved in receptor-evoked Ca²⁺ influx essential for the acrosome reaction[1]. While it is not classified as a receptor, ion channel, or enzyme, enkurin plays a specialized role as a signaling scaffold/adaptor. It is most highly expressed in testis and vomeronasal organ, with weaker expression in other tissues[1].
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