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Calmodulin-like protein 4 (CALML4) is a calcium-binding protein in humans, classified as an EF-hand protein related to calmodulin[4][5]. It functions as part of the intermicrovillar adhesion complex at the apical surface of epithelial cells, where it regulates the organization, differentiation, and length of microvilli by acting as a light chain for the myosin MYO7B and directing brush border architecture[4][5]. CALML4 is distinct from canonical calmodulins; it does not serve as a broad calcium sensor and is not a recognized therapeutic target such as receptors or enzymes[4]. Diseases linked to its function are rare and nonspecific. There is no evidence for direct drug targeting, biomarker development, or notable therapeutic safety challenges relating to CALML4[4][5].
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