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EF-hand calcium-binding domain-containing protein 1 (CLXN, also known as Calaxin) is a calcium-binding protein that is a component of the outer dynein arm-docking complex (ODA-DC)[3][7][5]. It mediates the attachment of the outer dynein arms to doublet microtubules in motile cilia and flagella, which is essential for their movement[3][11][7][5]. The protein plays a key role in cilium motility, regulation of sperm flagellar motility, and is required for proper assembly of the outer dynein arms onto ciliary microtubules[3][7][5]. Calaxin contains EF-hand domains, which are structural motifs involved in calcium ion binding[1][6][10]. Pathogenic variants are associated with primary ciliary dyskinesia, Kartagener syndrome, and related disorders affecting motile cilia and sperm function[3][11]. There is no evidence currently that this protein serves as a therapeutic target for drugs, nor are there established interacting drugs, known mechanisms of drug action, or clinical biomarkers for CLXN[3].
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