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ADAM metallopeptidase domain 3B, commonly known as cyritestin 2 (ADAM3B), is a member of the ADAM (a disintegrin and metalloproteinase) gene family that encodes multidomain, membrane-anchored proteins characterized by metalloprotease and disintegrin domains[1][2]. In mice, ADAM3 (cyritestin) is a functional sperm membrane protein implicated in mediating sperm-egg binding and fusion during fertilization, primarily through its disintegrin domain, which binds integrin-type receptors on the egg plasma membrane[1][3]. Disruption of the corresponding gene in male mice results in defective sperm-egg membrane adhesion and male infertility[1][3]. However, ADAM3B is not a functional protein in humans: it is considered a pseudogene in humans (non-functional gene locus)[5]; thus, it is not a therapeutically relevant target in human disease, nor is it an established drug target or biomarker. Most evidence for a direct function comes from mouse knockout models and in vitro assays[1][3]. As such, while it is part of the broader ADAM family, which has recognized members with clinical significance (e.g., ADAM10, ADAM17), ADAM3B itself should not be considered a therapeutic target for human diseases[5].
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