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Centrin-3 (CETN3) is a small, evolutionarily conserved calcium-binding protein belonging to the EF-hand superfamily, highly homologous to yeast CDC31 and found abundantly at the centrosome in mammalian cells[2][3]. It contains four EF-hand domains and functions as a calcium sensor, regulating centriole duplication and centrosome assembly through interaction and inhibitory regulation of Mps1 kinase activity[1][2][3]. Upon calcium binding, Centrin-3 undergoes conformational changes that facilitate its interaction with target peptides such as XPC and Kar1, modulating protein–protein interactions critical for centrosome function, genomic stability, and cell cycle progression[1][2]. Dysregulation of CETN3, including suppression via microRNA-410, has been implicated in certain cancer types and may contribute to tumorigenesis in a context-dependent manner[2][3]. Alternative splicing generates several isoforms of Centrin-3, but no functional redundancy with Centrin-2 has been observed in vertebrates[1].
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