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Kyphoscoliosis peptidase (KY) is a structural protein localized to the Z-disk of skeletal muscle, where it interacts with other sarcomeric and immunoglobulin-like proteins (e.g., FLNC, IGFN1, myosin binding protein C) to maintain normal protein organization and muscle integrity[2]. The protein belongs to the transglutaminase-like superfamily and contains a conserved transglutaminase/protease domain, but biochemical assays indicate the domain is not enzymatically active in humans. Instead, KY is required for normal maturation, stabilization, and response to mechanical stress in muscle, and its dysfunction provokes severe myopathies with muscle weakness, protein aggregation (notably filamin C), and impaired muscle hypertrophy responses[1][2][3][4]. KY may also have nuclear localization in human cells, possibly reflecting evolved functions in primates[2]. While suggested as a candidate biomarker for some muscle and cancer diseases, KY is not an established therapeutic target and no drugs directly modulate its activity[1][2][4].
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