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Protein transport protein Sec23B is a core component of the coat protein complex II (COPII), which mediates vesicle formation from the endoplasmic reticulum (ER) to the Golgi apparatus[1][3][4]. SEC23B acts as a GTPase-activating protein for SAR1, facilitating vesicle budding and cargo selection during ER-to-Golgi transport[1][5]. It is structurally composed of five domains (zinc finger, trunk, β-barrel, α-helix, and gelsolin-like domains)[1], and has functional overlap with its paralog SEC23A, though SEC23B’s deficiency in humans primarily leads to congenital dyserythropoietic anemia type II due to defective red blood cell maturation[3]. SEC23B is also involved in regulating autophagy and maintaining secretory tissue integrity[1][5]. Abnormal SEC23B function is implicated in certain rare genetic diseases and has emerging links to cancer biology, but there are currently no clinically approved drugs that target it directly[1][3].
Not applicable; not directly targeted by small molecules or biologics in current clinical practice[3].
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