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Valosin-containing protein (VCP or p97) belongs to the AAA (ATPase associated activities) family and acts as a molecular chaperone to a wide variety of cellular activities. Some of these activities include the alteration of both nuclear and mitotic golgi membranes, ubiquitin-proteasome dependent protein degradation, regulation of the NF-kappa b pathway, and extraction of membrane proteins. VCP has been shown to contain a substrate binding domain (N) and two conserved ATPase domains (D1 and D2). The three dimensional structure of VCP resembles that of a cylinder with the D1 and D2 stacked upon one another in a homo-hexameric ring formation. VCP is involved in the formation of neuronal inclusion bodies in neurodegenerative disease such as Parkinson's Disease. VCP has a calculated molecular weight of 89 kDa and an apparent molecular weight of 90-100 kDa.