VCPIP1, also known as VCIP135, is a deubiquitinating enzyme that functions in p97/p47-mediated Golgi reassembly []. It hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains []. It has also been found to dictate the duration of botulinum neurotoxin type A intoxication []. VCPIP1 can also deubiquitinate SPRTN (a metalloprotease that cleaves DNA-protein crosslinks) and promotes its chromatin relocalization []. VCPIP1 is a member of peptidase family C64.
Deubiquitinating protein VCPIP1, also known as VCIP135, is required for the p97/p47 and p97/p37 pathways and is involved in Golgi and ER membrane fusion. It reverses ubiquitination events that occurs during mitotic disassembly, regulating Golgi membrane dynamics during mitosis. This entry represents the N-terminal domain that interacts with WAC (the WW domain-containing adaptor with coiled coil). This interaction increases the deubiquitinating activity of VCPIP1 and is necessary for p97/p47-mediated Golgi membrane fusion [, ].
