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Abhydrolase domain-containing protein 17A (ABHD17A) is an enzyme of the alpha/beta hydrolase superfamily that functions as a protein depalmitoylase, hydrolyzing palmitate groups from S-acylated cysteine residues. ABHD17A is membrane-associated due to a palmitoylated N-terminal cysteine cluster and acts on various substrates including N-Ras, PSD95, and particular domains of ion channels such as the BK channel. Its activity regulates protein localization, influences signal transduction, and contributes to dynamic cellular processes such as the assembly of the NLRP3 inflammasome. ABHD17A has been implicated in neurological disorders and may play a modulatory role in oncogenic signaling through its regulation of protein palmitoylation and trafficking[1][2][3][4].
Enzymatic hydrolysis (removes palmitate from S-acylated cysteine residues); Relocalization of membrane-associated proteins (like N-Ras, PSD95) by altering palmitoylation status
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