Pantothenate kinase 4 (inactive) (PANK4)

Pantothenate kinase 4 (inactive) is a human protein encoded by the PANK4 gene. Unlike its paralogs (PANK1–3), which possess pantothenate kinase activity and catalyze the first step in coenzyme A (CoA) biosynthesis, PANK4 is a bifunctional protein consisting of an N-terminal type II pantothenate kinase-like domain and a C-terminal phosphatase domain. However, due to specific substitutions at key catalytic residues, the human enzyme is catalytically inactive as a kinase and acts instead as a pseudoenzyme[1][3]. Its C-terminal phosphatase domain is active and acts preferentially on 4'-phosphopantetheine and oxidatively damaged forms, suggesting a role in preventing the accumulation of toxic intermediates and regulating intracellular CoA levels[2]. PANK4 is most highly expressed in muscle but is present in all tissues[2][4][5]. Disease associations include certain types of cataract[2]. Currently, there are no known clinically approved drugs targeting PANK4, and it is not considered a classic therapeutic target.

Other names

4'-phosphopantetheine phosphatasehPanK4FLJ10782Inactive pantothenic acid kinase 4CTRCT49pantothenic acid kinase 4

None known