Serine protease 33 (PRSS33)

Serine protease 33 is a human protein belonging to the serine protease family of enzymes, encoded by the *PRSS33* gene. Serine proteases are enzymes that cleave peptide bonds in proteins via a serine residue in their active site, and are found widely in both eukaryotes and prokaryotes. PRSS33 is predicted to enable serine-type endopeptidase activity, specifically cleaving substrate peptides before arginine (Arg) residues. It is localized to the cytoplasm and contributes generally to proteolysis—protein degradation—within the cell. An important paralog is PRSS27. While serine proteases as a class have substantial relevance for diseases—including roles in cancer, inflammation, and cardiovascular conditions—the direct role of serine protease 33 (PRSS33) in specific diseases remains to be established. No drugs are known to act specifically on this target, and its clinical significance is not yet defined.

Other names

PRSS33