CPA2 (carboxypeptidase A2) encodes a zinc-dependent metallocarboxypeptidase that catalyzes the removal of C-terminal amino acids from proteins, with preference for large aromatic residues 1. The enzyme belongs to the A/B subfamily of metallocarboxypeptidases and shares 60% amino acid sequence identity with CPA1 1. CPA2 is located in a gene cluster with other carboxypeptidase genes (CPA1, CPA4, CPA5) on chromosome 7 1. The protein functions as an extracellular enzyme involved in proteolysis and protein catabolism. Clinical significance of CPA2 is primarily related to pancreatic diseases. While variants in CPA2 are not associated with chr7 pancreatitis 2, rare variants show strong association with acute pancreatitis in patients with acute lymphoblastic leukemia receiving asparaginase therapy. Specifically, a rare nonsense variant (rs199695765) confers extremely high risk for asparaginase-induced pancreatitis (hazard ratio 587) 3. Gene-level analysis revealed an excess of CPA2 variants in pancreatitis patients, with 13 of 24 carriers of risk variants developing the condition 3. This makes CPA2 a critical genetic risk factor for treatment-related pancreatitis in leukemia patients.