Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2.Dipeptidyl peptidases (DPPs) mediate regulatory activity of their substrates and have been linked to a variety of diseases including type 2 diabetes, obesity and cancer. DPPs have post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. DPPs can bind specific voltage-gated potassium channels and alter their expression and biophysical properties and may also influence T cells. DPP proteins include DPRP1, DPRP2, DPP3, DPP7, DPP10, DPPX and CD26. DPRP2 (dipeptidyl-peptidase IV-related protein 2), also known as DPP9 (dipeptidyl-peptidase 9), or DP9, is a member of the peptidase S9B family of proteins that exhibit prolyl oligopeptidase activity. DPRP2 localizes to the cytoplasm and is ubiquitously expressed with predominant expression in heart, muscle and liver. DPRP2 may play an important role in the regulation of signaling by peptide hormones.