Serine protease S9B/DPPIV
IPR050278
Definition
The peptidase S9B family, also known as the DPPIV subfamily, includes serine proteases with dipeptidyl peptidase activity, which cleave off N-terminal dipeptides from proteins with a preference for a proline residue at the penultimate position. Members of this family are involved in various physiological processes, including immune response regulation, tissue remodeling, and cell signaling. Some proteins within this family act as venom toxins, contributing to the processing of venom proteins and modulation of immune cell chemotaxis. Others are involved in cell surface expression and modulation of potassium channels, although they lack dipeptidyl aminopeptidase activity. The family also includes prolyl tripeptidyl peptidases that release tripeptides from protein N-termini, and proteins that participate in extracellular matrix degradation and play roles in tissue remodeling, fibrosis, wound healing, inflammation, and tumor growth.
6 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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