Inactive dipeptidyl peptidase 10 (DPP10)

Inactive dipeptidyl peptidase 10 (DPP10) is a single-pass type II membrane glycoprotein of the S9B serine protease subfamily, rendered enzymatically inactive by the substitution of a catalytic serine in its active site[1][3]. Despite lacking protease function, DPP10 serves as an essential auxiliary subunit that binds to and modulates the biophysical properties, expression, and localization of specific voltage-gated potassium channels, particularly Kv4.x family members[1][2]. DPP10’s activity influences neuronal excitability and airway epithelial physiology; it has key roles in regulating ion channel gating kinetics and facilitating cell surface localization of the channels[1][2][3]. Genetic variants or mutations in DPP10 are associated with asthma, neurodegenerative diseases (including Alzheimer’s and frontotemporal dementia), and autism spectrum disorders[2][3]. The absence of protease activity makes DPP10 unique among dipeptidyl peptidases, and its primary molecular role is in protein-protein interaction rather than catalysis[1][2][3]. There are currently no approved drugs known to interact directly with DPP10, nor established clinical biomarkers or mechanisms of action through inhibition/activation, but the protein is being studied for its role as a modulator of ion channel complexes and as a biological link to respiratory and neurological conditions[1][2][3].

Other names

DPRP3KIAA1492DPP XDPL2DPPYDipeptidyl peptidase IV-related protein 3Dipeptidyl peptidase XDipeptidyl peptidase-like protein 2DPRP-3