CPD Gene: Carboxypeptidase D - Function, Expression, Mutations | NCBI, UniProt, ClinVar

CPD (Carboxypeptidase D) encodes a metallocarboxypeptidase that cleaves C-terminal basic amino acids from proteins. It is involved in protein processing and trafficking, particularly in the trans-Golgi network and endosomal system. The enzyme is widely expressed and plays roles in neuropeptide processing, hormone maturation, and receptor recycling.

Tissue Expression

Cell Line Expression

Hotspot Mutations

Mutation functional classification

• Peptide hormone processing

• Neurotransmitter release cycle

• Lysosomal protein degradation

Carboxypeptidase D (CPD) is a 180 kDa transmembrane metallocarboxypeptidase that removes C-terminal arginine or lysine residues from polypeptide substrates. It localizes primarily to the trans-Golgi network and endosomes, where it processes prohormones, neuropeptides, and other proteins. CPD contains three carboxypeptidase-like domains, though only the first two are catalytically active. The protein is essential for proper protein trafficking and maturation.