Carboxypeptidase A5 (CPA5)

Carboxypeptidase A5 (CPA5) is a metallocarboxypeptidase enzyme of the A/B subfamily, encoded by the CPA5 gene on human chromosome 7[1][2][3][5][6]. It contains an approximately 90-amino acid pro region required for enzyme folding; this pro region is cleaved to activate CPA5[1][2][3]. CPA5 shows substrate specificity for C-terminal hydrophobic residues[1], and is predominantly expressed in tissues such as testis, brain, and pituitary, where it is thought to participate in biosynthesis and intracellular processing of neuroendocrine peptides and neuropeptide precursors[1][2]. In clinical research, CPA5 has been found in non-metastatic colorectal carcinoma cell lines and is absent in metastatic ones, suggesting its loss may be associated with tumor progression and it could serve as a marker for disease status[1]. In animal models, CPA5 is highly expressed during spermiogenesis, but knockout studies suggest it is non-essential for spermatogenesis and fertility[1]. In zebrafish, CPA5 marks a specific mast cell lineage and is regulated by developmental pathways such as Notch signaling[1]. No drugs are currently listed as targeting CPA5, and there are no specific safety concerns noted in the published literature as of this update[1][2][4]. Some external paralogs (like CP-A5 in Entamoeba histolytica) are implicated in infection- and cancer-related processes, but direct translational relevance to the human CPA5 protein requires further investigation[1].

Other names

Carboxypeptidase A5CPA5testicular tissue protein Li 32