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Carboxypeptidase A6 is a secreted metallocarboxypeptidase enzyme encoded by the CPA6 gene, which removes C-terminal hydrophobic amino acids from peptides and proteins[1][2][4][5]. It is highly expressed in certain regions of the brain during development, binds tightly to the extracellular matrix, and participates in the processing of neuroendocrine signaling peptides such as enkephalin, angiotensin I, and neurotensin[1][2]. Mutations in CPA6 have been linked to forms of epilepsy, febrile seizures, and Duane retraction syndrome, indicating its relevance in neurological health and disease[1][2][3][5]. The enzyme is unique within the metallocarboxypeptidase family by virtue of its substrate specificity and tight ECM binding[1]. The precise in vivo substrate repertoire and physiological functions are still being characterized, but loss of CPA6 activity is considered deleterious, particularly to neural development and function[1][3].
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