Cytosolic aminopeptidase 1 (IPR033852)

Short name: Cytosolic_aminopeptidase_1

Overlapping homologous superfamilies


Domain relationships


The entry includes the peptidase M14-like domain of cytosolic carboxypeptidase 1 (CCP1; MEROPS identifier M14.028), also known as Nna-1 (Nervous system Nuclear protein induced by Axotomy) or ATP/GTP binding protein (AGTPBP-1), and related proteins [PMID: 11083920, PMID: 17244817, PMID: 17244818]. The peptidase M14 family of metallocarboxypeptidases are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CCP1-like proteins are active metallopeptidases that are thought to act on cytosolic proteins such as alpha-tubulin, to remove a C-terminal tyrosine. CCP1-like proteins from the different phyla are highly diverse, but they all contain a unique N-terminal conserved domain right before the CP domain [PMID: 17244817]. It has been suggested that this N-terminal domain might act as a folding domain.

CCP1 is widely expressed in the developing and adult nervous systems, including cerebellar Purkinje and granule neurons, miral cells of the olfactory bulb and retinal photoreceptors. CCP1 is also induced in axotomized motor neurons [PMID: 18602413]. Mutations in CCP1 cause Purkinje cell degeneration (pcd) [PMID: 16952463]. The CCP1 CP domain is required to prevent the retinal photoreceptor loss and cerebellar ataxia phenotypes of pcd mice, and a functional zinc-binding domain is needed for CCP1 to support neuron survival in these mice.

GO terms

Biological Process

GO:0021702 cerebellar Purkinje cell differentiation

Molecular Function

GO:0004181 metallocarboxypeptidase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.