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Predicted to enable metallocarboxypeptidase activity. Predicted to be involved in peptide metabolic process and protein processing. Predicted to be active in extracellular space. Orthologous to human CPZ (carboxypeptidase Z). [provided by Alliance of Genome Resources, Apr 2025]
A protein domain is a distinct structural or functional region within a protein that can evolve, function, and exist independently of the rest of the protein chain. These domains in rat Cpz often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
Zinc carboxypeptidase
Zn_pept domain
peptidase
metallocarboxypeptidase
Fz domain
Peptidase_M14NE-CP-C_like
M14 family of metallocarboxypeptidases and related proteins
CarboxypepD_reg-like domain
Carboxypeptidase regulatory-like domain
CRD_domain cysteine-rich domain, also known as Fz (frizzled) domain
Pathways
Biological processes and signaling networks where the Cpz gene in rat plays a role, providing insight into its function and relevance in health or disease.
The most significant associations for this gene, including commonly observed domains, pathway involvement, and functional highlights based on current data.
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
Extracellular Space
cell surface
intercellular junctions
extracellular matrix
cellular protrusions
Gene Ontology Annotations
Describes the biological processes, cellular components, and molecular functions associated with the rat Cpz gene, providing context for its role in the cell.
Biological Process
Functions and activities the gene product is involved in
peptide metabolic process
proteolysis
Wnt receptor signaling pathway
protein processing
Cellular Component
Where in the cell the gene product is active
extracellular space
Molecular Function
What the gene product does at the molecular level
zinc ion binding
metallocarboxypeptidase activity
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