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Predicted to enable calcium-dependent cysteine-type endopeptidase activity and identical protein binding activity. Predicted to be involved in proteolysis. Predicted to act upstream of or within calcium-dependent self proteolysis. Predicted to be located in Golgi apparatus. Predicted to be active in cytoplasm. Orthologous to human CAPN8 (calpain 8). [provided by Alliance of Genome Resources, Jul 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 Capn8 often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
The penta-EF hand (PEF) family
Calpain family cysteine protease
calpain
peptidase
EFh
Calpain_III
CysPc
identical protein binding
Pathways
Biological processes and signaling networks where the Capn8 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.
binds
miR-132-3p (and other miRNAs w/seed AACAGUC)
miR-382-5p (miRNAs w/seed AAGUUGU)
miR-293-5p (and other miRNAs w/seed CUCAAAC)
disease
polycystic kidney disease
regulated by
olanzapine
Subcellular Expression
Locations within the cell where the protein is known or predicted to be active, providing insight into its function and cellular context.
Unknown
Gene-Specific Assays for Results You Can Trust
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