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Enables cysteine-type endopeptidase activity. Involved in several processes, including AIM2 inflammasome complex assembly; positive regulation of canonical NF-kappaB signal transduction; and positive regulation of interleukin-1 beta production. Acts upstream of or within several processes, including membrane hyperpolarization; mitochondrial depolarization; and positive regulation of cytokine production. Located in extracellular region. Part of IPAF inflammasome complex. Is active in cytosol. Is expressed in several structures, including forelimb mesenchyme; knee joint; oocyte; small intestine; and telencephalon. Orthologous to human CASP1 (caspase 1). [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 mouse Casp1 often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
CARD domain binding
CASc
Caspase recruitment domain
endopeptidase
cysteine endopeptidase
cytokine binding
kinase binding
peptidase
protein binding
Death Domain Superfamily of protein-protein interaction domains
identical protein binding
Pathways
Biological processes and signaling networks where the Casp1 gene in mouse 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.
Cytoplasm
Extracellular Space
cytosol
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