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Enables kininogen binding activity; peptidase activity; and peptide binding activity. Involved in several processes, including autophagic cell death; decidualization; and response to odorant. Located in several cellular components, including external side of plasma membrane; microvillus; and perikaryon. Used to study hepatocellular carcinoma. Biomarker of several diseases, including brain ischemia; hyperthyroidism; muscular atrophy; otitis media; and pancreatitis. Human ortholog(s) of this gene implicated in hypertrophic cardiomyopathy. Orthologous to several human genes including CTSV (cathepsin V). [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 Ctsl often fold into stable, three-dimensional structures and are associated with specific biological functions, such as binding to DNA, other proteins, or small molecules.
peptide binding
histone binding
Cathepsin propeptide inhibitor domain (I29)
Peptidase_C1
enzyme
protein binding
fibronectin binding
endopeptidase
cysteine-type peptidase
cysteine endopeptidase
binding protein
aminopeptidase
collagen binding
cysteine-type carboxypeptidase
Top Findings
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
intracellular membrane-bounded organelle
Extracellular Space
apical compartment
Nucleus
Plasma Membrane
lysosome
Golgi Apparatus
plasma membrane extracellular face
nucleoli
perinuclear vesicles
cytoplasmic vesicles
multivesicular bodies
secretory granules
microvilli
perikaryon
chromaffin vesicles
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