CTSC
Function
Thiol protease (PubMed:1586157). Has dipeptidylpeptidase activity (PubMed:1586157). Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids (PubMed:1586157). Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate (PubMed:1586157). Can act as both an exopeptidase and endopeptidase (PubMed:1586157). Activates serine proteases such as elastase, cathepsin G and granzymes A and B (PubMed:8428921).
Involvement in disease
Papillon-Lefevre syndrome
PLS
An autosomal recessive disorder characterized by palmoplantar keratosis and severe periodontitis affecting deciduous and permanent dentitions and resulting in premature tooth loss. The palmoplantar keratotic phenotype vary from mild psoriasiform scaly skin to overt hyperkeratosis. Keratosis also affects other sites such as elbows and knees.
None
The disease is caused by variants affecting the gene represented in this entry.
Haim-Munk syndrome
HMS
An autosomal recessive disorder characterized by palmoplantar keratosis, onychogryphosis and periodontitis. Additional features are pes planus, arachnodactyly, and acroosteolysis.
None
The disease is caused by variants affecting the gene represented in this entry.
Periodontititis, aggressive, 1
AP1
A disease characterized by severe and protracted gingival infections, generalized or localized, leading to tooth loss. Amounts of microbial deposits are generally inconsistent with the severity of periodontal tissue destruction and the progression of attachment and bone loss may be self arresting.
None
The disease is caused by variants affecting the gene represented in this entry.
Post-translational modifications
N-glycosylated. While glycosylation at Asn-53, Asn-119 and Asn-276 is mediated by STT3A-containing complexes, glycosylation at Asn-29 is mediated STT3B-containing complexes.
In approximately 50% of the complexes the exclusion domain is cleaved at position 58 or 61. The two parts of the exclusion domain are held together by a disulfide bond.
Sequence Similarities
Belongs to the peptidase C1 family.
Tissue Specificity
Ubiquitous. Highly expressed in lung, kidney and placenta. Detected at intermediate levels in colon, small intestine, spleen and pancreas.
Cellular localization
- Lysosome
Alternative names
CPPI, CTSC, Dipeptidyl peptidase 1, Cathepsin C, Cathepsin J, Dipeptidyl peptidase I, Dipeptidyl transferase, DPP-I, DPPI