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  Domain Name: Peptidase_C1A_Cathep
Cathepsin X; the only papain-like lysosomal cysteine peptidase exhibiting carboxymonopeptidase activity. It can also act as a carboxydipeptidase, like cathepsin B, but has been shown to preferentially cleave substrates through a monopeptidyl carboxypeptidase pathway. The propeptide region of cathepsin X, the shortest among papain-like peptidases, is covalently attached to the active site cysteine in the inactive form of the enzyme. Little is known about the biological function of cathepsin X. Some studies point to a role in early tumorigenesis. A more recent study indicates that cathepsin X expression is restricted to immune cells suggesting a role in phagocytosis and the regulation of the immune response.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 18
Total Disease Mutations Found: 15
This domain occurred 11 times on human genes (27 proteins).



  CEROID LIPOFUSCINOSIS, NEURONAL, 13
  HAIM-MUNK SYNDROME
  PAPILLON-LEFEVRE SYNDROME
  PERIODONTITIS, AGGRESSIVE, 1
  PYCNODYSOSTOSIS


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Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
active site
active site mini-loop
S2 subsite















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Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

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