Papain-like cysteine endopeptidase
IPR039417
Definition
This entry represents homologues of papain, from peptidase family C1 subfamily A, including the mammalian CPs (cathepsins F, H, L, K, O, S, V, X and W) PMID:11517925. Cathepsins B and C, which differ in their activation peptides, are not included here PMID:11440158. Papain is an endopeptidase with specific substrate preferences, primarily for bulky hydrophobic or aromatic residues at the S2 subsite, a hydrophobic pocket in papain that accommodates the P2 sidechain of the substrate (the second residue away from the scissile bond). Most members of the papain subfamily are endopeptidases. Some exceptions to this rule can be explained by specific details of the catalytic domains like the occluding loop in cathepsin B which confers an additional peptidyl-dipeptidase activity and the mini-chain of cathepsin H resulting in an N-terminal exopeptidase activity PMID:10350606.
8 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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