Seroatlas · Protein domains

Peptidase S1A, chymotrypsin family

IPR001314

Definition

This group of serine peptidases and non-peptidase homologues belong to the MEROPS peptidase family S1, subfamily S1A (chymotrypsin subfamily, clan PA(S)). These peptidases contain the catalytic triad histidine, aspartate and serine found in all members of subfamily S1A. Testes-specific protein TSP50 is also included in this family which has the serine replaced by threonine, although the serine is conserved in many vertebrates PMID:17283160. The type example being chymotrypsin A from Bos taurus (Bovine). Members of the chymotrypsin family may occasionally function intracellularly (for example, the intracellular digestion of bacteria in neutrophils), but most function extracellularly, for example in roles such as food digestion, fibrinolysis and complement activation PMID:7845208. The essential catalytic unit of the chymotrypsin family is around 220 amino acids in length, although the protein may be extended at the N terminus with unrelated sequences, often containing modules. They are rarely extended at the C terminus: exceptions include acrosin, complement component C2, and coagulation factor X, which has a 16 residue extension that is removed upon activation PMID:7845208.

112 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.

Download CSV (112 proteins: gene, accession, name)

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