|Family type peptidase||S72.001 - dystroglycan (Homo sapiens), MEROPS Accession MER0054741 (peptidase unit: 603-712)|
|Content of family||Peptidase family S72 contains autolytic serine-type endopeptidases.|
Identifier created: MEROPS 8.2 (4 August 2008)|
Dystroglycan is a component of the dystrophin-associated protein complex which may link the extracellular matrix to the cytoskeleton. Dystroglycan is a type I membrane protein which is synthesized as a precursor that is proteolytically processed into an alpha and a beta chain which remain non-covalently attached (Jayasinha et al., 2003). Cleavage occurs within a SEA domain, and is assumed to be autolytic because self-processing is known to occur in other proteins with SEA domains, such as mucin 1 (S71.001) (Akhavan et al., 2008).
|Active site residues||S654 |
|Active site||The N-terminal residue of the beta chain, Ser654, is assumed to be the only active site residue.|
|Activities and specificities||Cleavage occurs at Gly653Ser within the endoplasmic reticulum (Akhavan et al., 2008).|
|Molecular structure||No tertiary structure has been solved for any member of the family. The dystroglycan precursor is assumed to be an N-terminal nucleophile hydrolase and family S72 may be a member of clan PB.|