Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence P00748

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Peptide and protein substrates that are thought to be physiologically relevant are indicated by P. Peptide and protein substrates that are not physiologically relevant are indicated by N. How cleavage sites have been identified are indicated by the following evidence codes: NT = N-terminal sequencing, MS = mass spectroscopy, MU = mutation, CS = consensus sequence, LC = liquid chromatography. To see all annotated cleavages for a peptidase, click on the peptidase name.

Cleavage Site	Peptidase	Residue range	Cleavage type	Description	Evidence	Reference
19	unknown peptidase	1-615	P	release of a signal peptide	NT	McMullen & Fujikawa, 1985
28	matrix metallopeptidase-12	20-615	P	normal turnover		Hiller et al., 2000
28	matrix metallopeptidase-13	20-615	P	normal turnover		Hiller et al., 2000
30	matrix metallopeptidase-12	20-615	P	normal turnover		Hiller et al., 2000
93	matrix metallopeptidase-13	20-615	P	normal turnover		Hiller et al., 2000
350	matrix metallopeptidase-12	20-615	P	normal turnover		Hiller et al., 2000
350	membrane-type matrix metallopeptidase-1	20-615	P			Hiller et al., 2000
353	plasma kallikrein	20-615	P			Cool et al., 1985
362	kallikrein 1	20-615	P			<%Cool et al., 1985[]%>
362	plasma kallikrein	20-615	P			Cool et al., 1985
372	vibriolysin	20-615	N		NT	Miyoshi et al., 2004
372	coagulation factor XIIa	20-615	P			Ratnoff, 2004
372	plasma kallikrein	20-615	P			Cool et al., 1985
372	hepsin	20-615	P			Herter et al., 2005
376	vibriolysin	20-615	N		NT	Miyoshi et al., 2004
376	matrix metallopeptidase-12	20-615	P	normal turnover		Hiller et al., 2000
376	matrix metallopeptidase-13	20-615	P	normal turnover		Leeman et al., 2002
376	membrane-type matrix metallopeptidase-1	20-615	P			Hiller et al., 2000
379	matrix metallopeptidase-12	20-615	P	normal turnover		Hiller et al., 2000