Searches of the MEROPS database

Display Known Cleavages for a Protein

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Accession:

Sequence P01270

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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
25	unknown peptidase	1-115	P	release of a signal peptide	NT	Zhang & Henzel, 2004
31	kallikrein-related peptidase 4	1-115	P		CS	Matsumura et al., 2005
31	furin	26-115	P			Hendy et al., 1995
31	PCSK2 peptidase	26-35	N		CS	Remacle et al., 2008
31	PCSK4 peptidase	26-35	N		CS	Remacle et al., 2008
31	PCSK6 peptidase	26-35	N		CS	Remacle et al., 2008
31	PCSK5 peptidase	26-35	N		CS	Remacle et al., 2008
31	PCSK7 peptidase	26-115	P			Seidah & Chretien, 2004
46	meprin alpha subunit	32-115	N			Bylander et al., 2007
47	meprin alpha subunit	32-115	N			Bylander et al., 2007
48	meprin alpha subunit	32-115	N			Bylander et al., 2007
54	meprin alpha subunit	32-115	N			Bylander et al., 2007
56	yapsin-1	32-115	N			Sohn et al., 2012
56	GPI-anchored aspartic peptidase (Saccharomyces-type)	32-115	N			Sohn et al., 2012
56	omptin	32-115	N			McCarter et al., 2004
57	omptin	32-115	N			McCarter et al., 2004
57	meprin alpha subunit	32-115	N			Bylander et al., 2007
60	meprin alpha subunit	32-115	N			Bylander et al., 2007
61	meprin alpha subunit	32-115	N			Bylander et al., 2007
64	meprin alpha subunit	32-115	N			Bylander et al., 2007