Substrates for peptidase M04.025: protealysin

Summary Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates

Peptide and protein substrates that are thought to be physiologically relevant are indicated by P. Peptide and protein substrates that are thought to be pathologically relevant are indicated by D. Peptide and protein substrates that are not physiologically relevant are indicated by N. Synthetic substrates are indicated by S. Click on the symbol to show only physiological, non-physiological or synthetic substrates, or here to display all substrates. 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 protein substrate, click on the UniProt Accession.

Substrate	Uniprot	Residue range	Cleavage Site	Cleavage type	Evidence	P4	P3	P2	P1	P1'	P2'	P3'	P4'	Reference
actin, aortic smooth muscle	P68135	3-377	peptide-Gly65+Ile-peptide	P	NT	Ser	Lys	Arg	Gly	Ile	Leu	Thr	Leu	Tsaplina et al., 2009
actin, aortic smooth muscle	P68135	3-377	peptide-Thr68+Leu-peptide	P	NT	Gly	Ile	Leu	Thr	Leu	Lys	Tyr	Pro	Tsaplina et al., 2009
actin, aortic smooth muscle	P68135	3-377	peptide-Gly44+Val-peptide	P	NT	Arg	His	Gln	Gly	Val	Met	Val	Gly	Tsaplina et al., 2009
furylacryloyl-Gly-Leu-NH2 (FAGLA)			furylacryloyl-Gly+Leu-NH2	S		-	-	FA	Gly	Leu	NH2	-	-	Demidyuk et al., 2006
melittin	P01501	44-69	peptide-Ala58+Leu-peptide	N		Gly	Leu	Pro	Ala	Leu	Ile	Ser	Trp	Kazanina et al., 1995
melittin	P01501	44-69	peptide-Leu59+Ile-peptide	N		Leu	Pro	Ala	Leu	Ile	Ser	Trp	Ile	Kazanina et al., 1995
metalloproteinase	Q5MJ80	1-341	peptide-Ser8+Val-peptide	P	NT	Thr	Ala	Arg	Ser	Val	Ile	Pro	Pro	Gromova et al., 2009
metalloproteinase	Q5MJ80	9-341	peptide-Ser39+Leu-peptide	P	NT	His	Val	Gln	Ser	Leu	Leu	Gly	Asn	Gromova et al., 2009
metalloproteinase	Q5MJ80	9-341	peptide-Gly50+Ala-peptide	P	NT	Arg	Ala	Pro	Gly	Ala	Lys	Thr	Ser	Gromova et al., 2009