Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(DY-681)-Gly-Arg-Gln-Ser-Arg-Ala-Ile-Lys (DY-681)-NH + H2O
?
-
synthetic substrate, peptide sequence is derived from one of the preferred matriptase cleavage sequences, P4(Arg/Lys)-P3(Xxx)-P2(Ser)-P1(Arg)-P10(Ala), where Xxx is a nonbasic amino acid
-
-
?
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Ala-Tyr(3-NO2)-NH2 + H2O
ABZ-Ile-Arg-Ala-Arg + Ser-Ala-Ala-Tyr(3-NO2)-NH2
-
-
-
?
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Gly-Tyr(3-NO2)-NH2 + H2O
ABZ-Ile-Arg-Ala-Arg + Ser-Ala-Gly-Tyr(3-NO2)-NH2
-
-
-
?
ABZ-Ile-Arg-Ala-Arg-Ser-Ala-Ser-Tyr(3-NO2)-NH2 + H2O
ABZ-Ile-Arg-Ala-Arg + Ser-Ala-Ser-Tyr(3-NO2)-NH2
-
-
-
?
acetyl-L-lysyl-L-threonyl-L-lysyl-L-glutaminyl-L-leucyl-L-arginine-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
acetyl-Lys-Thr-Lys-Gln-Leu-Arg-4-methyl-coumaryl-7-amide + H2O
acetyl-Lys-Thr-Lys-Gln-Leu-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-Lys-Thr-Lys-Gln-Leu-Arg-4-methylcoumarin-7-amide + H2O
?
-
substrate almost matches the P5 to P1 residues of matriptase zymogen: P5(Thr)-P4(Lys)-P3(Gln)-P2(Ala)-P1(Arg). The hydrolysis of the substrate is expected to mimic the situation of activation cleavage of matriptase zymogen
-
-
?
acetyl-Lys-Thr-Lys-Gln-Leu-Arg-methyl-coumaryl-7-amide + H2O
acetyl-Lys-Thr-Lys-Gln-Leu-Arg + 7-amino-4-methylcoumarin
-
relative activity: 19% using engineered L-matriptase (secreted variant of matriptase activated by recombinant enterokinase), relative activity: 16% using engineered pseudozymogen His6t-S-CD (consisting of a spacer and the catalytical domain with an N-terminal His6-tag and a cleavage site for activation by enterokinase)
-
-
?
acid-sensing ion channel 1 + H2O
?
-
the matriptase recognition sites Arg-145, Lys-185, and Lys-384 are identified in the specific substrate acid-sensing ion channel 1
-
-
?
alphaEbeta7 integrin + H2O
?
-
-
-
-
?
alphaEbeta7integrin + H2O
?
-
-
-
?
amyloid precursor protein + H2O
?
-
-
-
-
?
Arg-Xaa-Ser-Arg-Ala + H2O
Arg-Xaa-Ser + Arg-Ala
-
X: non-basic amino acid, good substrate
-
?
benzoyl-L-arginine-4-methylcoumaryl-7-amide + H2O
benzoyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
?
benzyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-Gln-Ala-Arg-4-nitroanilide + H2O
Boc-Gln-Ala-Arg + 4-nitroaniline
-
-
-
?
Boc-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
Boc-Gln-Ala-Arg + 7-amino-4-methylcoumarin
fluorogenic substrate
-
-
?
Boc-Glu-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
Boc-Glu-Ala-Arg-7-amido-4-methylcoumarin + H2O
Boc-Glu-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
butyloxycarbonyl-L-Gln-L-Ala-L-Arg-4-nitroanilide + H2O
butyloxycarbonyl-L-Gln-L-Ala-L-Arg + 4-nitroaniline
-
-
-
-
?
CUB-domain-containing protein 1 + H2O
?
-
-
-
?
denatured collagen + H2O
?
-
-
-
-
?
dumpy + H2O
?
i.e. a zona pellucida-domain protein
-
-
?
EpCAM + H2O
?
-
i.e. epithelial cell adhesion molecule CD326
-
-
?
epidermal growth factor receptor + H2O
EGFR135 + EGFR110
fetuin-A + H2O
?
a liver-derived alpha2-Heremans-Schmid glycoprotein from plasma, processing into a two-chain form, cleavage sites are Arg and Lys residues in the 40 amino acid sequence of the linker connceting the two peptides
-
-
?
Fibrinogen + H2O
?
-
-
-
?
G-protein-coupled protease-activated receptor-2 + H2O
?
Glu-Gly-Arg-p-nitroanilide + H2O
?
-
substrate activity assay
-
-
?
growth factor macrophage-stimulating protein 1 + H2O
?
H-Glu-Gly-Arg-p-nitroanilide + H2O
H-Glu-Gly + Arg-p-nitroanilide
-
low activity
-
-
?
hemojuvelin (furin site) + H2O
?
-
-
-
?
hepatocyte growth factor + H2O
?
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
HGF/SF + H2O
?
-
i.e. hepatocyte growth factor/scatter factor, growth factor
-
-
?
Ile-Pro-Arg-p-nitroanilide + H2O
Ile-Pro + Arg-p-nitroanilide
-
-
-
?
influenza A H1 virus hemagglutinin + H2O
?
the soluble form of the protease is able to specifically cleave hemagglutinins from H1 virus, but not from H2 and H3 viruses, in a broad pH range
-
-
?
insulin growth factor binding protein-related protein-1 + H2O
?
-
cleaved by the soluble form of active matripase
-
-
?
insulin-like growth factor binding protein related protein-1
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
insulin-like growth factor binding-related protein-1 + H2O
?
Lys-Xaa-Ser-Arg-Ala + H2O
Lys-Xaa-Ser + Arg-Ala
-
X: non-basic amino acid, good substrate
-
?
matriptase + H2O
?
-
-
-
-
?
matriptase-2 + H2O
?
autocatalysis
-
-
?
matrix metalloprotease-3 + H2O
?
methyl-sulfonyl-D-cyclo-hexyltyrosyl-glycyl-L-arginine-4-nitroanilide + H2O
?
-
-
-
?
methylsulfonyl-D-cyclohexyltyrosyl-glycyl-arginine-p-nitroanilide + H2O
methylsulfonyl-D-cyclohexyltyrosyl-glycyl-arginine + p-nitroaniline
-
-
-
-
?
methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine-p-nitroanilide + H2O
methylsulfonyl-D-cyclohexyltyrosylglycyl-arginine + p-nitroaniline
-
-
-
-
?
MSP-1 + H2O
?
-
i.e. macrophage-stimulating protein 1, a growth factor
-
-
?
N-Ala-Ala-Ala-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-succinyl-Ala-Phe-Lys-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-succinyl-Ala-Phe-Lys-7-amido-4-methylcoumarin + H2O
N-succinyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
-
-
?
N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-tert-butoxy-carbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin
N-tert-butoxy-carbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-benzyl-Asp-Pro-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-benzyl-Asp-Pro-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-benzyl-Glu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-benzyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-gamma-benzyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg 7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
N-tert-butoxycarbonyl-Gly-Lys-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gly-Lys-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Leu-Arg-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
N-tert-butoxycarbonyl-Leu-Ser-Thr-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Ser-Thr-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Val-Pro-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
-
?
N2-t-butyloxycarbonyl-QNR-7-amido-4-methylcoumarin + H2O
?
matriptase-2 mediates efficient cleavage of artificial peptides corresponding to cleavage sites located in the proteins filaggrin, CUB-domain-containing protein 1 (CDCP1), and alphaE beta7 integrin
-
-
?
plasminogen + H2O
?
-
-
?
pro matrix metalloproteinase 1 + H2O
?
-
matriptase activates pro-matrix metalloproteinase-1 and processes pro-matrix metalloproteinase-3 to its fully active form
-
-
?
pro matrix metalloproteinase 3 + H2O
?
-
matriptase activates pro-matrix metalloproteinase-1 and processes pro-matrix metalloproteinase-3 to its fully active form
-
-
?
pro-form GPI-anchored serine protease prostasin + H2O
mature GPI-anchored serine protease prostasin + ?
pro-form influenza hemagglutinin H1 + H2O
mature influenza hemagglutinin H1 + ?
pro-form influenza hemagglutinin H2 + H2O
mature influenza hemagglutinin H2 + ?
subtype H2N2
-
-
?
pro-form influenza hemagglutinin H3 + H2O
mature influenza hemagglutinin H3 + ?
subtype H3N2
-
-
?
pro-form matriptase + H2O
mature matriptase + ?
autocatalytic activation
-
-
?
pro-hepatocyte growth factor + H2O
?
pro-hepatocyte growth factor/scatter factor + H2O
?
pro-HGF + H2O
?
-
matriptase is an efficient activator of hepatocyte growth factor
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
pro-urokinase plasminogen activator + H2O
?
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
pro-urokinase-type plasminogen activator + H2O
?
profilaggrin + H2O
?
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
proform acid-sensing ion channel 1 + H2O
mature acid-sensing ion channel 1 + ?
-
-
-
-
?
proform epithelial sodium channel + H2O
mature epithelial sodium channel + ?
-
-
-
-
?
proform G protein-coupled protease activated receptor-2 + H2O
mature G protein-coupled protease activated receptor-2 + ?
-
-
-
-
?
proform G-protein-coupled protease activated receptor-2 + H2O
mature G-protein-coupled protease activated receptor-2 + ?
-
-
-
-
?
proform hepatocyte growth factor + H2O
mature hepatocyte growth factor + ?
-
-
-
-
?
proform matriptase + H2O
mature matriptase
matriptase is expressed as a zymogen and is autocatalytically processed and activated through cleavage at Arg614 within the RQAR614-VVGG activation sequence
-
-
?
proform matriptase-2 + H2O
mature matriptase
matriptase-2 is expressed as zymogen form and undergoes autocatalysis at Arg576 within the PSSR576-IVGG sequence located in the consensus activation site of its pro-domain
-
-
?
proform platelet-derived growth factor-D + H2O
mature platelet-derived growth factor-D + ?
-
-
-
-
?
proform prostasin + H2O
mature prostasin + ?
proform urokinase-type plasminogen activator + H2O
mature urokinase-type plasminogen activator + ?
-
-
-
-
?
prostasin + H2O
activated prostasin + ?
protease activated receptor 2 + H2O
?
-
-
-
-
?
protease-activated receptor-2
?
protease-activated receptor-2 + H2O
?
-
-
-
-
?
proteinase-activated receptor 2 + H2O
?
-
-
-
-
?
RAARVVGG + H2O
RAAR + VVGG
-
-
-
-
?
RLARVVGG + H2O
RLAR + VVGG
-
-
-
-
?
RQARAVGG + H2O
RQAR + AVGG
-
-
-
-
?
RQARQVGG + H2O
RQAR + QVGG
-
-
-
-
?
RQARVVGG + H2O
RQAR + VVGG
-
-
-
-
?
RQARYVGG + H2O
RQAR + YVGG
-
-
-
-
?
RQLRVVGG + H2O
RQLR + VVGG
-
-
-
-
?
RQRRVVGG + H2O
RQRR + VVGG
-
-
-
-
?
RQYRVVGG + H2O
RQYR + VVGG
-
-
-
-
?
RRARVVGG + H2O
RRAR + VVGG
-
-
-
-
?
RYARVVGG + H2O
RYAR + VVGG
-
-
-
-
?
serine protease uPA + H2O
?
single-chain urokinase-type plaminogen activator + H2O
?
-
is activated by matriptase
-
?
single-chain urokinase-type plasminogen activator + H2O
?
-
sc-uPA
-
-
?
stromelysin + H2O
?
-
MMP-3
-
-
?
stromelysin + H2O
activated stromelysin + propeptide of stromelysin
Suc-Ala-Ala-Pro-Arg-p-nitroanilide + H2O
Suc-Ala-Ala-Pro + Arg-p-nitroanilide
-
low activity
-
-
?
Suc-Ala-Ala-Pro-Lys-p-nitroanilide + H2O
Suc-Ala-Ala-Pro-Lys + p-nitroaniline
-
-
-
-
?
succinyl-Ala-Phe-Lys-7-amido-4-methylcoumarin + H2O
succinyl-Ala-Phe-Lys + 7-amino-4-methylcoumarin
-
-
?
t-butoxycarbonyl-L-Gln-L-Ala-L-Arg-7-amido-4-methylcoumarin + H2O
t-butoxycarbonyl-L-Gln-L-Ala-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-Asp-Pro-Arg-methyl-coumaryl-7-amide + H2O
t-butyloxycarbonyl-Asp-Pro-Arg + 7-amino-4-methylcoumarin
-
relative activity: 66% using engineered L-matriptase (secreted variant of matriptase activated by recombinant enterokinase), relative activity: 69% using engineered pseudozymogen His6t-S-CD (consisting of a spacer and the catalytical domain with an N-terminal His6-tag and a cleavage site for activation by enterokinase)
-
-
?
t-butyloxycarbonyl-Gln-Ala-Arg-4-methyl-coumaryl-7-amide + H2O
t-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
t-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
enzymatic activity assay
-
-
?
t-butyloxycarbonyl-Gln-Ala-Arg-methyl-coumaryl-7-amide + H2O
t-butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
relative activity: 100%, using engineered L-matriptase (secreted variant of matriptase activated by recombinant enterokinase) or engineered pseudozymogen His6t-S-CD (consisting of a spacer and the catalytical domain with an N-terminal His6-tag and a cleavage site for activation by enterokinase)
-
-
?
t-butyloxycarbonyl-Glu-Gly-Arg-methyl-coumaryl-7-amide + H2O
t-butyloxycarbonyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
relative activity: 29% using engineered L-matriptase (secreted variant of matriptase activated by recombinant enterokinase), relative activity: 31% using engineered pseudozymogen His6t-S-CD (consisting of a spacer and the catalytical domain with an N-terminal His6-tag and a cleavage site for activation by enterokinase)
-
-
?
t-butyloxycarbonyl-L-Gln-L-Ala-L-Arg-4-methyl-coumaryl-7-amide + H2O
t-butyloxycarbonyl-L-Gln-L-Ala-L-Arg + 7-amino-4-methylcoumarin
-
activity assay
-
-
?
t-butyloxycarbonyl-L-glutamyl-L-alanyl-L-arginine-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Leu-Gly-Arg-methyl-coumaryl-7-amide + H2O
t-butyloxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
-
relative activity: 28% using engineered L-matriptase (secreted variant of matriptase activated by recombinant enterokinase), relative activity: 28% using engineered pseudozymogen His6t-S-CD (consisting of a spacer and the catalytical domain with an N-terminal His6-tag and a cleavage site for activation by enterokinase)
-
-
?
t-butyloxycarbonyl-Phe-Ser-Arg-methyl-coumaryl-7-amide + H2O
t-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
relative activity: 12% using engineered L-matriptase (secreted variant of matriptase activated by recombinant enterokinase), relative activity: 13% using engineered pseudozymogen His6t-S-CD (consisting of a spacer and the catalytical domain with an N-terminal His6-tag and a cleavage site for activation by enterokinase)
-
-
?
t-butyloxycarbonyl-[(2S)-2-amino-3-(benzyloxycarbonyl)propionyl]-L-prolyl-L-arginine-4-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-[(2S)-2-amino-3-(benzyloxycarbonyl)propionyl]-Pro-Arg-4-methyl-coumaryl-7-amide + H2O
t-butyloxycarbonyl-[(2S)-2-amino-3-(benzyloxycarbonyl)propionyl]-Pro-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
TMPRSS6 + H2O
?
autocleavage site: PSSR/IVGG
-
-
?
tracheal-prostasin zymogen + H2O
?
-
-
-
?
Type I collagen + H2O
?
-
-
-
?
urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
VPEKQTRGL + H2O
?
influenza hemagglutinin H3 cleavage site peptide mimic
-
-
?
Xaa-Arg-Ser-Arg-Ala + H2O
Xaa-Arg-Ser + Arg-Ala
-
X: non-basic amino acid, good substrate
-
?
Xaa-Lys-Ser-Arg-Ala + H2O
Xaa-Lys-Ser + Arg-Ala
-
X: non-basic amino acid, good substrate
-
?
Z-Phe-Val-Arg-p-nitroanilide + H2O
Z-Phe-Val + Arg-p-nitroanilide
-
-
-
-
?
additional information
?
-
Boc-QAR-Amc + H2O
?
-
-
-
?
Boc-QAR-Amc + H2O
?
matriptase-2 mediates efficient cleavage of artificial peptides corresponding to cleavage sites located in the proteins filaggrin, CUB-domain-containing protein 1 (CDCP1), and alphaE beta7 integrin
-
-
?
CDCP1 + H2O
?
-
-
-
-
?
collagen type IV + H2O
?
-
-
-
-
?
collagen type IV + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
collagen type IV + H2O
?
-
-
-
-
?
collagen type IV + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
epidermal growth factor receptor + H2O
EGFR135 + EGFR110
-
-
fragments of 135 and 110 kDa, EGFR110 is constitutively active, while EGFR135 is inactive in terms of tyrosine phosphorylation
-
?
epidermal growth factor receptor + H2O
EGFR135 + EGFR110
-
the epidermal growth factor receptor, EGFR is proteolytically cleaved in the N-terminal extracellular domain by the matriptase-prostasin serine protease cascade in cultured epithelial cells
fragments of 135 and 110 kDa, no longer responsive to EGF stimulation
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
filaggrin + H2O
?
-
-
-
-
?
filaggrin + H2O
?
-
-
-
?
G-protein-coupled protease-activated receptor-2 + H2O
?
-
-
-
-
?
G-protein-coupled protease-activated receptor-2 + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
Gelatin + H2O
?
-
-
-
-
?
Gelatin + H2O
?
-
involved in ECM degradation/remodeling
-
-
?
growth factor macrophage-stimulating protein 1 + H2O
?
-
-
-
-
?
growth factor macrophage-stimulating protein 1 + H2O
?
-
-
-
-
?
hemojuvelin + H2O
?
-
-
-
-
?
hemojuvelin + H2O
?
-
-
-
?
hemojuvelin + H2O
?
inactivation
-
-
?
hemojuvelin + H2O
?
a glycosylphosphatidylinositol-linked membrane protein. inactivation
-
-
?
hemojuvelin + H2O
?
bone morphogenetic protein co-receptor
-
-
?
hemojuvelin + H2O
?
-
-
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
-
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
proteolytic activation of hepatocyte growth factor/scatter factor, physiological function, overview
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
-
-
-
?
hepatocyte growth factor + H2O
activated hepatocyte growth factor + ?
-
proteolytic activation of hepatocyte growth factor/scatter factor, overview
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
-
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
activation
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
seven proteases are involved in the activation of HGF/SF, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness, overview
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
the enzyme is involved in tumor progression and metastasis
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
-
-
-
?
hepatocyte growth factor/scatter factor + H2O
activated hepatocyte growth factor/scatter factor + ?
-
seven proteases are involved in the activation of HGF/SF, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness, overview
-
-
?
IGFBP-rP1 + H2O
?
-
-
-
-
?
IGFBP-rP1 + H2O
?
-
an adhesion factor
-
-
?
IGFBP-rP1 + H2O
?
-
involved in involved in cell proliferation and adhesion
-
-
?
IGFBP-rP1 + H2O
?
-
-
-
-
?
IGFBP-rP1 + H2O
?
-
involved in involved in cell proliferation and adhesion
-
-
?
insulin-like growth factor binding protein related protein-1
?
-
IGFBP-rP1
-
-
?
insulin-like growth factor binding protein related protein-1
?
IGFBP-rP1
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
activation
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
proteolytical cleavage on the cell surface of a a single-chain IGFB-rP1 to a two-chain form, consisting of a 25 kDa chain and an 8 kDa chain, changing its biological in modulation of cellular adhesion and growth in an IGF/insulin-dependent or independent manner, as well as tumor-suppressive activity, the soluble form of active matriptase cleaves IGFBP-rP1 but HAI-1 or some other inhibitors block its activity in culture medium, overview
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
i.e. IGFBP-rP1
-
-
?
insulin-like growth factor binding protein-related protein-1 + H2O
?
-
i.e. IGFBP-rP1 or angiomodulin or mac25
-
-
?
insulin-like growth factor binding-related protein-1 + H2O
?
-
-
-
-
?
insulin-like growth factor binding-related protein-1 + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
Laminin + H2O
?
-
-
-
-
?
Laminin + H2O
?
-
involved in adhesion and migration/invasiveness
-
-
?
matrix metalloprotease-3 + H2O
?
-
-
-
-
?
matrix metalloprotease-3 + H2O
?
-
activation
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
?
N-tert-butoxycarbonyl-Leu-Gly-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Leu-Gly-Arg + 7-amino-4-methylcoumarin
-
-
?
PAR-2 + H2O
?
-
-
-
-
?
PAR-2 + H2O
?
-
G-protein coupled receptor
-
-
?
PAR-2 + H2O
?
-
involved in involved in cell adhesion
-
-
?
PAR-2 + H2O
?
-
G-protein coupled receptor
-
-
?
PAR-2 + H2O
?
-
involved in involved in cell adhesion
-
-
?
pro-form GPI-anchored serine protease prostasin + H2O
mature GPI-anchored serine protease prostasin + ?
activation
-
-
?
pro-form GPI-anchored serine protease prostasin + H2O
mature GPI-anchored serine protease prostasin + ?
activation, prostasin is also a regulator of the epidermal sodium channel like matriptase
-
-
?
pro-form influenza hemagglutinin H1 + H2O
mature influenza hemagglutinin H1 + ?
-
-
-
?
pro-form influenza hemagglutinin H1 + H2O
mature influenza hemagglutinin H1 + ?
preferred subtype H1N1
-
-
?
pro-hepatocyte growth factor + H2O
?
-
-
-
-
?
pro-hepatocyte growth factor + H2O
?
-
-
-
-
?
pro-hepatocyte growth factor + H2O
?
-
-
-
-
?
pro-hepatocyte growth factor/scatter factor + H2O
?
-
pro-HGF/SF
-
-
?
pro-hepatocyte growth factor/scatter factor + H2O
?
pro-HGF/SF
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
-
soluble matriptase efficiently converts soluble prostasin zymogen to an active two-chain form, prostasin is exclusively found in the zymogen form in matriptase-deficient epidermis
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
-
the channel activating protease prostasin/CAP1/PRSS8, a glycosylphosphatidylinositol-anchored membrane serine protease, is co-localized with matriptase
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
-
activation, cleavage after Arg12 within the amino acid sequence QPR12-ITG
-
-
?
pro-prostasin + H2O
prostasin + propeptide of prostasin
-
cleavage after Arg12 within the amino acid sequence QPR12-ITG
-
-
?
pro-uPA + H2O
?
-
-
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
-
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
activation
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
activation at the cell surface, where uPA and matriptase co-localize, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
the enzyme is involved in tumor progression and metastasis
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
-
-
-
?
pro-urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
activation at the cell surface, where uPA and matriptase co-localize, involved in cell proliferation and adhesion, ECM degradation/remodeling, and migration/invasiveness
-
-
?
pro-urokinase-type plasminogen activator + H2O
?
-
-
-
-
?
pro-urokinase-type plasminogen activator + H2O
?
-
-
-
-
?
pro-urokinase-type plasminogen activator + H2O
?
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
involved in terminal epithelial cell differentiation, mechanism of enzyme access for direct cleavage in vivo, overview
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
-
-
-
?
profilaggrin + H2O
filaggrin + propeptide of filaggrin
-
involved in terminal epithelial cell differentiation, mechanism of enzyme access for direct cleavage in vivo, overview
-
-
?
proform prostasin + H2O
mature prostasin + ?
-
-
-
-
?
proform prostasin + H2O
mature prostasin + ?
-
-
-
-
?
prostasin + H2O
?
-
-
-
-
?
prostasin + H2O
?
-
-
-
?
prostasin + H2O
?
-
a serine protease
-
-
?
prostasin + H2O
?
-
-
-
-
?
prostasin + H2O
?
-
a serine protease
-
-
?
prostasin + H2O
?
-
-
-
-
?
prostasin + H2O
activated prostasin + ?
-
proteolytic activation by matriptase, when expressed without matriptase, prostasin remains in the zymogen form and no prostasin-PN-1 complex is formed, overview
-
-
?
prostasin + H2O
activated prostasin + ?
-
proteolytic activation by matriptase
-
-
?
prostatin + H2O
?
-
-
-
-
?
prostatin + H2O
?
-
-
-
-
?
prostatin + H2O
?
-
-
-
-
?
protease-activated receptor-2
?
-
PAR2
-
-
?
protease-activated receptor-2
?
PAR2
-
-
?
serine protease uPA + H2O
?
-
-
-
-
?
serine protease uPA + H2O
?
-
-
-
-
?
SIMA135 + H2O
?
-
-
-
-
?
SIMA135 + H2O
?
-
-
-
-
?
stromelysin + H2O
activated stromelysin + propeptide of stromelysin
-
activation
-
-
?
stromelysin + H2O
activated stromelysin + propeptide of stromelysin
-
i.e. MMP-3 or matrix metalloproteinase-3, recombinant human substrate, activation
-
-
?
trask + H2O
?
-
-
-
-
?
trask + H2O
?
-
a transmembrane glycoprotein
-
-
?
trask + H2O
?
-
i.e. CDCP1 or SIMA 135, a transmembrane glycoprotein
-
-
?
urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
pro-uPA activation on THP-1 cells
-
-
?
urokinase plasminogen activator + H2O
urokinase plasminogen activator + propeptide of urokinase plasminogen activator
-
pro-uPA activation
-
-
?
VEGFR-2 + H2O
?
-
-
-
-
?
VEGFR-2 + H2O
?
-
i.e. vascular endothelial growth factor receptor 2, a growth factor receptor
-
-
?
VEGFR-2 + H2O
?
-
-
-
-
?
VEGFR-2 + H2O
?
-
i.e. vascular endothelial growth factor receptor 2, a growth factor receptor
-
-
?
additional information
?
-
-
enzyme inactivation by HAI-1 is required for epithelial integrity of the zebrafish epidermis, Hai1 and matriptase1a are involved in regualtion of skin homeostasis and remodeling, overview
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
cleaves synthetic substrates with arginine or lysine as their P1 sites and prefers small side chain amino acids, such as Ala and Gly, at P2 sites
-
?
additional information
?
-
-
cleaves synthetic substrates with arginine or lysine as their P1 sites and prefers small side chain amino acids, such as Ala and Gly, at P2 sites
-
?
additional information
?
-
-
preferred amino acid residues: at P4 position: Lys and Arg, at P3 position: basic residues and Glu, at P2 position: Gly, Ser and Phe
-
?
additional information
?
-
-
degrades extracellular matrix
-
?
additional information
?
-
-
degrades extracellular matrix
-
?
additional information
?
-
-
degrades extracellular matrix
-
?
additional information
?
-
degrades extracellular matrix
-
?
additional information
?
-
-
degrades extracellular matrix
-
?
additional information
?
-
degrades extracellular matrix
-
?
additional information
?
-
degrades extracellular matrix, matriptase-binding protein is a Kunitz-type serine protease inhibitor
-
?
additional information
?
-
-
degrades extracellular matrix, matriptase-binding protein is a Kunitz-type serine protease inhibitor
-
?
additional information
?
-
initiator of matrix-degrading protein cascade, activates hepatocyte growth factor scattering factor
-
?
additional information
?
-
-
initiator of matrix-degrading protein cascade, activates hepatocyte growth factor scattering factor
-
?
additional information
?
-
-
involved in multiple aspects of tumor progression and cancer invasion
-
?
additional information
?
-
-
enzyme regulation and deregulation in cancer, overview, matriptase is involved in cancer initiation and progression, it not only facilitates cellular invasiveness but may also activate oncogenic pathways, overview
-
-
?
additional information
?
-
-
matriptase blockade could potentially modulate tumorigenesis and metastasis in vivo
-
-
?
additional information
?
-
-
matriptase cleaves and activates proteins implicated in the progression of cancer
-
-
?
additional information
?
-
-
matriptase expression is correlated with tumor progression in epithelium-derived cancer cells
-
-
?
additional information
?
-
-
matriptase has an essential physiological role in profilaggrin processing, corneocyte maturation, and lipid matrix formation associated with terminal differentiation of the oral epithelium and the epidermis, and is also critical for hair follicle growth, matriptase and HAI expression are frequently dysregulated in human cancer, and matriptase expression, that is unopposed by HAI-1, potently promotes carcinogenesis and metastatic dissemination in animal models, matriptase dramatically increases apoptosis of immature thymocytes in the thymus, leading to thymocyte depletion, physiological functions of matriptase, the enzyme is involved in epithelial carcinogenesis, detailed overview
-
-
?
additional information
?
-
-
matriptase is a type II transmembrane serine protease and highly regulated in leukocytes, and correlates with the presence of active uPA on their surface, it is up-regulated in a variety of cancers and correlates closely with disease progression, it acts as initiator of protease cascades/signaling pathways, overview
-
-
?
additional information
?
-
-
matriptase promotes tumor growth and angiogenesis by enhancing extracellular matrix degradation in tumor cell microenvironments, overview
-
-
?
additional information
?
-
-
matriptase-1 enhances breast tumor growth and invasion and correlates with poor prognosis for breast cancer patients, while matriptase-2 shows the opposite effects, overview
-
-
?
additional information
?
-
matriptase-1 enhances breast tumor growth and invasion and correlates with poor prognosis for breast cancer patients, while matriptase-2 shows the opposite effects, overview
-
-
?
additional information
?
-
-
matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients, while matriptase-1 shows the opposite effects, overview
-
-
?
additional information
?
-
matriptase-2 inhibits breast tumor growth and invasion and correlates with favorable prognosis for breast cancer patients, while matriptase-1 shows the opposite effects, overview
-
-
?
additional information
?
-
mutation in gene ST14 causes autosomal recessive ichthyosis with hypotrichosis syndrome, characterized by congenital ichthyosis associated with abnormal hair, overview
-
-
?
additional information
?
-
-
physiological functions, overview, MT-SP1 is a type II transmembrane serine protease implicated in a range of cancers including those of the breast, cervix, ovaries, prostate, colon and gastrointestinal tract, MT-SP1 plays a role in embryologic development
-
-
?
additional information
?
-
-
physiological regulatory mechanisms, overview, matriptase is involved in cancer invasion and metastasis by serving as a membrane activator directly on cancer cell surfaces to recruit and activate urokinase type plasminogen activator, MMP-3, hepatocyte growth factor, and insulin-like growth factor binding protein-related protein-1, all of which are important in various aspects of cancers, including extracellular matrix degradation, adhesion, cellular motility and tumor vascularization
-
-
?
additional information
?
-
-
reduced matriptase activity is associated with incomplete terminal differentiation of epidermis, epidermal appendages, oral epithelium, and, likely, other epithelial structures, matriptase activity must be tightly controlled in epithelial tissues by transcriptional and posttranslational mechanisms, as matriptase dysregulation can cause embryonic demise as well as malignant transformation
-
-
?
additional information
?
-
-
the G827R mutation in patients with autosomal recessive ichthyosis with hypotrichosis leads to the expression of an inactive protease
-
-
?
additional information
?
-
-
matriptase binds cytosolic proteins to regulate enzymatic activity and cellular distribution of the protease
-
-
?
additional information
?
-
-
matriptase performs autoactivation
-
-
?
additional information
?
-
-
R/KXSR-/-A is the cleavage sequence of matriptase
-
-
?
additional information
?
-
-
the enzyme is a type II transmembrane serine protease
-
-
?
additional information
?
-
-
the enzyme performs autoproteolysis
-
-
?
additional information
?
-
-
matriptase does not cleave acid-sensing ion channel 2
-
-
?
additional information
?
-
-
the P1 residue for MT-SP1 substrates is either arginine or lysine
-
-
?
additional information
?
-
the optimized peptide substrate sequence is Ile-Arg-Ala-Arg-Ser-Ala-Gly
-
-
?
additional information
?
-
-
the optimized peptide substrate sequence is Ile-Arg-Ala-Arg-Ser-Ala-Gly
-
-
?
additional information
?
-
matriptase has an autocatalytic domain, RQAR. At physiological pH, matriptase is capable of cleaving both the H1 (IQSR-/-GLFG) and H3 (KQTR-/-GLFG) consensus cleavage sequences, whereas no cleavage is observed with the H2 (IESRGLFG) consensus sequence. RQRR-/-VVGG is the optimal cleavage sequence of matriptase
-
-
?
additional information
?
-
-
matriptase has an autocatalytic domain, RQAR. At physiological pH, matriptase is capable of cleaving both the H1 (IQSR-/-GLFG) and H3 (KQTR-/-GLFG) consensus cleavage sequences, whereas no cleavage is observed with the H2 (IESRGLFG) consensus sequence. RQRR-/-VVGG is the optimal cleavage sequence of matriptase
-
-
?
additional information
?
-
the enzyme shows low rate cleavage of the A/Japan/305/57 (H2) peptide mimic (VPQIESRGL) compared to that for the H1 consensus
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
?
additional information
?
-
-
component of the profilaggrin-processing pathway and a key regulator of terminal epidermal differentiation, involved in lipid matrix formation, cornified envelope morphogenesis and stratum corneum desquamation
-
?
additional information
?
-
-
a matriptase-prostasin zymogen activation cascade may be functionally operative in multiple epithelial tissues, but matriptase promotes epithelial carcinogenesis independent of prostasin, overview
-
-
?
additional information
?
-
-
enzyme regulation and deregulation in cancer, overview, matriptase is involved in cancer initiation and progression, it not only facilitates cellular invasiveness but may also activate oncogenic pathways, the protease is essential for postnatal survival, matriptase has pleiotropic functions in the development of the epidermis, hair follicles, and cellular immune system, the protease is essential for postnatal survival, overview
-
-
?
additional information
?
-
-
matriptase inhibition by hepatocyte growth factor activator inhibitor-1 is essential for placental development, mechanism, overview
-
-
?
additional information
?
-
-
matriptase is a type II transmembrane serine protease, that is up-regulated in a variety of cancers and correlates closely with disease progression, it acts as initiator of protease cascades/signaling pathways, overview
-
-
?
additional information
?
-
-
matriptase, a type II transmembrane serine protease, and prostasin, a glycosylphosphatidylinositol-anchored membrane serine protease, are both required for processing of the epidermis-specific polyprotein, profilaggrin, stratum corneum formation, and acquisition of epidermal barrier function, matriptase, an autoactivating protease, acts upstream from prostasin to initiate a zymogen cascade that is essential for epidermal differentiation, overview
-
-
?
additional information
?
-
-
physiological functions, overview, MT-SP1 is critical for proper epidermal development and postnatal survival, MT-SP1 plays a role in embryologic development
-
-
?
additional information
?
-
-
reduced matriptase activity is associated with incomplete terminal differentiation of epidermis, epidermal appendages, oral epithelium, and, likely, other epithelial structures, matriptase activity must be tightly controlled in epithelial tissues by transcriptional and posttranslational mechanisms, as matriptase dysregulation can cause embryonic demise as well as malignant transformation, spatial dysregulation of matriptase leads to the activation of the PI3K-Akt signaling pathway, and dysregulated matriptase synergizes strongly with activated ras to promote epithelial carcinogenesis
-
-
?
additional information
?
-
-
matriptase performs autoactivation
-
-
?
additional information
?
-
-
R/KXSR-/-A is the cleavage sequence of matriptase
-
-
?