3.4.22.26 (D)-Leu-(L)-Ser-(L)-Thr-(L)-Arg p-nitroanilide + H2O - Mus musculus ? - ? 15932 3.4.22.26 7-methoxycoumarin-4-acetyl-GYPGQV + H2O - Homo sapiens 7-methoxycoumarin-4-acetate + GYPGQV - ? 449381 3.4.22.26 7-methoxycoumarin-4-acetyl-IVGGQE + H2O - Homo sapiens 7-methoxycoumarin-4-acetate + IVGGQE - ? 449382 3.4.22.26 7-methoxycoumarin-4-acetyl-SFLLRN + H2O - Homo sapiens 7-methoxycoumarin-4-acetate + SFLLRN - ? 449383 3.4.22.26 7-methoxycoumarin-4-acetyl-VSQKSP + H2O - Homo sapiens 7-methoxycoumarin-4-acetate + VSQKSP - ? 449384 3.4.22.26 7-methoxycoumarin-4-acetyl-VYQPQP + H2O - Homo sapiens 7-methoxycoumarin-4-acetate + VYQPQP - ? 449385 3.4.22.26 AVSQSKP-7-amido-4-methylcoumarin + H2O low activity Rattus norvegicus AVSQSKP + 7-amino-4-methylcoumarin - ? 449623 3.4.22.26 AVYQPQP-7-amido-4-methylcoumarin + H2O low activity Rattus norvegicus AVYQPQP + 7-amino-4-methylcoumarin - ? 449624 3.4.22.26 benzyloxycarbonyl-Arg-Arg-4-nitroanilide + H2O - Homo sapiens benzyloxycarbonyl-Arg-Arg + 4-nitroaniline - ? 366770 3.4.22.26 benzyloxycarbonyl-Leu-Pro-Arg-4-nitroanilide + H2O - Homo sapiens benzyloxycarbonyl-Leu-Pro-Arg + 4-nitroaniline - ? 366768 3.4.22.26 benzyloxycarbonyl-Val-Pro-Arg-4-nitroanilide + H2O - Homo sapiens benzyloxycarbonyl-Val-Pro-Arg + 4-nitroaniline - ? 366769 3.4.22.26 Bz-Ile-Glu-Arg-4-nitroanilide + H2O chromogenic commercial substrate Homo sapiens Bz-Ile-Glu-Arg + 4-nitroaniline - ? 384389 3.4.22.26 collagen type IV + H2O - Homo sapiens ? - ? 65137 3.4.22.26 D-Ala-Pro-Arg-4-nitroanilide + H2O - Homo sapiens D-Ala-Pro-Arg + 4-nitroaniline - ? 366760 3.4.22.26 D-Ile-Pro-Arg-4-nitroanilide + H2O - Homo sapiens D-Ile-Pro-Arg + 4-nitroaniline - ? 361879 3.4.22.26 D-Phe-Pip-Arg-4-nitroanilide + H2O - Homo sapiens D-Phe-Pip-Arg + 4-nitroaniline - ? 366281 3.4.22.26 Factor X + H2O - Mus musculus Factor Xa + ? - ? 15931 3.4.22.26 Factor X + H2O - Homo sapiens Factor Xa + ? - ? 15931 3.4.22.26 Factor X + H2O - Oryctolagus cuniculus Factor Xa + ? - ? 15931 3.4.22.26 Factor X + H2O primary cleavage site: Tyr21-Asp22, secondary sites: Asp14-Ser15 and Thr18-Glu19 Homo sapiens Factor Xa + ? - ? 15931 3.4.22.26 Factor X + H2O primary cleavage site: Tyr21-Asp22, secondary sites: Asp14-Ser15 and Thr18-Glu19 Rattus norvegicus Factor Xa + ? - ? 15931 3.4.22.26 factor X + H2O - Homo sapiens ? - ? 65167 3.4.22.26 factor X + H2O that triggers blood coagulation by directly activating factor X in the absence of factor VII Mus musculus ? - ? 65167 3.4.22.26 factor X + H2O that triggers blood coagulation by directly activating factor X in the absence of factor VII Oryctolagus cuniculus ? - ? 65167 3.4.22.26 factor X + H2O thiol protease with thrombin-like specificity Mus musculus ? - ? 65167 3.4.22.26 factor X + H2O factor X-activating cysteine proteinase Mus musculus ? - ? 65167 3.4.22.26 factor X + H2O factor X-activating cysteine proteinase Oryctolagus cuniculus ? - ? 65167 3.4.22.26 factor X + H2O - Homo sapiens factor Xa - ? 74158 3.4.22.26 factor X + H2O cleavage of Arg-Ile bond Homo sapiens factor Xa - ? 74158 3.4.22.26 factor X + H2O cleavage of Arg-Ile bond Oryctolagus cuniculus factor Xa - ? 74158 3.4.22.26 factor X + H2O cleavage of Arg-Ile bond in factor X heavy chain Homo sapiens factor Xa - ? 74158 3.4.22.26 factor X + H2O cleavage of Arg-Ile bond in factor X heavy chain, activation of the coaglutation factor X and thereby activation of the plasma blood clotting cascade Homo sapiens factor Xa - ? 74158 3.4.22.26 factor X + H2O cleavage of Arg-Ile bond in factor X heavy chain, activation of the coaglutation factor X and thereby activation of the plasma blood clotting cascade Oryctolagus cuniculus factor Xa - ? 74158 3.4.22.26 factor X + H2O cleavage of Arg-Ile bond, activation of the coaglutation factor X Homo sapiens factor Xa - ? 74158 3.4.22.26 factor X + H2O activation Homo sapiens factor Xa - ? 74158 3.4.22.26 factor X + H2O activation, commercial substrate Homo sapiens factor Xa - ? 74158 3.4.22.26 Fibrinogen + H2O - Homo sapiens ? - ? 15619 3.4.22.26 Fibronectin + H2O enzyme CP cleaves fibronectin between Ala and Val residues, in regions rich in Pro and Gln residues. The 45 and 60 kDa fragments have the same N-terminal sequence, generated by cleavage of the bond between Ala292 and Val293 Homo sapiens ? - ? 15394 3.4.22.26 GDR-7-amido-4-methylcoumarin + H2O low activity Rattus norvegicus GDR + 7-amino-4-methylcoumarin - ? 449941 3.4.22.26 Glu-Glu-Phe-Lys-4-nitroanilide + H2O - Homo sapiens Glu-Glu-Phe-Lys + 4-nitroaniline - ? 366767 3.4.22.26 Glu-Glu-Pro-Arg-4-nitroanilide + H2O - Homo sapiens Glu-Glu-Pro-Arg + 4-nitroaniline - ? 366761 3.4.22.26 inactive factor X + H2O activation of blood coagulation factor X Homo sapiens active factor Xa + ? - ? 448689 3.4.22.26 inactive factor X + H2O activation of blood coagulation factor X Rattus norvegicus active factor Xa + ? - ? 448689 3.4.22.26 inactive factor X + H2O activation of blood coagulation factor X, degradation of factor X during 24 h Homo sapiens active factor Xa + ? - ? 448689 3.4.22.26 inactive factor X + H2O activation of blood coagulation factor X (57.3 kDa), cleavage of factor X at the conventional activation site, i.e. between Arg52 and Ile53, in the heavy chain Homo sapiens active factor Xa + ? - ? 448689 3.4.22.26 Laminin + H2O - Homo sapiens ? - ? 16571 3.4.22.26 Leu-Pro-Arg-4-nitroanilide + H2O - Homo sapiens Leu-Pro-Arg + 4-nitroaniline - ? 366766 3.4.22.26 LPAPR-7-amido-4-methylcoumarin + H2O - Homo sapiens LPAPR + 7-amino-4-methylcoumarin - ? 450235 3.4.22.26 methylsulfonyl-D-cyclohexylalanyl-butyl-Arg-4-nitroanilide + H2O - Homo sapiens methylsulfonyl-D-cyclohexylalanyl-butyl-Arg + 4-nitroaniline - ? 366763 3.4.22.26 additional information substrate specificity, overview Homo sapiens ? - ? 89 3.4.22.26 additional information substrate recognition depends on the secondary and tertiary configuration of the protein substrate rather than on the primary sequence alone, no activity with substrates containing the sequence Xaa-Lys-ProP2-TyrP1- Homo sapiens ? - ? 89 3.4.22.26 additional information enzyme seems to be regulated allosterically Homo sapiens ? - ? 89 3.4.22.26 additional information the activity of cancer procoagulant in cases of uterine leiomyomas, overview Homo sapiens ? - ? 89 3.4.22.26 additional information the enzyme is able to stimulate blood platelet adhesion to fibrinogen and collagen, which can also play a role in metastatic spread of cancer as well as primary tumor growth Homo sapiens ? - ? 89 3.4.22.26 additional information the enzyme plays a role in pathogenesis of cancer-related thrombosis, the enzyme concentration in serum is positively correlated to fibrinogen concentration, but negatively correlated to free protein S plasma content, determination of prothrobotic parameters and correlation to enzyme activity, overview Homo sapiens ? - ? 89 3.4.22.26 additional information the enzyme is a cysteine protease, the enzyme mediates growth and adhesion of MCF-7 cancer cells to vitronectin in vitro Homo sapiens ? - ? 89 3.4.22.26 additional information cancer procoagulant is a cysteine protease acting as an activator of coagulation factor X, the protein activates factor X in the absence of tissue factor and factor VII Rattus norvegicus ? - ? 89 3.4.22.26 additional information high level of cancer procoagulant is a risk factor for multiple myeloma Homo sapiens ? - ? 89 3.4.22.26 additional information rat and human cancer procoagulant activity bind similarly to antiCP antibodies Rattus norvegicus ? - ? 89 3.4.22.26 additional information in vitro screening of synthetic fluorogenic substrates for detection of cancer procoagulant activity, substrate design, synthesis, and evaluation, e.g. based on the RGD motif of fibronectin, overview. The most reliable assay for the quantification of cancer procoagulant activity is the three-stage chromogenic assay which utilises the ability of cancer procoagulant to activate factor X. In this assay, the activation of factor X leads to the formation of activated thrombin from prothrombin and the eventual hydrolyses of a thrombin chromogenic substrate which contains a p nitroaniline leaving group. No activity with tert-benzyloxycarbonyl-AVSQSKP-7-amido-4-methylcoumarin Rattus norvegicus ? - ? 89 3.4.22.26 additional information substrate specificity analysis, mass spectrometric detection of cleavage products. No activity with tert-benzyloxycarbonyl-QSPVR-7-amido-4-methylcoumarin and TLDPR-7-amido-4-methylcoumarin. Enzyme CP shows very little cysteine protease activity, it appears to exhibit mixed protease activity, but acts predominantly as a serine protease Homo sapiens ? - ? 89 3.4.22.26 N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O - Homo sapiens N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline - ? 366762 3.4.22.26 N-p-tosyl-Gly-Pro-Lys-4-nitroanilide + H2O - Homo sapiens N-p-tosyl-Gly-Pro-Lys + 4-nitroaniline - ? 366759 3.4.22.26 PAR-1 receptor + H2O - Homo sapiens ? - ? 366771 3.4.22.26 PAR-1 receptor + H2O enzyme competes with thrombin for the same protease-activated receptor, i.e. PAR-1, on the blood platelet surface Homo sapiens ? - ? 366771 3.4.22.26 PKSQSVA-7-amido-4-methylcoumarin + H2O low activity Rattus norvegicus PKSQSVA + 7-amino-4-methylcoumarin - ? 450473 3.4.22.26 PQPQYVA-7-amido-4-methylcoumarin + H2O low activity Rattus norvegicus PQPQYVA + 7-amino-4-methylcoumarin - ? 450488 3.4.22.26 PQVR-7-amido-4-methylcoumarin + H2O - Homo sapiens PQVR + 7-amino-4-methylcoumarin - ? 450489 3.4.22.26 PQVR-7-amido-4-methylcoumarin + H2O - Rattus norvegicus PQVR + 7-amino-4-methylcoumarin - ? 450489 3.4.22.26 QSPVR-7-amido-4-methylcoumarin + H2O - Homo sapiens QSPVR + 7-amino-4-methylcoumarin - ? 450536 3.4.22.26 QVR-7-amido-4-methylcoumarin + H2O - Homo sapiens QVR + 7-amino-4-methylcoumarin - ? 450537 3.4.22.26 RGD-7-amido-4-methylcoumarin + H2O low activity Rattus norvegicus RGD + 7-amino-4-methylcoumarin - ? 450552 3.4.22.26 Sar-Pro-Arg-p-nitroanilide + H2O - Rattus norvegicus Sar-Pro-Arg + p-nitroaniline - ? 406646 3.4.22.26 sarcosyl-Pro-Arg-4-nitroanilide + H2O - Homo sapiens sarcosyl-Pro-Arg + 4-nitroaniline - ? 366764 3.4.22.26 tert-butoxycarbonyl-AVR-7-amido-4-methylcoumarin + H2O high activity Rattus norvegicus tert-butoxycarbonyl-AVR + 7-amino-4-methylcoumarin - ? 450734 3.4.22.26 tert-butoxycarbonyl-AVYQPQP-7-amido-4-methylcoumarin + H2O high activity Rattus norvegicus tert-butoxycarbonyl-AVYQPQP + 7-amino-4-methylcoumarin - ? 450735 3.4.22.26 tert-butoxycarbonyl-GDR-7-amido-4-methylcoumarin + H2O - Rattus norvegicus tert-butoxycarbonyl-GDR + 7-amino-4-methylcoumarin - ? 450736 3.4.22.26 tert-butoxycarbonyl-PKSQSVA-7-amido-4-methylcoumarin + H2O low activity Rattus norvegicus tert-butoxycarbonyl-PKSQSVA + 7-amino-4-methylcoumarin - ? 450737 3.4.22.26 tert-butoxycarbonyl-PQPQYVA-7-amido-4-methylcoumarin + H2O - Rattus norvegicus tert-butoxycarbonyl-PQPQYVA + 7-amino-4-methylcoumarin - ? 450738 3.4.22.26 tert-butoxycarbonyl-PQVR-7-amido-4-methylcoumarin + H2O best substrate, this substrate is also cleaved by collagenase Rattus norvegicus tert-butoxycarbonyl-PQVR + 7-amino-4-methylcoumarin - ? 450739 3.4.22.26 tert-butoxycarbonyl-QVR-7-amido-4-methylcoumarin + H2O best synthetic substrate Homo sapiens tert-butoxycarbonyl-QVR + 7-amino-4-methylcoumarin - ? 450740 3.4.22.26 tert-butoxycarbonyl-QVR-7-amido-4-methylcoumarin + H2O high activity Rattus norvegicus tert-butoxycarbonyl-QVR + 7-amino-4-methylcoumarin - ? 450740 3.4.22.26 tert-butoxycarbonyl-RGD-7-amido-4-methylcoumarin + H2O - Rattus norvegicus tert-butoxycarbonyl-RGD + 7-amino-4-methylcoumarin - ? 450741 3.4.22.26 thrombin TH + H2O - Mus musculus ? - ? 15933 3.4.22.26 Val-Pro-Arg-4-nitroanilide + H2O - Homo sapiens Val-Pro-Arg + 4-nitroaniline - ? 366765