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EC Tree
The taxonomic range for the selected organisms is: Mus musculus The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala-/- > -Val-/-
Synonyms
proteinase 3, proteinase-3, protease 3, prtn3, myeloblastin, neutrophil serine protease, human pr3, neutrophil proteinase 3, human proteinase 3, proteinase3,
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Leukocyte proteinase 3
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-
-
-
Leukocyte proteinase 4
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-
-
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Wegener's autoantigen
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-
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Wegener's granulomatosis autoantigen
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-
-
-
PR3
-
-
-
-
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hydrolysis of peptide bond
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-
-
-
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MeOSuc-AAPV-4-nitroanilide + H2O
MeOSuc-AAPV + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
MeOSuc-AIPM-4-nitroanilide + H2O
MeOSuc-AIPM + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
oxidized insulin B chain + H2O
?
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
Suc-AAA-4-nitroanilide + H2O
Suc-AAA + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
Suc-AAPL-4-nitroanilide + H2O
Suc-AAPL + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
Suc-AAPV-4-nitroanilide + H2O
Suc-AAPV + 4-nitroaniline
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
-
-
?
surfactant protein D + H2O
?
-
a fragment of about 35000 Da
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?
DRDAVDRDID + H2O
?
-
-
-
-
?
DVARVKDRQEG + H2O
?
-
-
-
-
?
GDVAVYEEN + H2O
?
-
-
-
-
?
RDVARCRDRQEG + H2O
?
-
-
-
-
?
RDVARCRDRQQG + H2O
?
-
-
-
-
?
VARVRDR + H2O
?
-
-
-
-
?
additional information
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additional information
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in mouse PR3 binding sites S6, S5, S1' and S3' are clearly polar, S2' is pretty polar, while S4, S3, S1, S4' are rather hydrophobic. VADVKDR does not interact properly with mouse PR3
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?
additional information
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unlike human PR3, mouse PR3 is unlikely to bind substrates with acidic groups (Asp, Glu) on the S side. Efficient substrates of human PR3 may be poor substrates of mouse PR3
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?
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alpha1-antitrypsin
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 0.74 M
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Eglin c
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 3.3 M
elafin
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 0.99 M
-
SLPI
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, limited inhibition, more than 75% of activity remained in the presence of the highest concentration of inhibitor
Val15-aprotinin
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 447 M
-
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1.1
MeOSuc-AAPV-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
1.5
MeOSuc-AIPM-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
0.61
Suc-AAA-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
3.5
Suc-AAPL-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
2.5
Suc-AAPV-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
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6.2
MeOSuc-AAPV-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
7.2
MeOSuc-AIPM-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
0.031
Suc-AAA-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
0.16
Suc-AAPL-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
11.2
Suc-AAPV-4-nitroanilide
52 mM NaCl, 0.5% Triton X-100 (w/v), 10% dimethylformamide (v/v), pH 8.0
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740
alpha1-antitrypsin
Mus musculus
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 0.74 M
-
3300
Eglin c
Mus musculus
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 3.3 M
990
elafin
Mus musculus
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 0.99 M
-
447000
Val15-aprotinin
Mus musculus
MeOSuc-AAPV-4-nitroanilide as substrate, 1% Triton X-100 (w/v), 20% dimethylformamide (v/v), pH 8.0, IC50 = 447 M
-
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6.7
calculated from amino acid sequence
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-
SwissProt
brenda
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proteinase 3 is considerably more expressed in bone marrow than in the peripheral blood
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low expression
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behaves as a peripheral membrane protein. The mouse form is globally more electronegative than the human form. As a consequence of differences in sequence and structural properties, mouse PR3 is likely to be able to bind to the plasma membrane using the same region as human PR3, although less strongly and specifically
brenda
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malfunction
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in mice lacking neutrophil serine PR3 (DPPI-/- mice), inhibition of caspase 1 activity results in decreased bioactive IL-1beta concentrations in the synovial tissue and less suppression of chondrocyte anabolic function. Dual blockade of both PR3 and caspase 1 leads to protection against cartilage and bone destruction. Deficiency of PR3 in combination with inhibition of caspase 1 does not reduce the joint swelling in streptococcal cell wall-induced acute arthritis
physiological function
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caspase 1-independent processing of IL-1beta occurs in arthritis by serine proteases such as PR3
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PRTN3_MOUSE
254
0
27626
Swiss-Prot
Secretory Pathway (Reliability: 1 )
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22000
3 * 29000 + 1 * 22000, SDS-PAGE
29000
3 * 29000 + 1 * 22000, SDS-PAGE
30000
x * 30000, SDS-PAGE
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multimer
3 * 29000 + 1 * 22000, SDS-PAGE
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expression in HMC-1 cells and 293 cells
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medicine
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PR3-anti-neutrophil cytoplasmic antibodies from Wegeners granulomatosis patients do not recognize the natively folded murine PR3
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Wiesner, O.; Litwiller, R.D.; Hummel, A.M.; Viss, M.A.; McDonald, C.J.; Jenne, D.E.; Fass, D.N.; Specks, U.
Differences between human proteinase 3 and neutrophil elastase and their murine homologues are relevant for murine model experiments
FEBS Lett.
579
5305-5312
2005
Homo sapiens (P24158), Homo sapiens, Mus musculus (Q61096), Mus musculus
brenda
Hirche, T.O.; Crouch, E.C.; Espinola, M.; Brokelman, T.J.; Mecham, R.P.; DeSilva, N.; Cooley, J.; Remold-O'Donnell, E.; Belaaouaj, A.
Neutrophil serine proteinases inactivate surfactant protein D by cleaving within a conserved subregion of the carbohydrate recognition domain
J. Biol. Chem.
279
27688-27698
2004
Homo sapiens (P24158), Homo sapiens, Mus musculus (Q61096), Mus musculus
brenda
Jenne, D.E.; Kuhl, A.
Production and applications of recombinant proteinase 3, Wegeners autoantigen: problems and perspectives
Clin. Nephrol.
66
153-159
2006
Homo sapiens, Mus musculus
brenda
Csernok, E.; Moosig, F.; Gross, W.L.
Pathways to ANCA production: From differentiation of dendritic cells by proteinase 3 to B lymphocyte maturation in Wegeners granuloma
Clin. Rev. Allergy Immunol.
34
300-306
2008
Homo sapiens, Mus musculus
brenda
Hajjar, E.; Korkmaz, B.; Reuter, N.
Differences in the substrate binding sites of murine and human proteinase 3 and neutrophil elastase
FEBS Lett.
581
5685-5690
2007
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Joosten, L.A.; Netea, M.G.; Fantuzzi, G.; Koenders, M.I.; Helsen, M.M.; Sparrer, H.; Pham, C.T.; van der Meer, J.W.; Dinarello, C.A.; van den Berg, W.B.
Inflammatory arthritis in caspase 1 gene-deficient mice: contribution of proteinase 3 to caspase 1-independent production of bioactive interleukin-1beta
Arthritis Rheum.
60
3651-3662
2009
Homo sapiens, Mus musculus
brenda
Hajjar, E.; Broemstrup, T.; Kantari, C.; Witko-Sarsat, V.; Reuter, N.
Structures of human proteinase 3 and neutrophil elastase - so similar yet so different
FEBS J.
277
2238-2254
2010
Homo sapiens, Mus musculus
brenda
Relle, M.; Thomaidis, T.; Galle, P.R.; Schwarting, A.
Comparative aspects of murine proteinase 3
Rheumatol. Int.
31
1105-1111
2011
Mus musculus (Q61096), Mus musculus
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