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Information on EC 3.4.21.B7 - mannan-binding lectin-associated serine protease 1 and Organism(s) Mus musculus and UniProt Accession P98064
for references in articles please use BRENDA:EC3.4.21.B7preliminary BRENDA-supplied EC number
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3.4.21.B7 mannan-binding lectin-associated serine protease 1Specify your search results
Word Map
- 3.4.21.B7
- masp-3
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silk
- spider
- ficolins
-
dragline
- c1s
-
ampullate
-
spidroins
-
convertase
-
collagen-like
- clavipes
-
collectins
- m-ficolin
-
autoactivation
- nephila
-
subcomponents
-
complement-activating
- c1-inhibitor
- latrodectus
-
pattern-recognition
- widow
-
fibrinogen-like
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protease-2
-
opsonin
-
extensibility
-
urochord
-
c1-inh
- hesperus
- medicine
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
endopeptidase activity. It triggers the activation of complement cascade by activating the C4 and C2 components. It activates the C4 component by cleaving the alpha-chain of C4
Synonyms
masp-1, masp1, mbl-associated serine protease, mbl-masp, ra-reactive factor, mannose-binding lectin-associated serine protease, mannan-binding lectin-associated serine protease-1, mannan-binding lectin-associated serine protease, mbl-associated serine protease-1, mannan-binding lectin-associated serine protease 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MASP-1
Ra-reactive factor
-
complex of multiple polysaccaride-binding subunits associated with serine protease P100
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
214915-11-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-Phe-Pip-Arg-4-nitroanilide + H2O
D-Phe-Pip-Arg + 4-nitroaniline
a chromogenic thrombin substrate, recombinant human mannose-binding lectin alone fails to cleave the substrate, but cleavage is restored when the recombinant enzyme MASP-1 is added to either MASP-1/-3 KO sera or rhMBL
-
-
?
N-carbobenzoxy-L-lysine-4-nitrophenyl ester + H2O
N-carbobenzoxy-L-Lys + 4-nitrophenol
-
-
-
?
MASP-2 zymogen + H2O
mature MASP-2 + ?
MASP-2 is a key enzyme that cleaves C4 and C2 to assemble a C3 convertase
-
-
?
additional information
?
-
involved in activation of complement cascade, enzyme is complexed with the mannose-binding protein
-
?
additional information
?
-
-
involved in activation of complement cascade, enzyme is complexed with the mannose-binding protein
-
?
additional information
?
-
MASP-1 contributes to the activation of the lectin pathway, probably through the activation of MASP-2
-
-
?
additional information
?
-
-
MASP-1 contributes to the activation of the lectin pathway, probably through the activation of MASP-2
-
-
?
additional information
?
-
-
involved in activation of complement cascade
-
?
additional information
?
-
-
involved in activation of complement cascade
-
?
additional information
?
-
-
involved in activation of complement cascade, forms a complex with mannose-binding lectin
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
MASP-2 zymogen + H2O
mature MASP-2 + ?
MASP-2 is a key enzyme that cleaves C4 and C2 to assemble a C3 convertase
-
-
?
additional information
?
-
involved in activation of complement cascade, enzyme is complexed with the mannose-binding protein
-
?
additional information
?
-
-
involved in activation of complement cascade, enzyme is complexed with the mannose-binding protein
-
?
additional information
?
-
MASP-1 contributes to the activation of the lectin pathway, probably through the activation of MASP-2
-
-
?
additional information
?
-
-
MASP-1 contributes to the activation of the lectin pathway, probably through the activation of MASP-2
-
-
?
additional information
?
-
-
involved in activation of complement cascade
-
?
additional information
?
-
-
involved in activation of complement cascade
-
?
additional information
?
-
-
involved in activation of complement cascade, forms a complex with mannose-binding lectin
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
at physiological ionic strength, alternative pathway activity is observed, high ionic strength buffer suppresses the weaker alternative pathway activity of the Masp1 knockout mouse to background levels
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
MASP-1 is present in the sera of mannose binding lectin/ficolin-A-deficient mice
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
enzyme-deficient mice lack alternative pathway activation because factor D remains as a proenzyme in the serum
metabolism
the enzyme is part of the lectin pathway complement cascade, that is part of the innate immune system responsible for the initiation of inflammation and elimination of invading foreign cells
physiological function
metabolism
influence of buffer composition on the activity of the alternative pathway of complement activation in mice in the presence and the absence of the Masp1 gene products: MASP-1, MASP-3, and MAp44
physiological function
physiological function
MASP-1 and MASP-3 seem to be involved in activation of both the lectin and alternative complement system pathways
physiological function
the mannose-binding lectin-associated serine protease-1 is a significant contributor to coagulation in a murine model of occlusive thrombosis, it plays a key role in thrombus formation in vitro and in vivo. Whole blood aggregation demonstrated increased mannose-binding lectin-mannose-binding lectin-associated serine protease complex-dependent platelet aggregation
physiological function
-
MASP-1 does not require binding to mannose binding lectin-A, mannose binding lectin-C, or ficolin-A to activate the alternative pathway of complement
physiological function
the pro-factor D cleaving activity of MASP-1/-3 is not required for alternative pathway function, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29000
70000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
95% loss of C4-cleaving activity after 30 min in 130 mM NaCl, 2 mM CaCl2, 20 mM Tris, pH8
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takahashi, A.; Takayama, Y.; Hatsuse, H.; Kawakami, M.
Presence of a serine protease in the complement-activating component of the complement-dependent bactericidal factor, RaRF, in mouse serum
Biochem. Biophys. Res. Commun.
190
681-687
1993
Mus musculus
Matsushita, M.; Endo, Y.; Fujita, T.
MASP1 (MBL-associated serine protease 1)
Immunobiology
199
340-347
1998
Homo sapiens, Mus musculus
Takayama, Y.; Takada, F.; Takahashi, A.; Kawakami, M.
A 100-kDa protein in the C4-activating component of Ra-reactive factor is a new serine protease having module organization similar to C1r and C1s
J. Immunol.
152
2308-2316
1994
Mus musculus (P98064), Mus musculus, Mus musculus BALB/c (P98064)
Ogata, R.T.; Low, P.J.; Kawakami, M.
Substrate specificities of the protease of mouse serum Ra-reactive factor
J. Immunol.
154
2351-2357
1995
Mus musculus
Schwaeble, W.J.; Stover, C.; Reid, K.B.
Mannan-binding lectin-associated serine proteases
Handbook of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
2
1623-1627
2004
Lethenteron camtschaticum, Halocynthia roretzi, Homo sapiens, Mus musculus, Rattus norvegicus, Xenopus laevis, Branchiostoma belcheri
-
Takahashi, M.; Iwaki, D.; Kanno, K.; Ishida, Y.; Xiong, J.; Matsushita, M.; Endo, Y.; Miura, S.; Ishii, N.; Sugamura, K.; Fujita, T.
Mannose-binding lectin (MBL)-associated serine protease (MASP)-1 contributes to activation of the lectin complement pathway
J. Immunol.
180
6132-6138
2008
Mus musculus (P98064), Mus musculus
Banda, N.K.; Takahashi, M.; Takahashi, K.; Stahl, G.L.; Hyatt, S.; Glogowska, M.; Wiles, T.A.; Endo, Y.; Fujita, T.; Michael Holers, V.; Arend, W.P.
Mechanisms of mannose-binding lectin-associated serine proteases-1/3 activation of the alternative pathway of complement
Mol. Immunol.
49
281-289
2011
Mus musculus
Sekine, H.; Takahashi, M.; Iwaki, D.; Fujita, T.
The role of MASP-1/3 in complement activation
Adv. Exp. Med. Biol.
735
41-53
2013
Mus musculus (P98064), Mus musculus
La Bonte, L.; Pavlov, V.; Tan, Y.; Takahashi, K.; Takahashi, M.; Banda, N.; Zou, C.; Fujita, T.; Stahl, G.
Mannose-binding lectin-associated serine protease-1 is a significant contributor to coagulation in a murine model of occlusive thrombosis
J. Immunol.
188
885-891
2012
Mus musculus (P98064), Mus musculus
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