3.4.21.104: mannan-binding lectin-associated serine protease-2
This is an abbreviated version!
For detailed information about mannan-binding lectin-associated serine protease-2, go to the full flat file.
Word Map on EC 3.4.21.104
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3.4.21.104
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masps
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spider
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silk
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ficolins
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ampullate
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dragline
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spidroins
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c1s
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clavipes
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nephila
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collectins
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m-ficolin
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widow
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hesperus
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latrodectus
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medicine
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molecular biology
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diagnostics
- 3.4.21.104
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masps
- spider
-
silk
- ficolins
-
ampullate
-
dragline
-
spidroins
- c1s
- clavipes
- nephila
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collectins
- m-ficolin
- widow
- hesperus
- latrodectus
- medicine
- molecular biology
- diagnostics
Reaction
Selective cleavage after Arg223 in complement component C2 (-Ser-Leu-Gly-Arg-/-Lys-Ile-Gln-Ile) and after Arg76 in complement component C4 (-Gly-Leu-Gln-Arg-/-Ala-Leu-Glu-Ile) =
Synonyms
CCP1-CCP2-SP, Mannan-binding lectin associated serine protease-2, mannan-binding lectin-associated serine protease, mannan-binding lectin-associated serine protease 2, mannan-binding lectin-associated serine protease-2, mannose-binding lectin-associated serine protease 2, mannose-binding lectin-associated serine protease-2, mannose-binding lectin-associated-serine protease-2, Map19, MASP, MASP-2, MASP-2A, MASP-2K, MASP2, MBL-associated serine protease, MBL-associated serine protease 2, MBL-associated serine protease-2, MBL-associated-serine protease-2, MBL-MASP, MBL/ficolin-associated serine protease, MBP-associated serine protease, MBP-associated serine protease 2, MBP-associated serine protease-2, S01.229
ECTree
3.4.21.104 mannan-binding lectin-associated serine protease-2Advanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.21.104 - mannan-binding lectin-associated serine protease-2
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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
complement component C2 + H2O
complement component C2a + complement component C2b
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-
-
?
complement component C4 + H2O
complement component C4-alpha + complement component C4-alpha'
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-
-
?
N-tert-butyloxycarbonyl-L-Leu-Gly-L-Arg-7-amido-4-methylcoumarin + H2O
tert-butyloxycarbonyl-L-Leu-Gly-L-Arg + 7-amino-4-methylcoumarin
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-
-
-
?
Phe-Gly-Arg-7-amido-4-methylcoumarin + H2O
Phe-Gly-Arg + 7-amino-4-methylcoumarin
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recombinant enzyme, low activity
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-
?
Phe-Ser-Arg-7-amido-4-methylcoumarin + H2O
Phe-Ser-Arg + 7-amino-4-methylcoumarin
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recombinant enzyme, low activity
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-
?
complement component C2 + H2O
2 fragments of complement component C2
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-
-
-
?
complement component C2 + H2O
2 fragments of complement component C2
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-
-
?
complement component C2 + H2O
2 fragments of complement component C2
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formation of the C3 convertase C4b2a
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?
complement component C2 + H2O
2 fragments of complement component C2
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involved in lectin pathway being part of the innate immune system providing a first line of defense against infections by activation of the complement cascade
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-
?
complement component C2 + H2O
2 fragments of complement component C2
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human substrate
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-
?
complement component C2 + H2O
2 fragments of complement component C2
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involved in activation of complement cascade
-
-
?
complement component C2 + H2O
2 fragments of complement component C2
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only the activated enzyme binds to C2-component
C2a and C2b fragments, preferred substrate
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?
complement component C2 + H2O
?
-
the complement C3 convertase C4bC2b is generated by cleavage of complement C4 and complement C2
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?
complement component C2 + H2O
?
-
SP domain alone can autoactivate and cleave C2
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?
complement component C2 + H2O
?
37°C
the complement C3 convertase C4bC2b is generated by cleavage of complement C4 and complement C2
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?
complement component C2 + H2O
?
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the complement C3 convertase C4bC2b is generated by cleavage of complement C4 and complement C2
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?
complement component C4 + H2O
2 fragments of complement C4
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formation of the C3 convertase C4b2a
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?
complement component C4 + H2O
2 fragments of complement C4
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a fragment corresponding to C4b with appearance of the alpha'-chain
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?
complement component C4 + H2O
2 fragments of complement C4
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involved in lectin pathway being part of the innate immune system providing a first line of defense against infections by activation of the complement cascade
-
-
?
complement component C4 + H2O
2 fragments of complement C4
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human substrate
-
-
?
complement component C4 + H2O
2 fragments of complement C4
the complement control protein CCP module is essential for cleavage
-
-
?
complement component C4 + H2O
2 fragments of complement C4
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activated MBL-MASP-2 complex
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-
?
complement component C4 + H2O
2 fragments of complement C4
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involved in activation of complement cascade
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-
?
complement component C4 + H2O
2 fragments of complement C4
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no activity of the enzyme complexed with myelin basic protein before complex activation by binding to a suitable carbohydrate ligand
C4a fragment, an N-terminal portion, and C4b fragment, the activated form
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?
complement component C4 + H2O
?
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-
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?
complement component C4 + H2O
?
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the complement C3 convertase C4bC2b is generated by cleavage of complement C4 and complement C2
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?
complement component C4 + H2O
?
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SP domain is able to cleave C4, but the presence of the CCP2 domain significantly increases the efficiency
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?
complement component C4 + H2O
?
37°C
the complement C3 convertase C4bC2b is generated by cleavage of complement C4 and complement C2
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?
complement component C4 + H2O
?
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determination of C4b deposition on a mannan surface
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?
complement component C4 + H2O
?
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the complement C3 convertase C4bC2b is generated by cleavage of complement C4 and complement C2
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?
complement component C4 + H2O
complement component C4b + ?
no formation of C4i
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-
?
Protein + H2O
?
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cleaves oligopeptides that contain either Arg or Lys at their P1 positions
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?
Protein + H2O
?
enzyme circulates as a complex with mannose-binding protein, minimal functional unit for complement activation is a ASP homodimer bound to two mannose-binding protein trimeric subunits, complex is formed more readily in the presence of Ca2+
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?
prothrombin + H2O
thrombin + propeptide of thrombin
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activation of thrombin covalentyl bound to a bacterial cell surface
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?
prothrombin + H2O
thrombin + propeptide of thrombin
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cleavage scheme, overview
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?
additional information
?
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MASP-2 is associated with two mannose-binding lectin homologues, one, designated GalBL, corresponds to the MBL-like molecule with the galactose specificity, the other is an authentic MBL with mannose specificity, overview, bony fish have developed a diverged set of MBL homologs, which function in the lectin complement pathway
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?
additional information
?
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MASP-2 is associated with two mannose-binding lectin homologues, one, designated GalBL, corresponds to the MBL-like molecule with the galactose specificity, the other is an authentic MBL with mannose specificity, overview, bony fish have developed a diverged set of MBL homologs, which function in the lectin complement pathway
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?
additional information
?
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hardly any detectable activity on complement C3
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?
additional information
?
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complement C3 is not a natural substrate
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?
additional information
?
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L-ficolin/P35 competes with mannose-binding protein for Ca2+-dependent binding to MASP-2, complex activates complement
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?
additional information
?
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smallest functional unit for complement activation consists of mannose-binding protein dimers bound to MASP-2 homodimers
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?
additional information
?
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enzyme in serum is complexed with mannan-binding lectin MBL and ficolins
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?
additional information
?
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enzyme is complexed with the mannose-binding protein, a recognition molecule for the complement pathway
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?
additional information
?
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enzyme is Mg2+-dependently associated with the mannose-binding protein, a C-type lectin binding to terminal mannose and N-acetylglucosamine moieties on surfaces of certain pathogens and activating the classical complement pathway, the enzyme is not identical with C1r or C1s
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?
additional information
?
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substrate specificity, fluorescent amide compounds are poor substrates, overview
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?
additional information
?
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binding of MBL or ficolins to the cell surface carbohydrates of microbes initiates MASP activation, autoactivation of MASP-2 is the first step in the complement cascade, overview
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?
additional information
?
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binding of MBL or ficolins to the cell surface carbohydrates of microbes initiates MASP activation, autoactivation of MASP-2 is the first step in the complement cascade, overview
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?
additional information
?
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MASP-2 is a central component of the MBL pathway of complement activation, MBL and MASP-2 levels in serum and plasma of healthy individuals are similar and independent of gender and age, while they are increased in colorectal cancer patients, overview
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?
additional information
?
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the enzyme binds to the mannan-binding lectin, MBL, the complex activates the lectin pathway of the complement system, overview
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?
additional information
?
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the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, increased activity of MBL-bound MASP-2 and MASP-2-mediated complement activation in schizophrenia, while the levels of MASP-1 and unbound MBL are similar to healthy persons' levels, overview
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?
additional information
?
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the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, MASP-2 is the major protease of the lectin pathway besides MASP-1 and the minor component MASP-3, autoactivation of MASP-2 is the first step in the complement cascade, MASP-3 might be able to downregulate MASP-2 activity, overview
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-
?
additional information
?
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the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, overview
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?
additional information
?
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the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, overview
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?
additional information
?
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the lectin pathway is one of the ways leading to the cleavage of complement factor C3, a central event in the activation of the complement system, mannan-binding lectin, MBL, promotes the activation of C3 through the combined action of MASP-1 and MASP-2 without appreciable involvement of the alternative pathway, protease MASP-1 collaborates with MASP-2 in the generation of C3 convertase, overview
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?
additional information
?
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the lectin pathway of complement plays a key role in the immune system by recognising pathogens through patterns of sugar moities displayed on their cell sufaces and neutralizing them in an antibody-independent reaction cascade, MASP-2 binds to the mannan-binding lectin, MBL, the complex activates the lectin pathway of the complement system, interactions analysis, overview
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?
additional information
?
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development and evaluation of a fluorochrome-linked immunoassay for quantitative determination of MBL, MASP-2 and C3 convertase activity in serum samples, overview
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?
additional information
?
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MASP-2 acts in complex with mannan-binding lectin, MBL, overview
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?
additional information
?
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substrate specificity, overview, no activity with gelatin, the enzyme performs proteolytic autoactivation, the N-terminal third of MASP-2, i.e. MAp19 or sMAp, comprises the CUB1 and EGF modules of MASP-2 plus an extra C-terminal EQSL tetrapeptide, which is encoded by a separate exon, MAp19 is a product of alternative splicing of the MASP-2 gene and is catalytically inactive
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?
additional information
?
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the enzyme performs proteolytic autoactivation, mannan-binding lectin, MBL, structure and Ca2+-dependent interaction with the enzyme, overview, MAp19 is a product of alternative splicing of the MASP-2 gene and is catalytically inactive, overview
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?
additional information
?
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MBL-MASP complexes, bound to mannan-agarose, generate clots when incubated with calcified plasma or purified fibrinogen and factor XIII
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?
additional information
?
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MASP-2 has all the activities required for lectin pathway activation, it can autoactivate and cleave both complement components C4 and C2
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?
additional information
?
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-
binding of MBL or ficolins to the cell surface carbohydrates of microbes initiates MASP activation, autoactivation of MASP-2 is the first step in the complement cascade, overview
-
-
?
additional information
?
-
-
the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, overview, a truncated form of MASP-2, named small MBL-associated protein, sMAP, is also associated with MBL/ficolin-MASP complexes, MASP-2 is essential for the activation of C4 and sMAP plays a regulatory role in the activation of the lectin pathway, overview
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?
additional information
?
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MASP-2 acts in complex with mannan-binding lectin, MBL, a truncated form of MASP-2, named small MBL-associated protein, sMAP, is also associated with MBL/ficolin-MASP complexes, overview
-
-
?
additional information
?
-
-
the enzyme binds to the mannan-binding lectin, the complex activates the lectin pathway of the complement system, MASP-2 is the major protease of the lectin pathway besides MASP-1 and the minor component MASP-3, autoactivation of MASP-2 is the first step in the complement cascade, MASP-3 might be able to downregulate MASP-2 activity, overview
-
-
?
additional information
?
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the enzyme is part of the lectin pathway of the complement system, it is also capable of promoting fibrinogen turnover by cleavage of prothrombin, generating thrombin
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?
additional information
?
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MASP-2 interactions with wild-type and mutant ficolins, overview
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-
?
additional information
?
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MASP2 acts in a mannan-bound MBL/MASP2 complex
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?
