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Information on EC 3.4.21.104 - mannan-binding lectin-associated serine protease-2 and Organism(s) Mus musculus and UniProt Accession Q91WP0
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3.4.21.104 mannan-binding lectin-associated serine protease-2Specify your search results
Word Map
- 3.4.21.104
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masps
- spider
-
silk
- ficolins
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ampullate
-
dragline
-
spidroins
- c1s
- clavipes
- nephila
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collectins
- m-ficolin
- widow
- hesperus
- latrodectus
- medicine
- molecular biology
- diagnostics
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
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
masp2, map19, mbl-associated serine protease 2, mannan-binding lectin-associated serine protease-2, mbp-associated serine protease, ccp1-ccp2-sp, mannan-binding lectin-associated serine protease 2, mannose-binding lectin-associated serine protease-2, mannose-binding lectin-associated serine protease 2, mannan-binding lectin associated serine protease-2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
214915-16-9
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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 C4 + H2O
2 fragments of complement C4
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activated MBL-MASP-2 complex
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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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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
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?
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
additional information
?
-
-
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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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ficolins
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are pattern recognition proteins acting in innate immunity, and triggering the activation of the lectin complement pathway through MBL-associated serine proteases
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mannan-binding lectin
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a C-type serum lectin acting as a pattern recognition molecule, associated to MASPs, binding triggers activation of MASPs, overview
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mannose-binding lectin
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MBL, is a pattern recognition protein acting in innate immunity, and triggering the activation of the lectin complement pathway through MBL-associated serine proteases
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
effect of MASP-2 deficiency in an isogenic mouse model of renal transplantation. Wild-type kidneys grafted into wild-type recipients develop acute renal failure. Wild-type grafts transplanted into MASP-2-deficient recipients show significantly better kidney function, less C3 deposition, and less ischemia reperfusion injury. In the absence of donor or recipient complement C4, the wild-type to wild-type phenotype is preserved, indicating that the MASP-2-mediated damage is independent of C4 activation. In mice deficient for both MASP-2 and C4, the protection from postoperative acute renal failure is no greater than in mice with MASP-2 deficiency alone. Injury occurs through MASP-2-dependent activation events independent of C4
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). MASP2_MOUSE
685
0
75517
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000
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x * 87000, proenzyme form, SDS-PAGE, 1 * 52000, heavy enzyme chain, active enzyme form, SDS-PAGE
87000
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x * 87000, proenzyme form, SDS-PAGE, 1 * 52000, heavy enzyme chain, active enzyme form, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
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x * 87000, proenzyme form, SDS-PAGE, 1 * 52000, heavy enzyme chain, active enzyme form, SDS-PAGE
additional information
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enzyme structure and domain organization: CUB1 module, EGF module, CUB2 module, CCP1, CCP2, and serine protease domains, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
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autoactivation, autoactivation of the recombinant enzyme during purification
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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construction of MASP-2-deficient mice, MASP-2-deficient mice show reduced activity for C3 deposition on the surface of mannan and zymosan, lectin complement pathway and phenotype, overview
additional information
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when recombinant sMAP and recombinant MASP-2 reconstitute the MBL-MASP-sMAP complex in deficient serum, the binding of these recombinant proteins to MBL is competitive, and the C4 cleavage activity of the MBL-MASP-sMAP complex is restored by the addition of rMASP-2, whereas the addition of rsMAP attenuates the activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
MASP-2 promoter sequence analysis, phylogenetic analysis, expression regulation involves Stat3 and StatB, Stat3 is more important, overview
expression using a Drosophila melanogaster expression system, C4-cleavage activity reconstitution of the enzyme-deficient mutant by addition of recombinant enzyme to deficient serum
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of the MBL-MASP-sMAP complex using recombinant proteins, overview
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Iwaki, D.; Fujita, T.
Production and purification of recombinants of mouse MASP-2 and sMAP
J. Endotoxin Res.
11
47-50
2005
Mus musculus
Takahashi, M.; Mori, S.; Shigeta, S.; Fujita, T.
Role of MBL-associated serine protease (MASP) on activation of the lectin complement pathway
Adv. Exp. Med. Biol.
598
93-104
2007
Homo sapiens, Homo sapiens (O00187), Mus musculus
Unterberger, C.; Hanson, S.; Klingenhoff, A.; Oesterle, D.; Frankenberger, M.; Endo, Y.; Matsushita, M.; Fujita, T.; Schwaeble, W.; Weiss, E.H.; Ziegler-Heitbrock, L.; Stover, C.
Stat3 is involved in control of gene expression
Biochem. Biophys. Res. Commun.
364
1022-1025
2007
Homo sapiens, Mus musculus (Q91WP0), Mus musculus, Rattus norvegicus
Iwaki, D.; Kanno, K.; Takahashi, M.; Endo, Y.; Lynch, N.J.; Schwaeble, W.J.; Matsushita, M.; Okabe, M.; Fujita, T.
Small mannose-binding lectin-associated protein plays a regulatory role in the lectin complement pathway
J. Immunol.
177
8626-8632
2006
Mus musculus
Asgari, E.; Farrar, C.; Lynch, N.; Ali, Y.; Roscher, S.; Stover, C.; Zhou, W.; Schwaeble, W.; Sacks, S.
Mannan-binding lectin-associated serine protease 2 is critical for the development of renal ischemia reperfusion injury and mediates tissue injury in the absence of complement C4
FASEB J.
28
3996-4003
2014
Mus musculus (Q91WP0), Mus musculus
Oroszlan, G.; Kortvely, E.; Szakacs, D.; Kocsis, A.; Dammeier, S.; Zeck, A.; Ueffing, M.; Zavodszky, P.; Pal, G.; Gal, P.; Dobo, J.
MASP-1 and MASP-2 do not activate pro-factor D in resting human blood, whereas MASP-3 is a potential activator kinetic analysis involving specific MASP-1 and MASP-2 inhibitors
J. Immunol.
196
857-865
2016
Mus musculus (Q91WP0)
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