Cloned (Comment) | Organism |
---|---|
the MASP-2 catalytic SP-domain is encoded by a single exon, evolutionary aspects, overview | Homo sapiens |
the MASP-2 catalytic SP-domain is encoded by a single exon, evolutionary aspects, overview | Rattus norvegicus |
Crystallization (Comment) | Organism |
---|---|
C-terminal catalytic region of MASP-2, X-ray diffraction structure determination and anaylsis | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
benzyloxycarbonyl-D-Phe-Pro-methoxypropylboroglycinepinanediol ester | - |
Homo sapiens | |
C1-inhibitor | - |
Homo sapiens | |
C1-inhibitor | - |
Rattus norvegicus | |
additional information | MASP-3 might be able to downregulate MASP-2 activity | Homo sapiens | |
additional information | MASP-3 might be able to downregulate MASP-2 activity | Rattus norvegicus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | required for dimerization | Homo sapiens | |
Ca2+ | Ca2+-dependent dimerization, Ca2+ is bound to the distal end of the CUB1 module of MAp19 and of MASP-2 | Homo sapiens | |
Ca2+ | Ca2+-dependent dimerization, Ca2+ is bound to the distal end of the CUB1 module of MAp19 and of MASP-2 | Rattus norvegicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
complement component C2 + H2O | Homo sapiens | - |
? | - |
? | |
complement component C2 + H2O | Rattus norvegicus | - |
? | - |
? | |
complement component C4 + H2O | Homo sapiens | - |
? | - |
? | |
complement component C4 + H2O | Rattus norvegicus | - |
? | - |
? | |
additional information | Homo sapiens | 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 | Rattus norvegicus | 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 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Rattus norvegicus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
no glycoprotein | - |
Homo sapiens |
proteolytic modification | the enzyme performs autoactivation | Rattus norvegicus |
proteolytic modification | the enzyme performs autoactivation, C4 binding to the zymogen stabilizes the activating enzyme, overview | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
complement component C2 + H2O | - |
Homo sapiens | ? | - |
? | |
complement component C2 + H2O | - |
Rattus norvegicus | ? | - |
? | |
complement component C4 + H2O | - |
Homo sapiens | ? | - |
? | |
complement component C4 + H2O | - |
Rattus norvegicus | ? | - |
? | |
additional information | substrate specificity, overview | Rattus norvegicus | ? | - |
? | |
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 | Homo sapiens | ? | - |
? | |
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 | Rattus norvegicus | ? | - |
? | |
additional information | 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 | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Homo sapiens |
dimer | Ca2+-dependent homodimerization, no formation of heterodimers between MASP-2 and MAp19, even though they share the same N-terminal domains | Homo sapiens |
dimer | Ca2+-dependent homodimerization, no formation of heterodimers between MASP-2 and MAp19, eventhough they share the same N-terminal domains | Rattus norvegicus |
More | enzyme structure and domain organization: CUB1 module, EGF module, CUB2 module, CCP1, CCP2, and serine protease domains, overview | Rattus norvegicus |
More | enzyme structure and domain organization: CUB1 module, EGF module, CUB2 module, CCP1, CCP2, and serine protease domains, the very flexible C-terminal catalytic SP region shows a typical chymotrypsin fold with two six-stranded beta-barrels with the catalytic triad located at the junction of the to barrels and formed by Ser195, His57, and Asp102, active site structure, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
MASP-2 | - |
Homo sapiens |
MASP-2 | - |
Rattus norvegicus |
MASP-2 | protein of the lectin pathway, can autoactivate and cleaves complements C2 and C4 | Homo sapiens |