Inhibitors | Comment | Organism | Structure |
---|---|---|---|
hepatocyte growth factor activator inhibitor-1 | HAI-1 | Homo sapiens | |
L-arginyl-N1-[(2S)-1-[[(2S)-1-(1,3-benzothiazol-2-yl)-5-carbamimidamido-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]-L-glutamamide | EC50 is 0.00564-0.0068 mM, the inhibitor contains a ketobenzothiazole serine trap designed based on matriptase's auto-catalytic domain (RQAR), it is a selective, slow, tight-binding inhibitor of matriptase that significantly reduces viral replication of H1N1 influenza virus, including the 2009 pandemic virus | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell surface | apical surface of epithelial cells | Homo sapiens | 9986 | - |
endosome | membrane-bound form | Homo sapiens | 5768 | - |
extracellular | - |
Homo sapiens | - |
- |
soluble | - |
Homo sapiens | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
influenza A H1 virus hemagglutinin + H2O | Homo sapiens | the soluble form of the protease is able to specifically cleave hemagglutinins from H1 virus, but not from H2 and H3 viruses, in a broad pH range | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9Y5Y6 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
Calu-3 cell | - |
Homo sapiens | - |
epithelial cell | bronchial epithelial cells | Homo sapiens | - |
lung | bronchial epithelium | Homo sapiens | - |
additional information | matriptase co-localizes with hemagglutinin at the apical surface of human epithelial cells and within endosomes. No expression in A-549 cells | Homo sapiens | - |
NCI-H292 cell | - |
Homo sapiens | - |
NHBE cell | primary epithelial cells | Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
influenza A H1 virus hemagglutinin + H2O | the soluble form of the protease is able to specifically cleave hemagglutinins from H1 virus, but not from H2 and H3 viruses, in a broad pH range | Homo sapiens | ? | - |
? | |
additional information | matriptase has an autocatalytic domain, RQAR. At physiological pH, matriptase is capable of cleaving both the H1 (IQSR-/-GLFG) and H3 (KQTR-/-GLFG) consensus cleavage sequences, whereas no cleavage is observed with the H2 (IESRGLFG) consensus sequence. RQRR-/-VVGG is the optimal cleavage sequence of matriptase | Homo sapiens | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
influenza virus-activating protease | - |
Homo sapiens |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5 | 9 | broad pH range, substrate hemagglutinin H1 | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme is a member of the TTSP family | Homo sapiens |
malfunction | siRNA knockdown of matriptase by 80.0% in human bronchial epithelial cells significantly blocks influenza virus replication in these cells | Homo sapiens |
additional information | a three-pronged model for the action of matriptase: activation of incoming viruses in the extracellular space in its shed form, upon viral attachment or exit in its membrane-bound and/or shed forms at the apical surface of epithelial cells, and within endosomes by its membrane-bound form where viral fusion takes place | Homo sapiens |
physiological function | matriptase is a trypsin-like serine protease with specific proteolytic activity downstream of an arginine residue at the cleavage site. Matriptase proteolytically activates influenza virus and promotes multicycle replication in the human airway epithelium. Influenza viruses do not encode any proteases and must rely on host proteases for the proteolytic activation of their surface hemagglutinin proteins in order to fuse with the infected host cells | Homo sapiens |