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3.4.21.109: matriptase

This is an abbreviated version!
For detailed information about matriptase, go to the full flat file.

Word Map on EC 3.4.21.109

Reaction

cleaves various synthetic substrates with Arg or Lys at the P1 position and prefers small side-chain amino acids, such as Ala and Gly, at the P2 position =

Synonyms

Epi/MTP, epithin, epithin/matriptase, influenza virus-activating protease, matriptase, matriptase-1, matriptase-2, matriptase-3, matriptase1, matriptase1a, membrane-type serine protease 1, membrane-type serine protease 1/matripase, membrane-type serine protease-1, membrane-type serine protease1, membrane-type serine proteinase matripase, membrane-type serine proteinase matriptase, More, MT-2, MT-SP-1, MT-SP1, MT-SP1/matripase, MT2, notopleural, prostamin, PRSS14, r-matripase, serine protease matriptase-2, serine protease SNC19/matripase, SNC19, ST-14, ST14, suppression of tumorigenecity 14, suppressor of tumorigenicity 14, suppressor of tumorigenicity 14 protein, suppressor of tumorigenicity-14, TADG-15, TADG15, TMPRSS6, transmembrane serine protease 6, tumor-associated differentially expressed gene-15, tumor-associated type II transmembrane serine protease, type 2 transmembrane serine protease, type II transmembrane protease, type II transmembrane serine protease

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.109 matriptase

Cloned

Cloned on EC 3.4.21.109 - matriptase

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
activated matriptase-3 serine protease domain expressed in insect cells, expression in COS7 cells
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amino acid residues 596 to 855 and 615 to 855, corresponding to the active sites and catalytic domains of the peptide, respectively, are expressed with a N-terminal His tag in Escherichia coli
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amino acids 596-855 are expressed in Escherichia coli cells
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co-expressed Xenopus laevis oocytes and CHO K1 cells
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co-expression of prostasin and HA-tagged matripatse in FT-293 cells
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DNA and amino acid sequence comparison, genetic structure, phylogenetic analysis, regulation of enzyme expression, overview
expresed in COS-1 cells. Wild-type WT-matriptase is detected rarely when expressed alone but co-expression with hepatocyte growth factor activator inhibitor type 1 allowed the detection. Matriptase expression is detected abundantly from the conditioned medium but poorly from a cell membrane-enriched fraction in the co-expression
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expressed as a GFP fusion protein in Madin-Darby canine kidney epithelial cells
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expressed in CHO cells
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expressed in COS-1 cells
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expressed in HEK-MT2 cells
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expressed in Madin-Darby canine kidney cell line as a full-length rat matriptase with Myc-epitope-hexahistidine tag at its carboxyl-terminus
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expressed in mammalian cells as a full-length rat matriptase with Myc-epitope-hexahistidine tag at its carboxyl-terminus
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expression in M17 cell
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expression in MDA-MB-435 breast caner cells
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expression in Pichia pastoris
expression of His-tagged amino acids 596-855 of matriptase in Escherichia coli strain M15
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expression of mutant S805A in BT549 breast cancer cells, expression of truncated wild-type zymogen and mutant G287R, comprising residues 596-855 and consisting of the C-terminal end of the fourth LDLRA domain, the activation domain, and the catalytic domain, in Escherichia coli in inclusion bodies, expression of wild-type enzyme in HEK-293 cells
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expression of the His-tagged matriptase catalytic domain in Escherichia coli strain BL21(DE3) in inclusion bodies
for expression in Drosophila S2 cells
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full-length rat matriptase is expressed with a myc-epitope and a hexahistidine tag at its C-terminus in stably transfected Madin-Darby canine kidney cells
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gene ST14, DNA and amino acid sequence determination and anaylsis
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gene ST14, DNA and amino acid sequence determination and anaylsis, co-expression of matriptase with HAI-1 in basal keratinocytes of mouse epidermis negates the effects of matriptase
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gene ST14, localization at 11q24.3-q25, DNA and amino acid sequence determination and anaylsis, genotyping
gene TMPRSS6, expression of C-terminally c-Myc-tagged wild-type and mutant enzymes in HEK-293 cells
gene TMPRSS6, expression of C-terminally c-Myc-tagged wild-type and truncated mutant enzymes in Hep-G2 cells
into a pEF6-V5-His-TOPO plasmid vector for transfection of human PC-3 and DU-145 cells
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into pQE-vecto and expressed in Escherichia coli M15 strain
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into the vector pcDNA3.1
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into vector pcDNA3.1, expressed in BT549 breast cancer cells
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into vector pcMT-SP1 MycHis and MT-SP1wt, expressed in COS-1 monkey kidney cells
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overexpression in stomach cancer cell line AZ521, Mat-AZ521 cells release an active form of matriptase into culture medium
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overexpression of matriptase-2 in MDA-MB-231 cells
pseudozymogen forms of recombinant matriptase are expressed in Pichia pastoris and in CHO cells
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recombinant expression of c-Myc-tagged enzyme in HEK cells
recombinant human matriptase protease domain is expressed in Escherichia coli and Saccharomyces cerevisiae
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two soluble variants, containing the entire extracellular domains, Tyr81 - Val855, and the catalytic domain, Asp603 - Val855, are produced, the vectors pT7blue2 and pSec-ek-MT-SP1 are used
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using CHO-K1 cells, secreted variants of rat r-matriptase consisting of the entire extracellular domains (Tyr81-Val855) (HL-matriptase) and of the catalytic domain (and its N-terminal spacer region) (Asp603-Val855) (L-matriptase) are produced. They are activated in vitro by r-enteropeptidase
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