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glycoprotein
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the enzyme contains N-glycosylation sites, overview
glycoprotein
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the enzyme contains N-glycosylation sites, overview
glycoprotein
3 potential N-glycosylation sites
glycoprotein
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matriptase contains four functional N-glycosylation sites, Asn109, 302, 485, and 772, whereas the inactivation of Asn109 and Asn485 has no effect on the activation of matriptase, glycosylation of the first CUB domain, Asn302, and the catalytic domain, Asn772, is required for zymogen activation in cultured breast cancer cells
glycoprotein
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prolonged stabilization of matriptase by GnT-V-mediated glycosylation in vivo, thus extending its half-life and permitting it to play role in the early phases of papillary carcinoma, but not in its later phase progression, overview
glycoprotein
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putative N-linked glycosylation sites, overview
glycoprotein
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the enzyme contains N-glycosylation sites, overview
glycoprotein
sea urchin sperm protein, enteropeptidase, and agrin (SEA) domain is O-glycosylated
glycoprotein
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the enzyme contains N-glycosylation sites, overview
glycoprotein
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N-glycosylated
glycoprotein
the enzyme contains N-glycosylation sites, overview
glycoprotein
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sea urchin sperm protein, enteropeptidase, and agrin (SEA) domain is O-glycosylated
glycoprotein
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the enzyme contains N-glycosylation sites, overview
glycoprotein
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catalytic domain is N-glycosylated at Asn772
proteolytic modification
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proteolytic modification
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one-chain zymogen is converted to an active two-chain protease, enzyme with mutation in its catalytic triad is unable to undergo this activational cleavage
proteolytic modification
zymogen is activated by proteolytic cleavage
proteolytic modification
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activation of the matriptase zymogen requires sequential N-terminal cleavage, activation site autocleavage, and transient association with HAI-1, the mature single-chain proenzyme is first cleaved after Gly149 located in a conserved GSVIA motif in the N-terminal SEA domain by an unknown proteolytic activity or possibly by nonenzymatic hydrolysis of the dependent on SEA domain cleavage, matriptase next is converted into its active conformation by proteolytic cleavage after Arg614 within the highly conserved activation cleavage site R-VVGG in the serine protease domain
proteolytic modification
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autocatalytic cleavage from the zymogen to the active form, autocatalytic activation cleavage at Arg614, and processing at the Gly149 site after which the enzyme remains associated with the membrane, the recombinant refolded truncated wild-type zymogen is capable to autoactivate, overview
proteolytic modification
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matriptase is activated by cleavage at the activation sequence RQAR-/-V
proteolytic modification
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matriptase performs autoactivation
proteolytic modification
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MT-SP1 is activated by cleavage at Arg614 with the catalytic domain remaining attached to the upstream domains via a disulfide bond, the activation cleavage sequence of MT-SP1 is RXQXAXRXXV, MT-SP1 is able to autoactivate both in solution in the membrane-bound form
proteolytic modification
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proteolytic processing during maturation, activation, and shedding, molecular mechanism of zymogen activation and autoactivation, cleavage at Gly149 within the SEA domain, overview, the level of HAI-1 expression seems to be an important factor in the regulation of matriptase zymogen activation, matriptase zymogen activation may be regulated by two independent mechanisms: a soluble, cytosolic suppressor and autonomous, lipid anchored activation machinery at the lipid bilayer biomembrane
proteolytic modification
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matriptase is synthesized as a zymogen and undergoes autoactivation to become an active protease
proteolytic modification
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matriptase is synthesized as a zymogen and undergoes autoactivation to become an active protease that is immediately inhibited by, and forms complexes with, hepatocyte growth factor activator inhibitor (HAI-1)
proteolytic modification
the 811-amino-acid human protein is synthesized as an inactive zymogen and autoactivated by proteolytic cleavage
proteolytic modification
Matriptase is expressed in epithelial cells as a zymogen and needs to be activated. It undergoes spontaneous hydrolysis of a peptide bond at the Gly149 in the SEA domain. The protease is then autocatalytically processed and activated through cleavage at Arg614 within the RQAR614-VVGG activation sequence. Matriptase-2 is exclusively expressed in the liver initially under zymogen form. Matriptase-2 undergoes autocatalysis at Arg576 within the PSSR576-IVGG sequence located in the consensus activation site of its pro-domain
proteolytic modification
the enzyme performs autocatalytic activation
proteolytic modification
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the matriptase zymogen performs its own activation via autoproteolysis, also mutants S805A-matriptase and G827R-matriptase are readily cleaved to the two-chain form by recombinant matriptase
proteolytic modification
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matriptase is activated by cleavage at the activation sequence RQAR-/-V
proteolytic modification
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matriptase performs autoactivation
proteolytic modification
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the 811-amino-acid human protein is synthesized as an inactive zymogen and autoactivated by proteolytic cleavage
proteolytic modification
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matriptase zymogen is capable of auto-activation and proteolytic auotprocesses into an active protease. In order to become catalytically active, matriptase must undergo two sequential proteolytic processing events that occur near the termini of the stem region. The first cleavage occurs after Gly149 within a conserved GSVIA motif in the SEA domain and may occur spontaneously during intracellular transport as the result of conformation-induced hydrolysis. The second cleavage occurs after Arg614 within the highly conserved RVVGG activation motif and requires both the initial SEA domain cleavage event and the catalytic amino acids of the matriptase serine protease domain. Matriptase activation appears to require physical interaction with its related inhibitor, HAI-1, which may serve to protect against aberrant matriptase proteolysis
proteolytic modification
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proteolytic modification
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enzyme is post-translationally processed by cleavage between Gly149 and Ser150
proteolytic modification
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matriptase is first synthesized as a zymogen comprising 855 amino-acid residues, which requires processing by cleavage between Arg614 and Val615 (activation cleavage) to generate the disulfide-linked-two-chain fully active enzyme. In vivo activation of matriptase occurs via a mechanism involving the activity of zymogen
proteolytic modification
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matriptase is post-translationally processed by cleavage with unknown proteases between Gly149 and Ser150 within the sea-urchin sperm protein-enterokinase-agrin (SEA) domain
proteolytic modification
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matriptase is post-translationally processed via cleavage after Gly149. The N-terminal fragment part occurs on the basolateral side but poorly on the apical siden when expresssed in Madin-Darby canine kidney cells. Matriptase C-terminal fragment molecules are delivered to both the apical and the basolateral side of Madin-Darby canine kidney cells
proteolytic modification
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matriptase is processed post-translationally via cleavage between Gly149 and Ser150, the C-terminal fragment Ser150-Val855 is released from the cell surface
proteolytic modification
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matriptase is processed post-translationally via cleavage between Gly149 and Ser150. The C-terminal fragment Ser150-Val855 occurs abundantly in the conditioned medium
proteolytic modification
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matriptase is processed post-translationally via cleavage with an unknown intracellular processing enzyme after Gly149 within the SEA domain and that the C-terminal part (Ser150-Val855) is associated with cell membranes via anchoring with the N-terminal part