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ADAMTS9 propeptide + H2O
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the intact zymogen is secreted to the cell surface and is subsequently processed by furin before release into thge medium. ADAMTS9 processing is exclusively extracellular and occurs at the cell surface in cells that express high levels of furin
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DSSARIRRNAKG + H2O
DSSARIRR + NAKG
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peptide derived bone morphogenetic protein BMP10, cleavage occurs at residue R316
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factor IX + H2O
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feline foamy virus Env glycoprotein precursor + H2O
mature feline foamy virus leader protein Elp + SU protein + TM protein
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full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
G-protein-coupled receptor GPR107 + H2O
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cleavage by endoprotease furin, a disulfide bond connects the two resulting fragments, overview
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HIV-1 Tat protein + H2O
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furin processing is a likely mechanism for inactivating extracellular HIV-1 Tat protein. Furin cleavage reduces the transactivation activity of tat without preventing Tat uptake and entry into the nucleus
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human semaphorin 3F + H2O
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furin processing of semaphorin 3F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin, overview
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IBV spike protein + H2O
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insulin-like growth factor-1 receptor + H2O
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furin-like proprotein convertase activates insulin-like growth factor-1 receptor in vascular smooth muscle cell
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membrane type-1 matrix metalloproteinase proenzyme + H2O
membrane type-1 matrix metalloproteinase + propeptide of membrane type-1 matrix metalloproteinase
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intracellular processing in breast carcinoma MCF-MT1-E240A-FLAG cells
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membrane-tethered membrane type-1 matrix metallo-proteinase + H2O
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furin regulates the intracellular activation and the uptake rate of cell surface-associated MT1-MMP at the surface of cancer cells. Furin and related PCs are the essential components of the specialized cellular machinery that controls the levels of the functionally active, mature, MT1-MMP enzyme on the cell surface to continually support the potency of pericellular proteolysis
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Moloney murine leukemia virus Env precursor protein + H2O
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mouse pro-growth hormone-releasing hormone + H2O
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production of mature growth hormone-releasing hormone from pro-growth hormone-releasing hormone is a stepwise process mediated predomionantly by furin at the N-terminal cleavage site followed by PC1/3 at the C terminus
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PA83 + H2O
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a protective antigen
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precursor of transforming growth factor beta + H2O
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pro-ADAMTS4 + H2O
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furin plays an important role in the intracellular removal of ADAMTS4 prodomain. Multiple furin recognition sites: 206RPRR209, 209RAKR212, or 211KR212
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pro-B-type natriuretic peptide + H2O
B-type natriuretic peptide + pro-peptide of B-type natriuretic peptide
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activation by N-terminal fragment cleavage of proBNP in human plasma through furin
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pro-BMP4 + H2O
BMP4 + propeptide of BMP4
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pro-BMP4 is initially cleaved at a site adjacent to the mature ligand domain (S1) and then at an upstream site (S2) within the prodomain. Cleavage at the S2 site, which appears to occur in a tissue-specific fashion, regulates the activity and signaling range of mature BMP4. In Xenopus oocytes, furin and PC6 function redundantly to cleave both the S1 and S2 sites of pro-BMP4
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pro-bone morphogenetic protein-4 + H2O
mature bone morphogenetic protein-4 + ?
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pro-brain-derived neurotrophic factor + H2O
mature brain-derived neurotrophic factor + ?
pro-CD109 + H2O
CD109 + CD109 propeptide
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CD109 is produced as a 205 kDa glycoprotein, which is then processed in the Golgi apparatus into 180 kDa and 25 kDa proteins by furin
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pro-Notch1 + H2O
Notch1 + propeptide
pro-transforming growth factor-beta1 + H2O
transforming growth factor-beta1 + propeptide
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proform tissue growth factor 1beta + H2O
tissue growth factor beta1 + propeptide
proprotein convertase PCSK9 + H2O
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PCSK9 is inactivated by furin by cleavage at residue R218. PCSK9 mutants R218S and F216L show a 50% reduction in the levels of the inactivated form
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type 1 IGF receptor + H2O
mature type I IDF receptor + ?
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type 1 IGF receptor pro-form + H2O
mature type I IDF receptor + ?
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additional information
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full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
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i.e. (P)RR, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A. The soluble form of the (pro)renin receptor generated through intracellular cleavage by furin is secreted in plasma
i.e. s(P)RR, a 28 kDa protein
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full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
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i.e. (P)RR, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A. The soluble form of the (pro)renin receptor generated through intracellular cleavage by furin is secreted in plasma
i.e. s(P)RR, a 28 kDa protein
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full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
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i.e. (P)RR, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A. The soluble form of the (pro)renin receptor generated through intracellular cleavage by furin is secreted in plasma
i.e. s(P)RR, a 28 kDa protein
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precursor of transforming growth factor beta + H2O
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precursor of transforming growth factor beta requires cleavage by furin for its activation
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precursor of transforming growth factor beta + H2O
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precursor of transforming growth factor beta requires cleavage by furin for its activation
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pro-brain-derived neurotrophic factor + H2O
mature brain-derived neurotrophic factor + ?
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pro-brain-derived neurotrophic factor + H2O
mature brain-derived neurotrophic factor + ?
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pro-Notch1 + H2O
Notch1 + propeptide
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pro-Notch1 + H2O
Notch1 + propeptide
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proform tissue growth factor 1beta + H2O
tissue growth factor beta1 + propeptide
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proform tissue growth factor 1beta + H2O
tissue growth factor beta1 + propeptide
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additional information
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viruses can be activated by furin
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additional information
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processing of viral glycoproteins
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additional information
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prohormone convertases specificities for prohormone cleavage, overview
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additional information
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prohormone convertases specificities for prohormone cleavage, overview
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additional information
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the potential cleavage site delineating the pro-domain, Arg102-Xaa-Lys-Arg, is remarkably conserved among different species and is preceded by two preserved Gln residues located in positions 96 and 97
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additional information
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viruses can be activated by furin
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additional information
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endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway
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additional information
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probably involved in the proteolysis resulting in secretion of rat endopeptidase 24.18 alpha-subunit
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additional information
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possible role in processing essential cellular factors
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additional information
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processing of viral glycoproteins
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additional information
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implicated in maturation of substrates involved in development, signaling, coagulation, and pathogenesis, constitutive secretory pathway
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additional information
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proteolytic processing of a variety of proteins in the exocytic and endocytic pathways
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additional information
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furin possesses a strong preference for substrates containing the multibasic cleavage motif Arg-X-Arg/Lys-ArgV-X
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additional information
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the bioluminescence emission in the presence of firefly luciferase, recombinantly expressed as GFP-tagged enzyme in human MDA-MB-468 cells, breast adenocarcinoma cells, is furin-dependent and specific
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additional information
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activation mechanism of avian influenza virus H9N2 by furin, overview. Israel810 HA can be cleaved in cells with high levels of furin expression, a mutation that eliminates a glycosylation site in HA1 allows the Israel810 hemagglutinin to gain universal cleavage in cell culture. Influenza virus HA is a complex protein, folded in a tertiary structure. In this situation, accessibility of the cleavage site to proteases becomes as important as the primary sequence itself
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additional information
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activation mechanism of avian influenza virus H9N2 by furin, overview. Israel810 HA can be cleaved in cells with high levels of furin expression, a mutation that eliminates a glycosylation site in HA1 allows the Israel810 hemagglutinin to gain universal cleavage in cell culture. Influenza virus HA is a complex protein, folded in a tertiary structure. In this situation, accessibility of the cleavage site to proteases becomes as important as the primary sequence itself
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additional information
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proprotein convertases represent highly selective serine proteases that activate their substrates upon proteolytic cleavage
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additional information
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proprotein convertases represent highly selective serine proteases that activate their substrates upon proteolytic cleavage
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additional information
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endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway
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additional information
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role in processing of proenkephalin
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additional information
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proprotein processing activity
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additional information
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the bioluminescence emission in the presence of firefly luciferase is furin-dependent and specific in living mice, overview
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additional information
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probably plays a role in proprotein maturation
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additional information
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plays an important role in posttranslatioal protein processing
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additional information
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plays an important role in posttranslatioal protein processing
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