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(pro)renin receptor + H2O
soluble (pro)renin receptor + ?
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?
2-aminobenzoic acid-Asp-Ile-Tyr-Ile-Ser-Arg-Arg-Leu-Leu-Gly-Thr-Phe-Thr-(3-nitro)Tyr-Ala + H2O
2-aminobenzoic acid-Asp-Ile-Tyr-Ile-Ser-Arg-Arg-Leu-Leu + Gly-Thr-Phe-Thr-(3-nitro)Tyr-Ala
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cleaves between Leu and Gly
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?
2-aminobenzoic acid-Asp-Ile-Tyr-Ile-Ser-Arg-Arg-Leu-Leu-Gly-Thr-Phe-Thr-3-nitrotyrosyl-Ala-CONH2 + H2O
2-aminobenzoic acid-Asp-Ile-Tyr-Ile-Ser-Arg-Arg-Leu-Leu + Gly-Thr-Phe-Thr-3-nitrotyrosyl-Ala-CONH2
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?
2-aminobenzoic acid-SSGSRRLLSEESY(NO2)-Ala-NH2 + H2O
?
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?
2-aminobenzoyl-ALVLRKPLFLDSY(NO2)-Ala + H2O
?
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cleaves between Leu and Phe
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?
2-aminobenzoyl-Arg-Asn-Thr-Pro-Arg-Arg-Glu-Arg-Arg-Arg-Lys-Lys-Arg-Gly-Leu-(3-nitro)Tyr-Ala + H2O
2-aminobenzoyl-Arg-Asn-Thr-Pro-Arg-Arg-Glu-Arg-Arg-Arg-Lys-Lys-Arg-Gly-Leu + (3-nitro)Tyr-Ala
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cleaves between Leu and 3-nitrotyrosine
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?
2-aminobenzoyl-Arg-His-Ser-Ser-Arg-Arg-Leu-Leu-Arg-Ala-Ile-(3-nitro)Tyr-Ala + H2O
2-aminobenzoyl-Arg-His-Ser-Ser-Arg-Arg-Leu-Leu + Arg-Ala-Ile-(3-nitro)Tyr-Ala
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cleaves between Leu and Arg
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?
2-aminobenzoyl-Arg-Ser-Leu-Lys-Tyr-Ala-Glu-Ser-Asp-(3-nitro)-Tyr-Ala + H2O
2-aminobenzoyl-Arg-Ser-Leu-Lys + Tyr-Ala-Glu-Ser-Asp-(3-nitro)-Tyr-Ala
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cleaves between Lys and Tyr
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?
2-aminobenzoyl-Ser-Arg-Arg-Leu-Leu-Arg-Ala-Leu-Glu-(3-nitro)Tyr-Ala + H2O
2-aminobenzoyl-Ser-Arg-Arg-Leu-Leu + Arg-Ala-Leu-Glu-(3-nitro)Tyr-Ala
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cleaves between Leu and Arg
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?
2-aminobenzoyl-SSGSRRLLSEESY(NO2)-Ala + H2O
?
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cleaves between Leu and Ser
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?
2-aminobenzoyl-Val-Phe-Arg-Ser-Leu-Lys-Tyr-Ala-Glu-Ser-Asp-(3-nitro)Tyr-Ala + H2O
2-aminobenzoyl-Val-Phe-Arg-Ser-Leu-Lys + Tyr-Ala-Glu-Ser-Asp-(3-nitro)Tyr-Ala
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cleaves between Lys and Tyr
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?
Abz-Asp-Ile-Tyr-Ile-Ser-Arg-Arg-Leu-Leu-Gly-Thr-Phe-Thr-(3-nitro)Tyr-Ala-CONH2 + H2O
Abz-Asp-Ile-Tyr-Ile-Ser-Arg-Arg-Leu-Leu + Gly-Thr-Phe-Thr-(3-nitro)Tyr-Ala-CONH2
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i.e. QPC251-263
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?
Abz-Asp-Ile-Tyr-Ile-Ser-Arg-Arg-Leu-Leu-Gly-Thr-Phe-Thr-(3-nitro)Tyr-Ala-NH2 + H2O
?
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favored quenched fluorogenic substrate
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?
Abz-DIYISRRLL-GTFT-Tyx-A + H2O
Abz-DIYISRRLL + GTFT-Tyx-A
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?
Abz-DIYISRRLLGTFTY(NO2)A + H2O
?
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S1P displays pronounced positive cooperativity with this substrate derived from the viral coat glycoprotein of the lassa virus
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?
Ac-AISRRLL-7-amido-4-methylcoumarin + H2O
Ac-AISRRLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
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?
Ac-Arg-Arg-Leu-Leu-p-nitroanilide + H2O
?
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?
Ac-Arg-Ser-Leu-Lys-p-nitroanilide + H2O
?
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?
Ac-FISRRLL-7-amido-4-methylcoumarin + H2O
Ac-FISRRLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
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?
Ac-IAVGRTLK-7-amido-4-methylcoumarin + H2O
Ac-IAVGRTLK + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
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?
Ac-IYISRRLL-7-amido-4-methylcoumarin + H2O
Ac-IYISRRLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
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?
Ac-Leu-4-methyl-coumaryl-7-amide + H2O
?
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?
Ac-QKSIAVGRTLK-7-amido-4-methylcoumarin + H2O
Ac-QKSIAVGRTLK + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
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?
Ac-RKLL-7-amido-4-methylcoumarin + H2O
Ac-RKLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
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?
Ac-RRLL-7-amido-4-methylcoumarin + H2O
Ac-RRLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
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?
Ac-RRLQ-7-amido-4-methylcoumarin + H2O
Ac-RRLQ + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
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?
Ac-RTLK-7-amido-4-methylcoumarin + H2O
Ac-RTLK + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
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?
Ac-SFITRRLQ-7-amido-4-methylcoumarin + H2O
Ac-SFITRRLQ + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
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?
Ac-VFRSLK-4-methyl-coumaryl-7-amide + H2O
?
Ac-VFRSLK-4-methylcoumarin 7-amide
?
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?
Ac-VFRSLK-7-amido-4-methylcoumarin + H2O
?
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?
Ac-YISRRLL-7-amido-4-methylcoumarin + H2O
Ac-YISRRLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
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?
Ac-YSSVSRKLL-7-amido-4-methylcoumarin + H2O
Ac-YSSVSRKLL + 7-amino-4-methylcoumarin
an arenavirus envelope glycoprotein precursor protein-derived peptide substrate
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?
arenavirus envelope glycoprotein precursor + H2O
?
ATF6 precursor + H2O
nuclear ATF6
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rSt-1 and rSt-2 seem to affect the processing of ATF6 by SKI-1
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?
brain-derived neurotrophic factor precursor + H2O
?
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cleaves at an RGLTLS site between Thr and Ser
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?
CREB4 + H2O
?
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i.e. androgen-induced leucine zipper protein, C-terminal domain of CREB4 somehow confers resistance to cleavage by S1P, which can be released either by removal of the region or physiologically by some regulatory signal
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?
Crimean Congo hemorrhagic fever virus glycoprotein + H2O
?
Crimean Congo hemorrhagic fever virus glycoprotein + H2O
glycoprotein precursor Gn + glycoprotein precursor Gc
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?
Dabcyl-Arg-His-Ser-Ser-Arg-Arg-Leu-Leu-Arg-Ala-Leu-Glu-Gly-Gly-Lys(tetramethylrhodamine)-OH + H2O
?
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?
Dabcyl-Ser-Gly-Ser-Gly-Arg-Ser-Val-Leu-Ser-Phe-Glu-Ser-Gly-Ser-Lys(tetramethylrhodamine)-Arg-OH + H2O
?
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?
glycoprotein + H2O
?
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S1P is involved in the processing of the glycoproteins of the genetically more-distant South American hemorrhagic fever viruses Guanarito, Machupo, and Junin
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?
glycoprotein precursor Gc + H2O
?
glycoprotein precursor Gn + H2O
?
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?
Lassa virus envelope glycoprotein precursor + H2O
?
the enzyme recognition motif RRLL is critical for the processing of the Lassa virus envelope glycoprotein in the endoplasmic reticulum/cis-Golgi compartment
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?
Lassa virus glycoprotein + H2O
?
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cleavage at RRLL-sites
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?
Lassa virus glycoprotein precursor GP-C + H2O
Lassa virus glycoprotein GP-2 + ?
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cleavage at the C-terminal end of the recognition motif R-R-L-L
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?
Lassa virus glycoprotein precursor protein + H2O
peripheral virion attachment protein GP1 + fusion-active transmembrane protein GP2
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Arg-Arg-Leu-Leu + Gly-Thr-Phe
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?
lymphocytic choriomeningitis virus glycoprotein precursor protein + H2O
peripheral virion attachment protein GP1 + fusion-active transmembrane protein GP2
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Arg-Arg-Leu-Ala + Gly-Thr-Phe
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?
membrane-associated transcription factor bZIP28 + H2O
?
sterol regulatory element-binding protein + H2O
?
sterol regulatory element-binding protein SREBP-2 + H2O
?
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?
succinyl-YISRRLL-7-amido-4-methylcoumarin + H2O
succinyl-YISRRLL + 7-amino-4-methylcoumarin
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?
additional information
?
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Ac-VFRSLK-4-methyl-coumaryl-7-amide + H2O
?
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?
Ac-VFRSLK-4-methyl-coumaryl-7-amide + H2O
?
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?
arenavirus envelope glycoprotein precursor + H2O
?
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?
arenavirus envelope glycoprotein precursor + H2O
?
activation, F259A replacement at P7 of the viral protein substrate impaires the reaction, while replacement of with F does not affect enzyme processing. The catalytic pocket of the enzyme may interact with additional substrate residues distal from the actual cleavage site. Residue Y285 of the enzyme, located distal from the catalytic triad, is implicated in the molecular recognition of the aromatic signature residue at P7 and is crucial for efficient processing of OW and clade C NW arenavirus glycoprotein precursor
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?
arenavirus envelope glycoprotein precursor + H2O
?
activation/maturation
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?
ATF6 + H2O
?
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i.e. activating transcription factor 6
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?
ATF6 + H2O
?
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i.e. activating transcription factor 6
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?
Crimean Congo hemorrhagic fever virus glycoprotein + H2O
?
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cleavage at RRLL-sites
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?
Crimean Congo hemorrhagic fever virus glycoprotein + H2O
?
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posttranslational cleavage by furin/PC-mediated processing at its N-terminus at RSKR247 and by SKI-1 at its C-terminus at RRLL519
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?
glycoprotein precursor Gc + H2O
?
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?
glycoprotein precursor Gc + H2O
?
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?
membrane-associated transcription factor bZIP28 + H2O
?
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?
membrane-associated transcription factor bZIP28 + H2O
?
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endoplasmic reticulum stress-induced activation, the RRIL573 site, but not the RVLM373 site, on the lumen-facing domain of bZIP28 is critical for the biological function of bZIP28 under endoplasmic reticulum stress condition
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?
RsiW + H2O
?
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PrsW is both necessary and sufficient for site-1 cleavage of the anti-sigmaW factor RsiW. Site-2 cleavage depends on the prior action of PrsW
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?
RsiW + H2O
?
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site-1 proteolysis of RsiW. Is converted to a C-terminally truncated form that remains membrane bound
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?
RsiW + H2O
?
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PrsW is both necessary and sufficient for site-1 cleavage of the anti-sigmaW factor RsiW. Site-2 cleavage depends on the prior action of PrsW
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?
sterol regulatory element-binding protein + H2O
?
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SREBP
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?
sterol regulatory element-binding protein + H2O
?
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SREBP, cleaves the luminal loop following the tetrapeptide sequence Arg-Xaa-Xaa-Leu
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?
sterol regulatory element-binding protein + H2O
?
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mutating the crucial Arg at position 486 to Ala blocks cleavage by dS1P
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?
sterol regulatory element-binding protein + H2O
?
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S1P cleaves in the luminal loop of the membrane-bound SREBP precursor, cutting it in two. The NH2- and COOH-terminal domains remain membrane bound owing to their single membrane-spanning helices
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?
sterol regulatory element-binding protein + H2O
?
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SREBP
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?
sterol regulatory element-binding protein + H2O
?
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?
additional information
?
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initiates a process by which the transcriptionally active N-terminal fragments of SREBPs are released from membranes
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?
additional information
?
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initiates a process by which the active fragments of the SREBPs translocate to the nucleus and activate genes controlling the synthesis and uptake of cholersterol and unsaturated fatty acids in animal cells
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?
additional information
?
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peptides containing RSLK and RRLL are cleaved best
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?
additional information
?
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RRLL peptide representing the Gn processing site is efficiently cleaves but an RKPL peptide representing the GC processing site is cleaved at negligible levels
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?
additional information
?
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SKI-1 cleaves inactive proproteins at the motif R-X-(hydrophobic)-Z with Z being mostly Leu
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?
additional information
?
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the enzyme performs autocatalytic cleavage and activation. The cleavage of arenavirus glycoproteins, but not cellular substrates, critically depends on the autoprocessing of the enzyme, suggesting differences in the processing of cellular and viral substrates. The exogenous soluble enzyme is unable to process arenavirus lymphocytic choriomeningitis virus and pathogenic Lassa virus envelope glycoproteins displayed at the surface of enzyme-deficient cells, indicating that glycoprotein processing occurs in an intracellular compartment
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?
additional information
?
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zymogen activation of the enzyme involving sequential autocatalytic processing of its N-terminal prodomain at sites B'/B followed by the C'/C sites. Enzyme autoprocessing results in intermediates whose catalytic domain remains associated with prodomain fragments of different lengths. All incompletely matured intermediates of SKI-1/S1P show full catalytic activity toward cellular substrates, whereas optimal cleavage of viral glycoproteins depends on B'/B processing. Incompletely matured forms of SKI-1/S1P further process cellular and viral substrates in distinct subcellular compartments
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?
additional information
?
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substrate specificity and activity of wild-type enzyme and pro-domain mutants towards cellular and viral substrates, construction and evaluation of a cell-based chimeric protein molecular sensor, containing the LASVGPC cleavage site IYISRRLL-/-G, to monitor endogenous enzyme activity, overview
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?
additional information
?
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the SKI-1/S1P recognition site RRLL is present in the enzyme SKI-1/S1P prodomain and Lassa virus envelope glycoprotein precursor , but not in the lymphocytic choriomeningitis virus envelope glycoprotein precursor, it is crucial for the processing of the Lassa virus glycoprotein in the endoplasmic reticulum/cis-Golgi compartment
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?
additional information
?
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cleaves after lysine or leucine rather than arginine
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?
additional information
?
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functions to control lipid biosynthesis and uptake in animal cells
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?
additional information
?
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can cleave postsingle and possibly pairs of Thr residues in certain precursors
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?