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2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM + H2O
?
2-aminobenzoyl-KSKTKC(farnesyl)dinitrophenyldiaminopropionic acid-IM + H2O
2-aminobenzoyl-KSKTKC(farnesyl) + dinitrophenyldiaminopropionic acid-IM
-
34% of activity with KSKTKC(farnesyl)VIM
-
?
2-aminobenzoyl-KSKTKC(farnesyl)lysine-epsilon-dinitrophenyl-IM + H2O
2-aminobenzoyl-KSKTKC(farnesyl) + lysine-epsilon-dinitrophenyl-IM
-
50% of activity with KSKTKC(farnesyl)VIM
-
?
2-aminobenzoyl-KSKTKC(farnesyl)QLIM + H2O
?
-
cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)
-
-
?
2-aminobenzoyl-KSKTKC(farnesyl)VI + H2O
?
-
-
-
-
?
2-aminobenzoyl-KSKTKC(farnesyl)VI-dinitrophenyldiaminopropionic acid + H2O
2-aminobenzoyl-KSKTKC(farnesyl) + VI-dinitrophenyldiaminopropionic acid
-
4.8% of activity with KSKTKC(farnesyl)VIM
-
?
2-aminobenzoyl-KSKTKC(farnesyl)VI-lysine-epsilon-dinitrophenyl + H2O
2-aminobenzoyl-KSKTKC(farnesyl) + VI-lysine-epsilon-dinitrophenyl
-
25% of activity with KSKTKC(farnesyl)VIM
-
?
2-aminobenzoyl-KSKTKC(farnesyl)VIM + H2O
2-aminobenzoyl-KSKTKC(farnesyl) + VIM
-
-
-
?
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)-dinitrophenyldiaminopropionic acid-IM + H2O
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl) + dinitrophenyldiaminopropionic acid-IM
-
2.5% of activity with KSKTKC(farnesyl)VIM
-
?
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)-VI-dinitrophenyldiaminopropionic acid + H2O
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl) + VI-dinitrophenyldiaminopropionic acid
-
1% of activity with KSKTKC(farnesyl)VIM
-
?
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)lysine-epsilon-dinitrophenyl + H2O
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl) + lysine-epsilon-dinitrophenyl-IM
-
-
-
?
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)VI-lysine-epsilon-dinitrophenyl + H2O
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl) + VI-lysine-epsilon-dinitrophenyl
-
2% of activity with KSKTKC(farnesyl)VIM
-
?
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl)VIM + H2O
7-methoxycoumarin-4-acetyl-KSKTKC(farnesyl) + VIM
-
35% of activity with KSKTKC(farnesyl)VIM
-
?
a-factor + H2O
fragments of a-factor
-
-
-
?
a-factor derived synthetic farnesylated pentadecapeptide + H2O
?
-
-
-
-
?
a-factor-CaaX + H2O
a-factor-C + aaX
ABZ-KSKTKC(S-farnesyl)-K(Dnp)-IM + H2O
?
-
-
-
?
Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E)-4-[(3-benzoylbenzyl)oxy]-3-methylbut-2-en-1-yl]-L-Cys-N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met + H2O
Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E)-4-[(3-benzoylbenzyl)oxy]-3-methylbut-2-en-1-yl]-L-Cys + N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met
-
i.e. 2-aminobenzoyl-KSKTKC(3-methylbenzophenone prenyl ether)K(dinitrophenyl)IM, an aryl ketone-containing peptide photophore, incorporating a benzophenone-modified isoprenoid, synthesis and structure, mass spectrometrical analysis, overview
mass spectrometrical product analysis
-
?
Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-L-Cys-N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met + H2O
Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-L-Cys + N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met
-
the isoprenylated peptide substrate is derived from the C-terminal sequence of mammalian K-Ras4B, synthesized from 2-aminobenzoyl-KSKTKCK(dinitrophenyl)IM, synthesis and structure, mass spectrometrical analysis, overview
mass spectrometrical product analysis
-
?
dansyl-G(farnesyl)CIIS + H2O
dansyl-G(farnesyl)C + IIS
-
-
-
?
dansyl-GLP(farnesyl)CVVM + H2O
dansyl-GLP(farnesyl)C + VVM
-
-
-
?
dansyl-KTK(farnesyl)CVIM + H2O
dansyl-KTK(farnesyl)C + VIM
-
-
-
?
dansyl-SAK(farnesyl)CVLS + H2O
dansyl-SAK(farnesyl)C + VLS
-
-
-
?
dansyl-WDPA(farnesyl)CVIA + H2O
dansyl-WDPA(farnesyl)C + VIA
-
-
-
?
dansyl-WDPA(geranylgeranyl)CVIA + H2O
dansyl-WDPA(geranylgeranyl)C + VIA
-
-
-
?
farnesyl-Ha-Ras-CaaX + H2O
farnesyl-Ha-Ras-C + aaX
-
-
?
farnesyl-Ki-Ras-CaaX + H2O
farnesyl-Ki-Ras-C + aaX
specific for prenylated proteins containing a C-terminal CaaX motif
-
?
farnesyl-N-Ras-CaaX + H2O
farnesyl-N-Ras-C + aaX
-
-
?
G-gamma1-CaaX + H2O
G-gamma1-C + aaX
-
-
?
geranylgeranyl-Ki-Ras-CaaX + H2O
geranylgeranyl-Ki-Ras-C + aaX
-
-
?
geranylgeranyl-Rab1b-CaaX + H2O
geranylgeranyl-Rab1b-C + aaX
-
-
?
K-Ras(farnesyl)VIM + H2O
K-Ras(farnesyl) + VIM
-
-
-
?
KSKTKC(farnesyl)VI + H2O
?
-
a better substrate for hRCE1 than a KSKTKC(f)VIM
-
-
?
KSKTKC(farnesyl)VIM + H2O
KSKTKC(farnesyl) + VIM
-
no activity with unfarnesylated peptides
-
?
KWDPA(farnesyl)CVIA + H2O
KWDPA(farnesyl)C + VIA
-
-
-
?
KWDPAC(S-trans,trans-farnesyl)VIA + H2O
KWDPAC(S-trans,trans-farnesyl) + VIA
-
-
-
?
N-acetyl-S-farnesyl-Cys-Val-Ile-Ser + H2O
N-acetyl-S-farnesyl-Cys + Val-Ile-Ser
-
-
-
-
?
N-Boc-S-farnesyl-L-Cys-Val-Ile-Met + H2O
N-Boc-S-farnesyl-L-Cys + Val-Ile-Met
-
-
-
-
?
phosphodiesterase 6 + H2O
?
-
-
-
?
Ras + H2O
fragments of Ras
-
-
-
?
Ras-CaaX + H2O
Ras-C + aaX
-
a stands for aliphatic amino acid, X is any amino acid
-
?
Ras2 + H2O
Ras2-C + aaX
-
a stands for aliphatic amino acid, X is any amino acid
-
?
small GTPase RalA + H2O
?
-
-
-
?
small GTPase RalB + H2O
?
-
-
-
?
YIIKGVFWDPAC(farnesyl)-VIA + H2O
a-factor + ?
-
-
-
-
?
additional information
?
-
2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM + H2O
?
-
cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (aminobenzoylZ-KSKTKC(farnesyl)-K(Dnp)-IM)
-
-
?
2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM + H2O
?
-
cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (ABZ-KSKTKC(farnesyl)QLIM)
-
-
?
a-factor-CaaX + H2O
a-factor-C + aaX
-
endoproteolytic removal of the last three amino acids by Rce1 (i.e, -aaX)
-
-
?
a-factor-CaaX + H2O
a-factor-C + aaX
-
-
-
-
?
a-factor-CaaX + H2O
a-factor-C + aaX
-
CaaX proteolysis of all three forms of Ras and other CaaX proteins is absent in RCE1 deficient mice, RCE1 is required for correct localization of these proteins
-
-
?
a-factor-CaaX + H2O
a-factor-C + aaX
-
-
-
-
?
a-factor-CaaX + H2O
a-factor-C + aaX
-
a stands for aliphatic amino acid, X is any amino acid
-
?
a-factor-CaaX + H2O
a-factor-C + aaX
-
a stands for aliphatic amino acid, X is any amino acid
-
?
a-factor-CaaX + H2O
a-factor-C + aaX
-
removal of the last three amino acids of carboxyl-terminal sequence motif CaaX, enzyme proteolyzes a-factor with A, V, L, I, C or M at the a1 position, V, L, I, C or M at the a2 position or any amino acid at the X position
-
?
CALM + H2O
?
-
-
-
-
?
CALQ + H2O
?
-
-
-
-
?
CAMQ + H2O
?
-
-
-
-
?
CASQ + H2O
?
-
no cleavage when RCE1 is expressed from low copy plasmids or is overexpressed
-
-
?
CASQ + H2O
?
-
no cleavage when RCE1 is expressed from low copy plasmids or is overexpressed
-
-
?
CASQ + H2O
?
-
no cleavage when RCE1 is expressed from low copy plasmids, but overexpressed RCE1 appears to have marginal activity towards CASQ
-
-
?
CSVM + H2O
?
-
-
-
-
?
CTLM + H2O
?
-
one of the preferred CAAX motifs, when RCE1 is expressed from low copy plasmids or is overexpressed
-
-
?
CTLM + H2O
?
-
one of the preferred CAAX motifs, when RCE1 is expressed from low copy plasmids or is overexpressed
-
-
?
CTLM + H2O
?
-
one of the preferred CAAX motifs, when RCE1 is expressed from low copy plasmids or is overexpressed
-
-
?
CTSM + H2O
?
-
-
-
-
?
CTVM + H2O
?
-
-
-
-
?
CVIA + H2O
?
-
one of the preferred CAAX motifs, when RCE1 is expressed from low copy plasmids or is overexpressed
-
-
?
CVIA + H2O
?
-
one of the preferred CAAX motifs, when RCE1 is expressed from low copy plasmids or is overexpressed
-
-
?
CVIA + H2O
?
-
one of the preferred CAAX motifs, when RCE1 is expressed from low copy plasmids or is overexpressed
-
-
?
additional information
?
-
-
CTSQ motif poorly cleaved
-
-
?
additional information
?
-
-
the enzyme is responsible for one step in Ras membrane localization
-
-
?
additional information
?
-
-
when hRCE1 activity is examined on the same K-Ras core peptide with H-Ras (VLS) or N-Ras (VVM) C-terminal AAX sequences, in each case, the CAA peptides are better hRCE1 substrates. For each peptide set the P2' (A) and P3' (X) positions appear independent in influencing hRCE1 activity on peptide substrates. The P3' position methionine is better than serine; while at the P2' position, isoleucine and valine are better than leucine
-
-
?
additional information
?
-
-
In MEF cells lacking Rce1, farnesylated Ras proteins are mislocalized, intracellular localizations of geranylated Rho GTPases are not perturbed, RhoGDI binding and actin remodeling is normal in Rce1-deficient cells, swapping geranylgernalytion for farnesylation on Ras proteins or vice versa on Rho proteins reversed the differential sensitivity to Rce1 deficiency
-
-
?
additional information
?
-
-
in the absence of Rce1, splenocytes and bone marrow cells expressing oncogenic KRAS yield more and larger colonies when grown in methylcellulose. The inactivation of Rce1 worsens the myeloproliferative disease caused by oncogenic K-RAS
-
-
?
additional information
?
-
-
CTSQ motif poorly cleaved
-
-
?
additional information
?
-
-
Rce1p proteolysis requires histidine and glutamate residues, sequential analysis of Rce1p identifies invariant residues reminiscent of a consensus HEXXH motif found in metalloproteases
-
-
?
additional information
?
-
-
the Trypanosoma brucei RCE1 ortholog appears to be the dominant prenyl-CaaX protease
-
-
?
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4-(((1-hydroxynaphthalen-2-yl)(phenyl)methyl)amino)benzoic acid
inhibitor causes a reduction in Rce1 in vitro activity, exhibits low cell toxicity, and induces mislocalization of EGFP-Ras from the plasma membrane in human colon carcinoma cells. FTase activity is not inhibited at concentrations as high as 50 microM
4-(((4-bromo-2,6-difluorophenyl)(1-hydroxynaphthalen-2-yl)methyl)amino)benzoic acid
inhibitor causes a reduction in Rce1 in vitro activity, exhibits low cell toxicity, and induces mislocalization of EGFP-Ras from the plasma membrane in human colon carcinoma cells. FTase activity is not inhibited at concentrations as high as 50 microM
4-(((4-bromophenyl)(1-hydroxynaphthalen-2-yl)methyl)amino)benzoic acid
inhibitor causes a reduction in Rce1 in vitro activity, exhibits low cell toxicity, and induces mislocalization of EGFP-Ras from the plasma membrane in human colon carcinoma cells. FTase activity is not inhibited at concentrations as high as 50 microM
4-(((4-bromophenyl)(8-hydroxyquinolin-7-yl)methyl)amino)benzoate
inhibitor causes a reduction in Rce1 in vitro activity, exhibits low cell toxicity, and induces mislocalization of EGFP-Ras from the plasma membrane in human colon carcinoma cells. FTase activity is not inhibited at concentrations as high as 50 microM
4-(((8-hydroxyquinolin-7-yl)(phenyl)methyl)amino)benzoate
inhibitor causes a reduction in Rce1 in vitro activity, exhibits low cell toxicity, and induces mislocalization of EGFP-Ras from the plasma membrane in human colon carcinoma cells
benzyloxycarbonyl-Phe-Ala-2,4,6-trimethylbenzoyloxymethyl ketone
benzyloxycarbonyl-Phe-Lys-2,4,6-trimethylbenzoyloxymethyl ketone
beta-(2-naphthyl)-Ala-CH2Cl
-
affinity labeling agent of the enzyme
Ca2+
-
0.087 mM, 97% inhibition
Co2+
-
0.087 mM, 48% inhibition
Cu+
-
0.087 mM, 97% inhibition
Mersalyl acid
-
0.022 mM, 99% inhibition
methyl methanothiosulfonate
-
0.05 mM, 40% inhibition
N-Boc-Cys(farnesyl)-methylenamin-VIM-OH
N-Boc-S-farnesyl-L-cys-CH2Cl
-
-
N-Boc-S-farnesyl-L-cysteine aldehyde
-
potent competetive inhibitor
N6-[1-(4,4-dimethyl-2,6-dioxocyclohexylidene)ethyl]-N2-{4,15-dioxo-19-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-8,11,14-trioxa-5-azanonadecan-1-oyl}-L-lysyl-L-lysyl-L-seryl-L-lysyl-L-threonyl-L-lysyl-S-{(2E)-4-[(3-benzoylbenzyl)oxy]-3-methylbut-2-en-1-yl}-L-cysteinyl-N6-{3-[hydroxy(oxo)ammonio]-5-nitrophenyl}-L-lysyl-L-isoleucyl-L-methionine
-
labels the active site by crosslinking to the biotinylated probe, competitive to Abz-L-Lys-L-Ser-L-Lys-L-The-L-Lys-S-[(2E,6E)-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-L-Cys-N6-(3,5-dinitrophenyl)-L-LysL-L-Ile-L-Met
Nalpha-tosyl-L-lysine chloromethyl ketone
-
0.3 mM, 32% inhibition
Nalpha-tosyl-L-phenylalanine chloromethyl ketone
-
0.3 mM, 94% inhibition
Ni2+
-
0.087 mM, 48% inhibition
p-chloromercuribenzoate
-
inactivates the partially purified enzyme, with 0.005 mM substantial inhibition
p-hydroxymercuribenzoic acid
-
0.022 mM, 99% inhibition
p-Hydroxymercuriphenylsulfonic acid
-
0.022 mM, 99% inhibition
pseudo peptide R (CH2-NH)
-
-
-
RPI
farnesyl-peptide analogue, 0.000005 mM, 50% inhibition
Tos-Phe-CH2Cl
-
affinity labeling agent of the enzyme
tosyl-L-lysyl-chloromethylketone
tosyl-L-phenylalanyl-chloromethylketone
USP17
-
USP17 deubiquitinates RCE1 and negatively regulates the activity of RCE1. Constitutive expression of USP17 blocks cell growth and decreases Ras activation, knockdown of USP17 expression results in a marked elevation in the level of GTP-bound Ras. USP17 and RCE1 co-localize at the endoplasmic reticulum
-
benzyloxycarbonyl-Phe-Ala-2,4,6-trimethylbenzoyloxymethyl ketone
-
0.25 mM, 8% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)
benzyloxycarbonyl-Phe-Ala-2,4,6-trimethylbenzoyloxymethyl ketone
-
0.25 mM, 12% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)
benzyloxycarbonyl-Phe-Ala-2,4,6-trimethylbenzoyloxymethyl ketone
-
0.25 mM, 10% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)
benzyloxycarbonyl-Phe-Lys-2,4,6-trimethylbenzoyloxymethyl ketone
-
0.25 mM, 61% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM), inhibition is not readily reversible
benzyloxycarbonyl-Phe-Lys-2,4,6-trimethylbenzoyloxymethyl ketone
-
0.25 mM, 94% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM), inhibition is not readily reversible
benzyloxycarbonyl-Phe-Lys-2,4,6-trimethylbenzoyloxymethyl ketone
-
0.25 mM, 75% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM), inhibition is not readily reversible
N-Boc-Cys(farnesyl)-methylenamin-VIM-OH
-
i.e. isoprenyl protease inhibitor RPI, 0.000058 mM, 50% inhibition
N-Boc-Cys(farnesyl)-methylenamin-VIM-OH
-
0.0001 mM, 50% inhibition
tosyl-L-lysyl-chloromethylketone
-
0.25 mM, 26% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)
tosyl-L-lysyl-chloromethylketone
-
0.25 mM, 54% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobvenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)
tosyl-L-lysyl-chloromethylketone
-
0.25 mM, 12% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)
tosyl-L-phenylalanyl-chloromethylketone
-
0.25 mM, complete inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)
tosyl-L-phenylalanyl-chloromethylketone
-
0.25 mM, 93% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM)
tosyl-L-phenylalanyl-chloromethylketone
-
0.25 mM, 68% inhibition of cleavage of a quenched fluorogenic farnesylated peptide that is based on the C-terminal sequence of the K-Ras4b precursor (2-aminobenzoyl-KSKTKC(farnesyl)-K(Dnp)-IM). No significant inhibition of a-factor production
Zn2+
-
0.087 mM, 99% inhibition
Zn2+
-
at high concentration
additional information
-
not inhibited by chyostatin, DTT, E-64, 1,10-phenanthroline and PMSF, Tos-Lys-CH2Cl
-
additional information
-
not inhibited by protese inhibitors bestatin, antipain, chymostatin, pepstatin A, leupeptin, E64 and PMSF
-
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Hollander, I.; Frommer, E.; Mallon, R.
Human Ras-Converting Enzyme (hRCE1) Endoproteolytic Activity on K-Ras-Derived Peptides
Anal. Biochem.
286
129-137
2000
Homo sapiens
brenda
Dolence, J.M.; Steward, L.E.; Dolence, E.K.; Wong, D.H.; Poulter, C.D.
Studies with Recombinant Saccharomyces cerevisiae CaaX Prenyl Protease Rce1p
Biochemistry
39
4096-4104
2000
Saccharomyces cerevisiae
brenda
Otto, J.C.; Kim, E.; Young, S.G.; Casey, P.J.
Cloning and characterization of a mammalian prenyl protein-specific protease
J. Biol. Chem.
274
8379-8382
1999
Homo sapiens (Q9Y256), Homo sapiens
brenda
Ashby, M.N.; Rine, J.
Ras and a-factor converting enzyme
Methods Enzymol.
250
235-251
1995
Saccharomyces cerevisiae
brenda
Trueblood, C.E.; Boyartchuk, V.L.; Picologlou, E.A.; Rozema, D.; Poulter, C.D.; Rine, J.
The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities
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Homo sapiens (Q9Y256)
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