3.4.21.75: Furin
This is an abbreviated version!
For detailed information about Furin, go to the full flat file.
Word Map on EC 3.4.21.75
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3.4.21.75
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proproteins
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sars-cov-2
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covid-19
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metalloproteinase
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ectodomain
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spike
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endoprotease
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coronavirus
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viruses
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trans-golgi
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disintegrin
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adam17
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ace2
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pandemic
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tmprss2
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neuropeptides
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endosomes
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neuroendocrine
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endoproteolytic
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propeptide
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proinsulin
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zymogen
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prodomain
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mt1-mmp
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virion
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anthrax
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subtilisins
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proglucagon
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proopiomelanocortin
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exotoxin
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uncleaved
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alpha1-antitrypsin
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prorenin
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baffs
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portland
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betacoronavirus
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prostasin
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secretogranin
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alpha-amidating
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juxtamembrane
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pharmacology
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sds-stable
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medicine
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corticotrophs
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polybasic
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prosegment
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monobasic
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drug development
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industry
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mers-cov
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pcsk9
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paramyxoviruses
-
membrane-type
-
subtilase
-
analysis
- 3.4.21.75
- proproteins
- sars-cov-2
- covid-19
- metalloproteinase
- ectodomain
- spike
- endoprotease
- coronavirus
- viruses
-
trans-golgi
-
disintegrin
- adam17
- ace2
- pandemic
- tmprss2
- neuropeptides
- endosomes
-
neuroendocrine
-
endoproteolytic
- propeptide
- proinsulin
- zymogen
- prodomain
- mt1-mmp
- virion
- anthrax
- subtilisins
- proglucagon
- proopiomelanocortin
-
exotoxin
-
uncleaved
- alpha1-antitrypsin
- prorenin
-
baffs
- portland
- betacoronavirus
- prostasin
-
secretogranin
-
alpha-amidating
-
juxtamembrane
- pharmacology
-
sds-stable
- medicine
-
corticotrophs
-
polybasic
- prosegment
-
monobasic
- drug development
- industry
- mers-cov
- pcsk9
- paramyxoviruses
-
membrane-type
-
subtilase
- analysis
Reaction
Release of mature proteins from their proproteins by cleavage of -Arg-Xaa-Yaa-Arg-/- bonds, where Xaa can by any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors =
Synonyms
Bfurin, Dfurin1, Dibasic processing enzyme, FUR, furin, furin A, furin B, furin convertase, furin protease, furin-like pro-protein convertase, furin-like prohormone convertase, furin-like proprotein convertase, furin-like protease, furin-like proteinase, FurinA, furinase, hfurin, KPC-1, More, PACE, Paired basic amino acid cleaving enzyme, Paired basic amino acid converting enzyme, Paired basic amino acid residue cleaving enzyme, PC1, PC1/3, PC2, PCSK3, proconvertase, prohormone convertase, prohormone convertase 1, prohormone convertase 2, Proprotein convertase, proprotein convertase subtilisin/kexin 3, proprotein convertase subtilisin/kexin type 3, proprotein convertase subtilisin/kexin type3, Serine proteinase PACE, Sfurin, sheddase, SPC3, subtilisin-like proprotein convertase, subtilisin-like protein convertase, Trans golgi network protease furin
ECTree
3.4.21.75 FurinAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.21.75 - Furin
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2-Aminobenzoyl)-Lys-Glu-Arg-Ser-Lys-Arg-Ser-Ala-Leu-Arg-Asp-(3-nitro)Tyr-Ala + H2O
(2-Aminobenzoyl)-Lys-Glu-Arg-Ser-Lys-Arg + Ser-Ala-Leu-Arg-Asp-(3-nitro)Tyr-Ala
-
-
-
?
2-amino benzoyl-AEQDRNTREVFAQ-T(3-nitro-tyrosine)-A + H2O
2-amino benzoyl-AEQDRNTR + EVFAQ-T(3-nitro-tyrosine)-A
-
furin-mediated cleavage of a fluorogenic peptide derived from hSARS-CoV spike protein
-
-
?
5-carboxyfluorescein-Gln-Arg-Val-Arg-Arg-Ala-Val-Gly-Ile-Asp-Lys(5-carboxytetramethylrhodamine)-OH + H2O
?
-
-
-
?
Abz-GIRRKRSVSHQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-GIRRKR + SVSHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Rous sarcoma viral envelope glycoprotein
-
-
?
Abz-GRRTRREAIVQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-GRRTRR + EAIVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Ebola Zaire viral envelope glycoprotein
-
-
?
Abz-HHRQRRSVSIQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-HHRQRR + SVSIQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from human A disintegrin and metalloproteinase with thrombospondin ADAM-TS 6
-
-
?
Abz-HKREKRQAKHQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-HKREKR + QAKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from human bone morphogenetic protein hBMP-2
-
-
?
Abz-HRREKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-HRREKR + SVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Dengue 2 viral envelope glycoprotein
-
-
?
Abz-HRRQKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-HRRQKR + SVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Dengue 3 viral envelope glycoprotein
-
-
?
Abz-KIRRRRDVVDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-KIRRRR + DVVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Herpes HHV-6A viral envelope glycoprotein
-
-
?
Abz-LKRRRRDTQQQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-LKRRRR + DTQQQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Borna disease viral envelope glycoprotein
-
-
?
Abz-NLRRRRDLVDQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-NLRRRR + DLVDQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Herpes HHV-6B viral envelope glycoprotein
-
-
?
Abz-RERRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RERRRKKR + GLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from a mutation of the H5N1 influenza hemagglutinin processing site
-
-
?
Abz-RKRSRRQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RKRSRR + QVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Ebola Sudan viral envelope glycoprotein
-
-
?
Abz-RRRAKRSPKHQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRAKR + SPKHQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from human bone morphogenetic protein hBMP-4
-
-
?
Abz-RRRDKRSVALQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRDKR + SVALQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Dengue 4 viral envelope glycoprotein
-
-
?
Abz-RRRKKRGLFGQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRKKR + GLfGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from the H5N1 influenza hemagglutinin processing site
-
-
?
Abz-RRRKKRGLSGQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRKKR + GLSGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from a mutation of the H5N1 influenza hemagglutinin processing site
-
-
?
Abz-RRRKKRSLFGQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-RRRKKR + SLFGQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from a mutation of the H5N1 influenza hemagglutinin processing site
-
-
?
Abz-SKRSRRSVSVQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SKRSRR + SVSVQVNTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Japan beta-encephalitis viral envelope glycoprotein
-
-
?
Abz-SRRHKRFAGVQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SRRHKR + FAGVQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from measle virus Fo viral envelope glycoprotein
-
-
?
Abz-SRRKRRDVTPQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SRRKRR + DVTPQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Ebola Ivory Coast viral envelope glycoprotein
-
-
?
Abz-SRRKRRSASTQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SRRKRR + SASTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from Herpes HHV-8 viral envelope glycoprotein
-
-
?
Abz-SSRHRRALDTQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-SSRHRR + ALDTQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from human transforming growth factor TGF-beta3
-
-
?
Abz-TRRFRRSITEQ-N-(2,4-dinitrophenyl)ethylenediamine + H2O
Abz-TRRFRR + SITEQ-N-(2,4-dinitrophenyl)ethylenediamine
-
FRET-peptide derived from infectious bronchitis viral envelope glycoprotein
-
-
?
Ac-AAKYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-AAKYKR
-
-
-
?
Ac-AARYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-AARYKR
-
-
-
?
Ac-Arg-Val-Arg-Arg-4-nitroanilide + H2O
Ac-Arg-Val-Arg-Arg + 4-nitroaniline
-
-
-
-
?
Ac-KARYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-KARYKR
-
-
-
?
Ac-norleucine-YKR-4-methylcoumarin-7-amide
acetyl-norleucine-YKR + 7-amino-4-methylcoumarin
-
-
-
-
?
Ac-RA-norvaline-YKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RA-norvaline-YKR
-
-
-
?
Ac-RAKYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RAKYKR
-
-
-
?
Ac-RARYAR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RARYAR
-
-
-
?
Ac-RARYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RARYKR
-
-
-
?
Ac-RARYRR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RARYRR
-
-
-
?
Ac-RYKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RYRR
-
-
-
?
Ac-RYRFKR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Ac-RYRFKR
-
-
-
?
acetyl-norleucine-YKR-7-amido-4-methylcoumarin + H2O
acetyl-norleucine-YKR + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-Tyr-Glu-Lys-Glu-Arg-Ser-Lys-7-amido-4-methylcoumarin + H2O
acetyl-Tyr-Glu-Lys-Glu-Arg + Ser-Lys-7-amido-4-methylcoumarin
-
-
-
-
?
Acetyl-Tyr-Glu-Lys-Glu-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
AcRARYKK-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + AcRARYKK
-
-
-
?
Boc-RVRR-4-methylcoumarin 7-amide + H2O
Boc-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
Boc-RVRR-4-methylcoumarin-7-amide + H2O
7-amino-4-methylcoumarin + Boc-RVRR
-
-
-
?
Boc-RVRR-7-amido-4-methylcoumarin + H2O
Boc-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
duck carboxypeptidase D + H2O
?
-
i.e. DCPD, duck carboxypeptidase D acts as species-specific docking receptor for the duck hepatitis B virus. No cleavage of recombinant DCPD expressed in LMH cells
-
-
?
duck hepatitis B virus large envelope pre-S protein + H2O
?
-
the protein needs to be cleaved by duck endosomal furin or furin-like proprotein convertase for duck hepatocyte infection by duck hepatitis B virus
-
-
?
feline foamy virus Env glycoprotein precursor + H2O
mature feline foamy virus leader protein Elp + SU protein + TM protein
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
Glu-Arg-Thr-Lys-Arg-(7-methylcoumarin-4-yl)acetate + H2O
Glu-Arg-Thr-Lys-Arg + (7-methylcoumarin-4-yl)acetate
-
-
-
-
?
hBMP-2 precursor protein + H2O
?
-
cleavage sites are HKREKR-/-QAKH and HVRISR-/-SLHQ
-
-
?
hBMP-4 precursor protein + H2O
?
-
cleavage sites are RRRAKR-/-SPKH and HVRISR-/-SLPQ
-
-
?
hemagglutinin high pathogenic avian influenza virus subtype H5 + H2O
?
-
hemagglutinin loop of high pathogenic avian influenza virus subtype H5 binds much more tightly into the catalytic site of furin than the hemagglutinin low pathogenic avian influenza virus subtype H3 and hemagglutinin low pathogenic avian influenza virus subtype H5 systems. The -RRRKK- insertion in the hemagglutinin high pathogenic avian influenza virus subtype H5 in particular two arginines at S4 and S6 positions helps directly to hold the hemagglutinins cleavage loop in place by forming many strong hydrogen bonds between residues of hemagglutinin and furin
-
-
?
heparan sulfate 6-O-endosufatase Sulf2 + H2O
?
-
cleavage at arginine 570, located in the consensus sequence for the cleavage by furin-type proprotein convertases. The consensus sequence of the cleavage by furin and PCs is R/K-X-R/K-X-R/K-R-/-X. R, K, X, and denote arginine, lysine, any amino acid. Proteolytic processing of SulfFP2 protein by furin and furin-like proprotein convertases, and activity with Sulf2 truncation and exchange mutants, overview
-
-
?
high pathogenic H5N1 hemagglutinin + H2O
?
-
furin can only cleave the high pathogenic hemagglutinin. It generates most of its selectivity through interactions with subsites P1, P4, and P6, with interactions at P2 being less important and little preference at P3, P5, P7, and P8. The S1, S4, and S6 pockets are specifically designed to accommodate arginine, with lysine substitution fitting less well in different degrees
-
-
?
highly pathogenic Queretaro H5N2 hemagglutinin + H2O
?
-
only processed in the presence of heparin
-
-
?
histonin + H2O
?
-
furin releases intact histonin monomers from F4-multimeric histonin (12-mer). Histonin has an RLKR motif at the C-terminus after which furin cleaves specifically
-
-
?
HIV-1 gp160 + H2O
?
-
13mer and 19mer peptides digested equally well by furin at site1, showing complete processing at 5 h. 41mer and 51mer peptides are either barely or unprocessed, respectively. Product inhibition does not explain inability of furin to process the 41mer and 51mer peptides. Extended sequences require heparin for optimal processing
-
-
?
influenza variant Fujian-like H5N1 hemagglutinin + H2O
?
-
mutations at the furin-processing site of the hemagglutinin, is less cleaved (38%) by furin as compared to the parent Fujian-like strain derived peptides
-
-
?
insulin-like growth factor-1 receptor + H2O
?
-
furin-like proprotein convertase activates insulin-like growth factor-1 receptor in vascular smooth muscle cell
-
-
?
membrane type-1 matrix metalloproteinase proenzyme + H2O
membrane type-1 matrix metalloproteinase + propeptide of membrane type-1 matrix metalloproteinase
membrane-bound collagen XXIII + H2O
shed collagen XXIII
-
furin is the major protease to process collagen XXIII. Processing occurs after the downstream recognition motif 94KIRTVR99, releasing the ectodomain
-
-
?
N-benzyloxycarbonyl-RVRR-4-methylcoumarin 7-amide + H2O
N-benzyloxycarbonyl-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
N-tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
nodal + H2O
?
-
cripto interacts with the nodal pro segment and mature domain and presents uncleaved precursor to extracellular furin that is recruited through its P-domain
-
-
?
PC1/3 C-terminal peptide + H2O
?
-
cleavage by furin into a peptide with an apparent molecular mass of 12.5 kDa. Cleavage of the C-terminal to the pair of Args occupying positions 627 and 628
-
-
?
PC2-S383A
?
-
furin fully processes the PC2 mutant at the secondary site in AtT-20 cells, site is accessible to in trans cleavage
-
-
?
PCSK9 + H2O
?
-
cleavage by furin at Arg218. Mutations R218S, F216L, and D374Y of PCSK9 associated with hypercholesterolemia result in total or partial loss of furin/PC5/6A processing at the motif RFHR21, mutant A443T shows enhanced susceptibility to furin cleavage
-
-
?
PE2 glycoprotein precursor + H2O
?
enzyme is involved in maturation of PE2 glycoprotein of alphaviruses. Enzyme cleaves efficiently PE2 glycoprotein mutants with residues arginine, serine, phenylalanine, histidine, asparagine, or aspartic acid at the +1 position
-
-
?
pGlu-Arg-Thr-Lys-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methyl-coumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
pGlu-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
?
phenylacetyl-Arg-Val-Arg-7-amido-4-methylcoumarin + H2O
phenylacetyl-Arg-Val-Arg + 7-amino-4-methylcoumarin
-
-
-
?
POMC prohormone precursor + H2O
ACTH + alpha-MSH + beta-endorphin
-
human pituitary may utilize the cathepsin L and prohormone convertase pathways for producing POMC-derived peptide hormones
-
-
?
pro-ADAMTS4 + H2O
?
-
furin plays an important role in the intracellular removal of ADAMTS4 prodomain. Multiple furin recognition sites: 206RPRR209, 209RAKR212, or 211KR212
-
-
?
pro-B-type natriuretic peptide + H2O
B-type natriuretic peptide + pro-peptide of B-type natriuretic peptide
pro-bone morphogenetic protein-4 + H2O
mature bone morphogenetic protein-4 + ?
-
-
-
?
pro-transforming growth factor-beta1 + H2O
transforming growth factor-beta1 + propeptide
-
-
-
?
procollagen V + H2O
?
-
proteolytic processing of the proalpha1(V) C-propeptide chain. Proteolytic C-propeptide removal by furin occurs between Arg1585 and Asn1586. Processing of the C-propeptide by furin is more efficient than processing by bone morphogenetic protein-1
-
-
?
proPDGF-B + H2O
PDGF-B + PGDF-B propeptide
-
a growth factor proform of 31 kDa
mature form of 17 kDa
-
?
proprotein convertase PCSK9 + H2O
?
-
-
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, PCSK9 is inactivated by furin by cleavage at residue R218
-
?
Protective antigen component of anthrax toxin + H2O
?
-
cleavage at the sequence Arg-Lys-Lys-Arg
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumaryl-7-amide + H2O
7-amino-4-methylcoumarin + Pyr-Arg-Thr-Lys-Arg
-
pERTKR-MCA
-
?
Pyr-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
a fluorogenic substrate
-
-
?
pyroglutamic acid-Arg-Thr-Lys-Arg-methylcoumaryl-7-amide + H2O
?
-
-
-
-
?
pyroglutamic acid-RTKR-4-methylcoumarin 7-amide + H2O
pyroglutamic acid-RTKR + 7-amino-4-methylcoumarin
-
-
-
-
?
SARS coronavirus spike glycoprotein + H2O
?
-
introduction of a prototypic furin recognition motif at R667 allows for efficient cleavage of the mutant glycoprotein
-
-
?
Sema3B + H2O
?
cleavage at the furin recognition site is critical for the function of this tumor suppressor
-
-
?
Sema3C + H2O
?
cleavage at the furin recognition site 742RNRR745. The point mutation R745A at the basic domain at the hypothetical furin recognition site 742RNRR745 disables the processing of Sema3C at this specific location. The C-terminal arginine of the putative furin cleavage site at the basic domain of Sema3C protein is critical for its functions in angiogenesis process
-
-
?
Synthetic peptides + H2O
?
-
based on the N-terminal sequence of human proalbumin
-
-
?
t-butoxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
tert-butyloxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumaryl-7-amide + H2O
tert-butyloxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
viral precursor protein E3E2
?
-
processes E3E2 from African Chikungunya virus strain at the HRQRR642ST site, whereas a Chikungunya virus strain of Asian origin is cleaved at site RRQRR642SI
-
-
?
acetyl-RVRR-4-methylcoumarin 7-amide + H2O
acetyl-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-RVRR-4-methylcoumarin 7-amide + H2O
acetyl-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-RVRR-aminoluciferin + H2O
acetyl-RVRR + D-aminoluciferin
-
the substrate consists of D-aminoluciferin coupled to the C-terminus of furin recognition peptide sequence, furin cleaves at the C-terminal to the last arginine residue. In the presence of furin, the probes are hydrolyzed to remove the peptide caging group and generate free D-aminoluciferin which subsequently produces light emission in the presence of firefly luciferase
-
-
?
acetyl-RVRR-aminoluciferin + H2O
acetyl-RVRR + D-aminoluciferin
-
the substrate consists of D-aminoluciferin coupled to the C-terminus of furin recognition peptide sequence, furin cleaves at the C-terminal to the last arginine residue. In the presence of furin, the probes are hydrolyzed to remove the peptide caging group and generate free D-aminoluciferin which subsequently produces light emission in the presence of firefly luciferase
-
-
?
acetyl-RYKR-4-methylcoumarin 7-amide + H2O
acetyl-RYKR + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-RYKR-4-methylcoumarin 7-amide + H2O
acetyl-RYKR + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-RYKR-aminoluciferin + H2O
acetyl-RYKR + D-aminoluciferin
-
the substrate consists of D-aminoluciferin coupled to the C-terminus of furin recognition peptide sequence, furin cleaves at the C-terminal to the last arginine residue. In the presence of furin, the probes are hydrolyzed to remove the peptide caging group and generate free D-aminoluciferin which subsequently produces light emission in the presence of firefly luciferase
-
-
?
acetyl-RYKR-aminoluciferin + H2O
acetyl-RYKR + D-aminoluciferin
-
the substrate consists of D-aminoluciferin coupled to the C-terminus of furin recognition peptide sequence, furin cleaves at the C-terminal to the last arginine residue. In the presence of furin, the probes are hydrolyzed to remove the peptide caging group and generate free D-aminoluciferin which subsequently produces light emission in the presence of firefly luciferase
-
-
?
ADAMTS9 propeptide + H2O
?
-
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
-
-
?
ADAMTS9 propeptide + H2O
?
-
ADAMTS is a disintegrin and metalloprotease domain with thrombospondin type 1 repeats
-
-
?
avian influenza virus A hemagglutinin + H2O
?
-
from strain vian influenza virus, A/chicken/Israel/810/2001 (H9N2), with R-S-K-R cleavage site
-
-
?
avian influenza virus A hemagglutinin + H2O
?
from strain vian influenza virus, A/chicken/Israel/810/2001 (H9N2), with R-S-K-R cleavage site
-
-
?
chimeric transforming growth factor-beta1/beta2 + H2O
?
-
consists of the transforming growth factor-beta1 LAP region, the transforming growth factor-beta2 cleavage site and the transforming growth factor-beta2 mature peptide
-
-
?
chimeric transforming growth factor-beta1/beta2 + H2O
?
-
efficiently cleaved
-
-
?
DSSARIRRNAKG + H2O
DSSARIRR + NAKG
-
peptide derived bone morphogenetic protein BMP10, cleavage occurs at residue R316
-
-
?
DSSARIRRNAKG + H2O
DSSARIRR + NAKG
-
peptide-derived bone morphogenetic protein BMP10, cleavage occurs at residue R316
-
-
?
epithelial Na+ channel + H2O
?
-
furin-dependent cleavage of the ectodomain at two sites in the alpha subunit and at a single site within the gamma subunit. Cleavage of the gamma subunit by furin and prostasin is required to release an inhibitory domain
-
-
?
epithelial Na+ channel + H2O
?
-
furin-dependent cleavage of the ectodomain at two sites in the alpha subunit and at a single site within the gamma subunit. Cleavage of the gamma subunit by furin and prostasin is required to release an inhibitory domain
-
-
?
epithelial Na+ channel + H2O
?
-
furin cleavage of epithelial Na+ channel subunits activates the channels by relieving Na+ self-inhibition. Activation requires that the alpha-subunit is cleaved twice
-
-
?
epithelial Na+ channel + H2O
?
-
epithelial Na+ channel activation during preferential assembly requires furin-dependent and furin-independent processing. Furin consensus site on the alpha subunit is required for epithelial Na+ channel activation upon assembly into alphabetagamma complexes, beta subunit may play a distinct furin-independent role in activation. No causal relationship between gamma cleavage and epithelial Na+ channel activation upon preferential assembly
-
-
?
feline foamy virus Env glycoprotein precursor + H2O
mature feline foamy virus leader protein Elp + SU protein + TM protein
-
-
-
-
?
feline foamy virus Env glycoprotein precursor + H2O
mature feline foamy virus leader protein Elp + SU protein + TM protein
-
the furin consensus site RRRR-/-D is located between the feline foamy virus Env residues 127 and 128
-
-
?
FPV precursor molecule HA0 + H2O
subunit HA1 + subunit HA2
-
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
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
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
i.e. (P)RR, a 35 kDa protein, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A
i.e. s(P)RR, a 28 kDa protein
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
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
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
i.e. (P)RR, a 35 kDa protein, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A
i.e. s(P)RR, a 28 kDa protein
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
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
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
-
i.e. (P)RR, a 35 kDa protein, cleavage site at Arg275-X-X-Arg278-/-, no activity with (P)RR mutant R275A/KT/R278A
i.e. s(P)RR, a 28 kDa protein
-
?
G-protein-coupled receptor GPR107 + H2O
?
cleavage by endoprotease furin, a disulfide bond connects the two resulting fragments, overview
-
-
?
G-protein-coupled receptor GPR107 + H2O
?
recombinant HA-tagged substrate expressed in HeLa cells. GPR107 contains an extended furin recognition site that includes KSKR, a variant of the classical furin cleavage motif (Arg-Xaa-(Lys/Arg)-Arg), although not common among furin substrates, in GPR107 the Lys residue replaces the first conserved Arg
-
-
?
gp40/15 + H2O
gp40 + gp15
-
cleaves recombinant Cryptosporidium parvum and Cryptosporidium hominis gp40/15. Putative furin cleavage site RSRR
-
-
?
gp40/15 subtype 1e + H2O
gp40 + gp15
-
RSRR sequence is replaced by ISKR, has an alternative furin cleavage site at KSISKR2
-
-
?
gp40/15 subtype 1e + H2O
gp40 + gp15
-
RSRR sequence is replaced by ISKR, has an alternative furin cleavage site at KSISKR2
-
-
?
hepatitis B e antigen precursor + H2O
?
-
furin can cleave the RRDR, RRGR, and RSPR motifs
-
-
?
HIV-1 Tat protein + H2O
?
-
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
-
-
?
HIV-1 Tat protein + H2O
?
-
furin cleaves full-length Tat protein between amino acid 56 and 57, irrespective of seuence differences at amino acid 57
-
-
?
human semaphorin 3F + H2O
?
-
furin processing of semaphorin 3F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin, overview
-
-
?
human semaphorin 3F + H2O
?
-
the substrate is produced as a C-terminal or an N-terminal human growth hormone fusion from the pLexM vector. Cleavage at the RXRR furin recognition site in the C-terminus, which is essential for the interaction of the C-terminus of Sema3F with the b1 domain of neuropilin
-
-
?
membrane type-1 matrix metalloproteinase proenzyme + H2O
membrane type-1 matrix metalloproteinase + propeptide of membrane type-1 matrix metalloproteinase
-
-
-
-
?
membrane type-1 matrix metalloproteinase proenzyme + H2O
membrane type-1 matrix metalloproteinase + propeptide of membrane type-1 matrix metalloproteinase
-
intracellular processing in breast carcinoma MCF-MT1-E240A-FLAG cells
-
-
?
membrane-tethered membrane type-1 matrix metallo-proteinase + H2O
?
-
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
-
-
?
membrane-tethered membrane type-1 matrix metallo-proteinase + H2O
?
-
there are two furin cleavage motifs, R89-R-P-R-C93 and R108-R-K-R-Y112
-
-
?
Moloney murine leukemia virus Env precursor protein + H2O
?
furin cleaves the Env precursor into the surface and transmembrane subunits in the cell and then the viral protease cleaves the R-peptide from TM in newvirus. Structure analysis of the open cage-like structure like that of the R-peptide precursor and of the mature protein, overview. Furin cleavage not only separates the subunits and liberates the fusion peptide at the end of TM but also allows the C-terminal domain to relocate into a peripheral position. This conformational change might explain how the C-terminal domain of surface subunit gains the potential to undergo disulfide isomerization, an event that facilitates membrane fusion
-
-
?
mouse pro-growth hormone-releasing hormone + H2O
?
-
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
-
-
?
mouse pro-growth hormone-releasing hormone + H2O
?
-
furin is the most efficient convertase in cleaving the N-terminal RXXR/RXRR site
-
-
?
PA83 + H2O
PA63 + PA20
the protective antigen substrate is from Bacillus anthracis, commercial plant-produced deglycosylated PA83 (dPA83). Cleavage of the substrate generates two protein fragments with distinctly different molecular masses of 63 kDa (PA63) and 20 kDa (PA20). Plant-produced PA83 protein is almost fully cleaved by commercial furin, while plant-produced truncated enzymatically active furin displays about 75% relative activity compared to commercial human furin in vitro
-
-
?
peptidyl-7-amido-4-methyl-coumarin + H2O
7-amino-4-methyl-coumarin + peptide
-
-
-
?
peptidyl-7-amido-4-methyl-coumarin + H2O
7-amino-4-methyl-coumarin + peptide
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
precursor of transforming growth factor beta + H2O
?
-
precursor of transforming growth factor beta requires cleavage by furin for its activation
-
-
?
precursor of transforming growth factor beta + H2O
?
-
precursor of transforming growth factor beta requires cleavage by furin for its activation
-
-
?
pro-B-type natriuretic peptide + H2O
B-type natriuretic peptide + pro-peptide of B-type natriuretic peptide
-
activation by N-terminal fragment cleavage of proBNP in human plasma through furin
-
-
?
pro-B-type natriuretic peptide + H2O
B-type natriuretic peptide + pro-peptide of B-type natriuretic peptide
-
cleavage sequence is Arg73-Ala-Pro-Arg76-/-Ser77
-
-
?
pro-BMP4 + H2O
BMP4 + propeptide of BMP4
-
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
-
-
?
pro-BMP4 + H2O
BMP4 + propeptide of BMP4
-
i.e. pro-bone morphogenetic protein 4, site-specific cleavage by furin
-
-
?
pro-brain-derived neurotrophic factor + H2O
mature brain-derived neurotrophic factor + ?
-
-
-
-
?
pro-brain-derived neurotrophic factor + H2O
mature brain-derived neurotrophic factor + ?
-
-
-
-
?
pro-CD109 + H2O
CD109 + CD109 propeptide
-
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
-
-
?
pro-CD109 + H2O
CD109 + CD109 propeptide
-
CD109 is a glycosylphosphatidylinositol-anchored glycoprotein, cleavage motif comprises amino acids 1270-RRRR-1273
-
-
?
pro-hepcidin + H2O
active mature hepcidin
-
furin processes the iron-regulatory peptide hepcidin to the bioactive mature hepcidin-25 form
-
-
?
pro-hepcidin + H2O
active mature hepcidin
-
furin processes the iron-regulatory peptide hepcidin to the bioactive mature hepcidin-25 form
-
-
?
proform tissue growth factor 1beta + H2O
tissue growth factor beta1 + propeptide
-
-
-
?
proform tissue growth factor 1beta + H2O
tissue growth factor beta1 + propeptide
-
-
-
?
Protein precursor + H2O
?
-
cleavage of-Arg-Xaa-Yaa-Arg-+- bonds where Xaa can be any amino acid and Yaa is Arg or Lys
-
-
?
Protein precursor + H2O
?
-
pro-von Willebrand factor (both the P4 arginine and the P2 lysine play an important role in substrate recognition)
-
-
?
Protein precursor + H2O
?
-
the term -+- depicts the point of cleavage, e.g. stromelysin 3
-
-
?
Protein precursor + H2O
?
-
pro-von Willebrand factor (both the P4 arginine and the P2 lysine play an important role in substrate recognition)
-
-
?
Protein precursor + H2O
?
-
cleavage of-Arg-Xaa-Yaa-Arg-+- bonds where Xaa can be any amino acid and Yaa is Arg or Lys
-
-
?
Protein precursor + H2O
?
-
pro-von Willebrand factor (both the P4 arginine and the P2 lysine play an important role in substrate recognition)
-
-
?
Protein precursor + H2O
?
-
rapid cleavage of the-Arg-Arg-Asp-site, no significant cleavage of natural unprocessed variants with cleavage site sequences of-Arg-Arg-Val-, His-Arg-Asp- or Cys-Arg-Asp
-
-
?
Protein precursor + H2O
?
-
circulating human proalbumin variants with a mutation at either of the basic amino acids adjacent to the cleavage site are not cleaved
-
-
?
Protein precursor + H2O
?
-
cleavage following the prosequence Arg-Gly-Val-Phe-Arg-Arg
-
-
?
Protein precursor + H2O
?
-
also cleaves chicken proalbumin after a single arginine residue following the Arg-Asn-Leu-Gln-Arg-Phe-Ala-Arg prosequence
-
-
?
RPTPkappa + H2O
?
-
furin is required for S1 processing of RPTPkappa in the secretory pathway. Purified furin cleaves RPTPkappa within the membrane-proximal fibronectin type III domain at the sequence RTKR
-
-
?
RTKR 4-methyl-coumarin 7-amide + H2O
7-amino-4-methyl-coumarin + RTKR
-
-
-
?
RTKR 4-methyl-coumarin 7-amide + H2O
7-amino-4-methyl-coumarin + RTKR
-
-
?
Shiga toxin + H2O
?
-
not only the sequence known to be a minimal furin-recognition site, but also the structure around this site are important for furin processing of Shiga toxin and for rapid intoxication
-
-
?
Shiga toxin + H2O
?
-
not only the sequence known to be a minimal furin-recognition site, but also the structure around this site are important for furin processing of Shiga toxin and for rapid intoxication
-
-
?
t-butyloxycarbonyl-Arg-Val-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
additional information
?
-
-
LRR peptidyl-7-amido-4-methyl-coumarin is no substrate
-
?
additional information
?
-
-
Borna disease virus glycoprotein is synthesized as a precursor that is cleaved by cellular furin to produce the mature glycoproteins GP1 and GP2
-
-
?
additional information
?
-
-
mutation in the RSRR cleavage site prevents processing of gp40/15
-
-
?
additional information
?
-
alternative PE2 cleavage phenotypes observed in vertebrate and arthropod cells are due to differences in substrate specificity between the arthropod and vertebrate furin enzymes and not to differences in host cell glycoprotein processing pathways
-
-
?
additional information
?
-
-
alternative PE2 cleavage phenotypes observed in vertebrate and arthropod cells are due to differences in substrate specificity between the arthropod and vertebrate furin enzymes and not to differences in host cell glycoprotein processing pathways
-
-
?
additional information
?
-
-
intracellular processing by furin-like prohormone convertases is required for secretion of cysteine-rich FGF receptor
-
-
?
additional information
?
-
prohormone convertases specificities for prohormone cleavage, overview
-
-
?
additional information
?
-
-
prohormone convertases specificities for prohormone cleavage, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
no processing of: human lactase-phlorizin hydrolase
-
-
?
additional information
?
-
-
Preference for Arg-Glu-Lys-Arg-+-Ala vs. Lys-Ala-Lys-Arg-+-Arg
-
-
?
additional information
?
-
-
peptides patterned on the sequence 307-330 of the specific viral strains of the gp120 V3 loop
-
-
?
additional information
?
-
-
study of the specificity of human prohormone convertase PC1 and human furin
-
-
?
additional information
?
-
-
endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway
-
-
?
additional information
?
-
-
probably involved in the proteolysis resulting in secretion of rat endopeptidase 24.18 alpha-subunit
-
-
?
additional information
?
-
-
possible role in processing essential cellular factors
-
-
?
additional information
?
-
-
implicated in maturation of substrates involved in development, signaling, coagulation, and pathogenesis, constitutive secretory pathway
-
?
additional information
?
-
-
proteolytic processing of a variety of proteins in the exocytic and endocytic pathways
-
?
additional information
?
-
-
low pathogenic Mexico H5N2 hemagglutinin is not processed by furin
-
-
?
additional information
?
-
-
mutation in the RSRR cleavage site prevents processing of gp40/15
-
-
?
additional information
?
-
-
a three-step autocatalytic processing including the cleavage of the prodomain at the Arg-Leu-Gln-Arg89Q-Glu90 site, is required for the efficient activation of furin
-
-
?
additional information
?
-
-
furin possesses a strong preference for substrates containing the multibasic cleavage motif Arg-X-Arg/Lys-ArgV-X
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
furin cleavage sequence is RXXR-/-X, X is not Cys
-
-
?
additional information
?
-
-
furin is a proprotein convertase that requires the cleavage sequence R-X-K/R-R, clear interdependence of furin subsites, substrate specificity with synthetic peptide substrates, overview
-
-
?
additional information
?
-
-
furin performs a calcium-dependent proteolytic cleavage at the C-terminus of a consensus amino acid motif R-X-K/R-R, with X being any amino acid. This tetrapeptide motif provides sufficient specificity to bind the active furin
-
-
?
additional information
?
-
-
furin performs autocleaqvage to its soluble form
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
proprotein convertases represent highly selective serine proteases that activate their substrates upon proteolytic cleavage
-
-
?
additional information
?
-
-
proprotein convertases represent highly selective serine proteases that activate their substrates upon proteolytic cleavage
-
-
?
additional information
?
-
high substrate selectivity and enzymatic activity of furin
-
-
?
additional information
?
-
recombinant expression of Sema3 wild-type substrates and of mutant Sema3C (R745A, 85.2 kDa) in HEK-293FT cells
-
-
?
additional information
?
-
-
recombinant expression of Sema3 wild-type substrates and of mutant Sema3C (R745A, 85.2 kDa) in HEK-293FT cells
-
-
?
additional information
?
-
to transiently express the substrate factor IX (FIX, amino acids 29-461) in Nicotiana benthamiana plants, the signal peptide (amino acids 1-28) is removed from the FIX sequence (UniProt ID P00740) and replaced with a Nicotiana tabacum PR-1a signal peptide. a KDEL sequence and the His6 tag are added to the C-terminus. Enzyme substrate precursor polypeptide of factor IX (FIX) undergoes several post translational modifications (PTMs), including the removal of the signal peptide (aa 1-28), carboxylation of the first 12 glutamic acid residues downstream from the 18-amino acid propeptide sequence (aa 29-46) in the region rich in glutamic acid (aa 47-92, called the gamma-carboxyglutamic acid or Gla domain) at the N-terminus. Proper gamma-carboxylation of the Gla domain is required for binding to calcium and phospholipids that is critical for proper protease activity during coagulation. In vivo, vitamin K-dependent gamma-carboxylase binds to the 18-amino acid propeptide of FIX, which is then cleaved and is required for optimal binding of the Gla domain to Ca2+ and phospholipids
-
-
?
additional information
?
-
-
to transiently express the substrate factor IX (FIX, amino acids 29-461) in Nicotiana benthamiana plants, the signal peptide (amino acids 1-28) is removed from the FIX sequence (UniProt ID P00740) and replaced with a Nicotiana tabacum PR-1a signal peptide. a KDEL sequence and the His6 tag are added to the C-terminus. Enzyme substrate precursor polypeptide of factor IX (FIX) undergoes several post translational modifications (PTMs), including the removal of the signal peptide (aa 1-28), carboxylation of the first 12 glutamic acid residues downstream from the 18-amino acid propeptide sequence (aa 29-46) in the region rich in glutamic acid (aa 47-92, called the gamma-carboxyglutamic acid or Gla domain) at the N-terminus. Proper gamma-carboxylation of the Gla domain is required for binding to calcium and phospholipids that is critical for proper protease activity during coagulation. In vivo, vitamin K-dependent gamma-carboxylase binds to the 18-amino acid propeptide of FIX, which is then cleaved and is required for optimal binding of the Gla domain to Ca2+ and phospholipids
-
-
?
additional information
?
-
-
survey of furin substrate specificity using substrate phage display
-
-
?
additional information
?
-
-
synthetic tripeptide substrates containing only pairs of basic amino acids are not well cleaved
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additional information
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the term -+- depicts the point of cleavage, the enzyme prefers substrates with an arginine 4-amino acid amino-terminal to the cleavage site
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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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no cleavage of the low pathogenic H1N1 H1 hemagglutinin
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additional information
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soluble hemojuvelin originates from a furin cleavage at position 332-335. Soluble hemojuvelin is increased in cells overexpressing exogenous furin
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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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3D structural environment of the furin binding pocket surrounding the core region P6-P2' of furin substrates, comparison to other protein convertases, to allow the rational design of novel specific molecular inhibitors targeting specific members of the mammalian proprotein convertase family, overview. The furin autocleavage site is RGVTKR75 -/-
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additional information
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furin performs a calcium-dependent proteolytic cleavage at the C-terminus of a consensus amino acid motif R-X-K/R-R, with X being any amino acid. This tetrapeptide motif provides sufficient specificity to bind the active furin
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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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LRR peptidyl-7-amido-4-methyl-coumarin is no substrate
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additional information
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LRR peptidyl-7-amido-4-methyl-coumarin is no substrate
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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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additional information
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regular (short) form of transforming growth factor-beta2 and its spliced variant with an additional exon (long form) are insensitive to furin
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additional information
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transforming growth factor-beta2 and its spliced variant with an additional exon (long form) are insensitive to furin. Transforming growth factor-beta2 is only inefficiently cleaved as a consequence of the isoform specific characteristics of its latency-associated peptide region structures
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