Any feedback?
Information on EC 3.4.21.75 - Furin
for references in articles please use BRENDA:EC3.4.21.75Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.21.75 FurinSpecify your search results
Word Map
- 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
The enzyme appears in viruses and cellular organisms
Synonyms
furin, sheddase, prohormone convertase, furin a, furin protease, proconvertase, subtilisin-like proprotein convertase, furin-like protease, furin convertase, kpc-1, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Dibasic processing enzyme
-
-
-
-
furin
furin-like protease
PACE
Paired basic amino acid cleaving enzyme
-
-
-
-
Paired basic amino acid converting enzyme
-
-
-
-
Paired basic amino acid residue cleaving enzyme
-
-
-
-
PC1
PCSK3
prohormone convertase
prohormone convertase 1
Proprotein convertase
Serine proteinase PACE
-
-
-
-
SPC3
-
-
-
-
subtilisin-like protein convertase
Trans golgi network protease furin
-
-
-
-
additional information
PACE
-
-
-
-
PC1
-
-
-
-
prohormone convertase
-
-
-
-
Proprotein convertase
-
-
-
-
Proprotein convertase
-
-
Proprotein convertase
-
additional information
-
at least 3 related enzymes are recognized in mammals: PC2, PC3, identical with PC1and PC4, which have somewhat different specificities, the integral membrane protein furin may be of ancient origin, possibly ancestral to the secretory granule processing enzymes lacking transmembrane domains, such as PC2 and PC3
additional information
-
at least 3 related enzymes are recognized in mammals: PC2, PC3, identical with PC1and PC4, which have somewhat different specificities, the integral membrane protein furin may be of ancient origin, possibly ancestral to the secretory granule processing enzymes lacking transmembrane domains, such as PC2 and PC3
additional information
-
at least 3 related enzymes are recognized in mammals: PC2, PC3, identical with PC1and PC4, which have somewhat different specificities, the integral membrane protein furin may be of ancient origin, possibly ancestral to the secretory granule processing enzymes lacking transmembrane domains, such as PC2 and PC3
additional information
-
at least 3 related enzymes are recognized in mammals: PC2, PC3, identical with PC1and PC4, which have somewhat different specificities, the integral membrane protein furin may be of ancient origin, possibly ancestral to the secretory granule processing enzymes lacking transmembrane domains, such as PC2 and PC3
additional information
-
at least 3 related enzymes are recognized in mammals: PC2, PC3, identical with PC1and PC4, which have somewhat different specificities, the integral membrane protein furin may be of ancient origin, possibly ancestral to the secretory granule processing enzymes lacking transmembrane domains, such as PC2 and PC3
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
additional information
furin belongs to the family of proprotein convertase subtilisin/kexin type proteases
additional information
-
also cf. EC 3.4.21.93. Prohormone convertases are calcium-dependent serine endoproteases of the subtilisin family
additional information
-
furin is a crucial member of secretory mammalian subtilase, the proprotein convertase or proprotein convertase subtilisin/kexin, PCSK, superfamily
additional information
-
at least 3 related enzymes are recognized in mammals: PC2, PC3, identical with PC1and PC4, which have somewhat different specificities, the integral membrane protein furin may be of ancient origin, possibly ancestral to the secretory granule processing enzymes lacking transmembrane domains, such as PC2 and PC3
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
additional information
-
furin belongs to the subtilisin/Kex2p-like proprotein convertases
additional information
-
at least 3 related enzymes are recognized in mammals: PC2, PC3, identical with PC1and PC4, which have somewhat different specificities, the integral membrane protein furin may be of ancient origin, possibly ancestral to the secretory granule processing enzymes lacking transmembrane domains, such as PC2 and PC3
additional information
-
one of a group of subtilisin homologues structurally and functionally similar to kexin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
cleavage of-Arg-Xaa-Yaa-Arg-+- bonds where Xaa can be any amino acid and Yaa is Arg or Lys, releases albumin, complement component C3 and von Willebrand factor from their respective precursors, the term -+- depicts the point of cleavage
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
141760-45-4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
lethal factor inhibitor 2 +