Any feedback?
Information on EC 3.4.21.75 - Furin and Organism(s) Mus musculus
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 taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected 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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Dibasic processing enzyme
-
-
-
-
PACE
-
-
-
-
Paired basic amino acid cleaving enzyme
-
-
-
-
Paired basic amino acid converting enzyme
-
-
-
-
Paired basic amino acid residue cleaving enzyme
-
-
-
-
PC1
-
-
-
-
prohormone convertase
-
-
-
-
Proprotein convertase
Serine proteinase PACE
-
-
-
-
SPC3
-
-
-
-
Trans golgi network protease furin
-
-
-
-
additional information
-
furin belongs to the subtilisin/Kex2p-like proprotein convertases
Proprotein convertase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
141760-45-4
-
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
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-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
-
-
?
Boc-RVRR-7-amido-4-methylcoumarin + H2O
Boc-RVRR + 7-amino-4-methylcoumarin
-
-
-
-
?
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
-
-
?
full-length (pro)renin receptor + H2O
soluble (pro)renin receptor + 10 kDa fragment of (pro)renin receptor
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
pGlu-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
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
-
-
-
?
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
-
?
Pyr-Arg-Thr-Lys-Arg-4-methylcoumarin 7-amide + H2O
Pyr-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
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
-
-
?
Synthetic peptides + H2O
?
-
based on the N-terminal sequence of human proalbumin
-
-
?
tert-butoxycarbonyl-Arg-Val-Arg-Arg-4-methylcoumarin 7-amide + H2O
tert-butoxycarbonyl-Arg-Val-Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
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
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
synthetic tripeptide substrates containing only pairs of basic amino acids are not well cleaved
-
-
?
additional information
?
-
-
the term -+- depicts the point of cleavage, the enzyme prefers substrates with an arginine 4-amino acid amino-terminal to the cleavage site
-
-
?
additional information
?
-
-
endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway
-
-
?
additional information
?
-
-
no cleavage of the low pathogenic H1N1 H1 hemagglutinin
-
-
?
additional information
?
-
-
soluble hemojuvelin originates from a furin cleavage at position 332-335. Soluble hemojuvelin is increased in cells overexpressing exogenous furin
-
-
?
additional information
?
-
-
the bioluminescence emission in the presence of firefly luciferase is furin-dependent and specific in living mice, overview
-
-
?
additional information
?
-
-
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 -/-
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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
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
-
?
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
-
-
?
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
-
-
?
proform tissue growth factor 1beta + H2O
tissue growth factor beta1 + propeptide
-
-
-
?
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
-
?
additional information
?
-
-
endoproteolytic cleavage at paired basic residues of proproteins of the eukaryotic secretory pathway
-
-
?
additional information
?
-
-
the bioluminescence emission in the presence of firefly luciferase is furin-dependent and specific in living mice, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha1-antitrypsin Portland variant
-
i.e. alpha1-PDX, inhibits furin and the generation of soluble (pro)renin receptor
-
decanoyl-Arg-Val-Lys-Arg-chloromethyl ketone
-
efficiently inhibits ectodomain shedding by 95%
pro-hepcidin
-
hydrolytic activity of membrane furin against the fluorescent substrate Boc-RVRR-7-amino-4-methyl-coumarin is reduced by approximately 50% in presence of 2 micromol pro-hepcidin and completely abolished in presence of 5 micromol pro-hepcidin
-
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
blocks furin activity, 99% inhibition of parathyroid hormone-related peptide maturation
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
furin inhibitor, pro-hepcidin activity is abolished
hexa-D-arginine
-
blocks furin activity, 85% inhibition of parathyroid hormone-related peptide maturation
additional information
-
soluble hemojuvelin is reduced in cells treated with a furin inhibitor
-
additional information
-
pepstatin A, 1,10-ortho-phenanthroline, EDTA, or TAPI-0 do not inhibit ectodomain shedding
-
additional information
-
design of specific small molecule inhibitors targeting furi, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
furin is up-regulated by iron deficiency and hypoxia in association with the stabilization of HIF-1alpha
-
additional information
-
relationship between Sox-9 dependent expression of furin and the maturation/bioactivation of substrates involved in chondrogenesis. Peak expression of both furin mRNA and furin parathyroid hormone-related peptide maturation in ATDC5 cells during chondrocyte nodule formation stage
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000574
biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Pro-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.000009
biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Thr-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.0000151
biotin-(8-(amino)-3,6-dioxa-octanoyl)3-Arg-Pro-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.0000383
biotin-8-(amino)-3,6-dioxa-octanoyl-Arg-Pro-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
0.0042
biotin-8-(amino)-3,6-dioxa-octanoyl-Val-Arg-4-amidinobenzylamide
-
pH 7.0, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 6.5
-
5: about 35% of activity maximum, 6.5: about 15% of activity maximum, mouse, acetyl-Arg-Ser-Lys-Arg-4-methylcoumarin 7-amide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
29699, 29700, 667392, 669253, 670247, 677460, 677511, 677962, 678739, 678910, 678922, 680811, 680878, 697609, 699309, 701154, 707598, 708682, 708758, 717230, 717317, 717857, 718256, 731605
-
-
rat somatomammotroph cell line, GH4C1 infected with vaccinia virus recombinants of murine PC1
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
PCSK3 is primarily expressed in the duodenum and the jejunum. PCSK3 is detectable in 75% of glucose-dependent insulinotropic polypeptide positive cells and 60% of substance P positive cells
additional information
additional information
-
furin mRNA and protein highly expressed in T helper 1 cells compared with T helper 2 cells. Stat4 binding sites in the putative promoter region (2000 bp upstream of exon 1). Also present in CD4+ T cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
human, mainly, the enzyme can translocate between the cell surface and the trans-Golgi network
-
additional information
-
localization of furin predominantly outside lipid rafts
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
molecular evolution of enzyme function in the proprotein convertase family, overview
malfunction
metabolism
furin-dependent transactivators in different mouse CD4+ T-cell subsets, overview
physiological function
malfunction
-
placenta-specific knockdown of furin in the mouse leads to severe defects in syncytialization and embryonic lethality, phenotype, overview
malfunction
interleukin-2 is increased initially in furin-deficient mouse CD4+ T cells, but the T-cell receptor-induced interleukin-2 mRNA expression is not sustained in the absence of furin. Conditional deletion of FURIN in CD4+ T-cells leads to hyperactive T-cells and the overproduction of Th1 and Th2 cytokines and systemic autoimmunity as a result of the loss of Treg-mediated immunologic tolerance
physiological function
-
furin is responsible for the shedding of the endogenous (pro)renin receptor, (P)RR, it generates the soluble form of (P)RR, in cultured cells
physiological function
-
the bioluminescence emission in the presence of firefly luciferase is furin-dependent and specific, furin activates the luciferase activity 30fold
physiological function
-
furin serves as an intermolecular chaperone for matrix metalloprotease MMP-28 secretion by interacting with the propeptide domain of MMP-28. cleavage of MMP-28 at the furin consensus sequence does not occur and proteolytic inactive furin is equally effective in enhancing MMP-28 secretion
physiological function
-
in mice lacking furin in hepatocytes, the PCSK9-inactivated form is strongly reduced. Full-length, membrane-bound, but not soluble, furin is the cognate convertase which inactivates PCSK9 by cleavage at R218
physiological function
-
the multinucleated syncytial trophoblast, which forms the outermost layer of the placenta and serves multiple functions, is differentiated from and maintained by cytotrophoblast cell fusion. Cytotrophoblast cell fusion and syncytialization are accompanied by furin expression. Processing of type 1 IGF receptor by furin is an essential mechanism for syncytialization. Furin function is required for the development of syncytiotrophoblast structure in the labyrinth layer, as well as for normal embryonic development
physiological function
morula compaction and inner cell mass formation depend on PC7 and the related proteases Furin and Pace4. These proteases jointly regulate cell-cell adhesion mediated by E-cadherin processing during blastocyst formation
physiological function
proprotein convertase substilisin/kexin-type (PCSK) enzymes regulate proprotein maturation by catalyzing the proteolytic cleavage of their substrates. The prototype PCSK furin is induced upon T-cell receptor (TCR) activation, and its expression in T cells is critical for the maintenance of peripheral immune tolerance. Proprotein convertase furin regulates T cell receptor-induced transactivation. TGF-beta1 and NOTCH1 are synthesized initially as inactive precursors and are proteolytically activated during T-cell activation. In Jurkat cells, furin is dispensable for immediate T-cell receptor (TCR) signaling steps, such as ERK, ZAP70, or LAT phosphorylation. Furin regulates the expression of interleukin-2 in human Jurkat T-cell lines, specific TGF-beta1-independent role for furin in interleukin-2 regulation. Furin activates specifically and nonredundantly the anti-inflammatory cytokine pro-TGF-beta1 and thus, directly modulates the activity of CD4+ and CD8+ T-cells. Importantly, Furin regulates its own activity by autocleavage, and its mRNA and protein levels are modulated dynamically during alterations in T-cell physiology
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). FURIN_MOUSE
793
2
86772
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
3 different forms, MW 81000, 83000 and 96000, may be produced by differential processing of a furin molecule and mature furin may be autocatalytically produced
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of furin with bound decanoyl-Arg-Val-Lys-Arg-chloromethylketone inhibitor
-
triclinic crystals, space group P1, unit cell dimensions a = 93.3 A, b = 135.4 A, c = 137.8 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
LoVo/neo cells lacking functional furin are unable to activate both wild type Shiga toxin and mutant Shiga-2D toxin
additional information
-
deletion of the cysteine-rich domain and the cytoplasmic tail of furin does not abolish binding to cripto
additional information
-
production of lentiviruses carrying shRNA for furin and infection of blastocyststage embryos with the viruses, along with lentiviruses expressing EGFP
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 5 mg/ml bovine serum albumin, less than 5% loss of activity after 2 months
-
4°C, 5 mg/ml bovine serum albumin, 0.02% NaN3, less than 5% loss of activity after 2 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification protocol combining the heterologous expression of furin from CHO cells with an affinity step that efficiently extracts only active furin from the conditioned medium by using furin-specific inhibitor moieties as bait. The best affinity tag used, biotin-(8-(amino)-3,6-dioxa-octanoyl)2-Arg-Pro-Arg-4-4-amidinobenzylamide coupled to streptavidin-Sepharose beads, is used in a three-step chromatographic protocol and routinely results in a high yield of a homogeneous furin preparation with a specific activity of about 60 units/mg protein
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
furin cDNA ligated into a modified pCEP-Pu vector carrying a 5'-SPARC/BM40 signal peptide and a 3'-FLAG tag. HEK 293-EBNA cells cotransfected with full-length alpha1(XXIII) or furin cDNA and phosphatidylinositol-linked placental alkaline phosphatase or human transferrin receptor cDNA, respectively
-
soluble ectodomain of furin is expressed in dihydrofolate reductase-amplified CHO cells
-
stably transfected LoVo cells expressing either furin (LoVo/fur) or the vector alone (LoVo/neo)
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
furin expression is upregulated by the Th1 hallmark cytokine interleukin-12. T-cell activation via T-cell receptor induces FURIN expression
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
bioluminogenic probes can specifically image furin activity in xenografted breast cancer tumors in mice
medicine
medicine
-
inhibiting furin-like proprotein convertases protects the host from the distinct furin-dependent infections and lay a foundation for novel, host cell-focused therapies against acute diseases
medicine
-
interleukin 12 induction of furin plays a role in interferon gamma protein regulation and control of T helper 1 cell differentiation
medicine
-
some mutations of H5N1 H5 cleavage sequence fit less well into furin and hence may reduce the high pathogenicity of the H5N1 virus
medicine
-
peptide CMGTINTRTKKC has strong affinity for rhabdomyosarcoma cells in vitro and in vivo, by binding to furin. Treatment of rhabdomyosarcoma cells in mice with doxorubicin coupled to the targeting peptide results in a two-fold increase in therapeutic efficacy compared to doxorubicin treatment alone. Surface-furin binding may be used as novel mechanism for therapeutic cell penetration
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hatsuzawa, K.; Murakami, K.; Nakayama, K.
Molecular and enzymatic properties of furin, a Kex2-like endoprotease involved in precursor cleavage at Arg-X-Lys/Arg-Arg sites
J. Biochem.
111
296-301
1992
Mus musculus
Nakayama, K.
Purification of recombinant soluble forms of furin produced in Chinese hamster ovary cells
Methods Enzymol.
244
167-175
1994
Mus musculus
Brennan, S.O.; Nakayama, K.
Cleavage of proalbumin peptides by furin reveals unexpected restrictions at the P2 and P1 sites
FEBS Lett.
347
80-84
1994
Mus musculus
Hatsuzawa, K.; Nagahama, M.; Takahashi, S.; Takada, K.; Murakami, K.; Nakayama, K.
Purification and characterization of furin, a Kex2-like processing endoprotease, produced in Chinese hamster ovary cells
J. Biol. Chem.
267
16094-16099
1992
Mus musculus
Oda, K.; Misumi, Y.; Ikehara, Y.; Brennan, S.O.; Hatsuzawa, K.; Nakayama, K.
Proteolytic cleavages of proalbumin and complement Pro-C3 in vitro by a truncated soluble form of furin, a mammalian homologue of the yeast Kex2 protease
Biochem. Biophys. Res. Commun.
189
1353-1361
1992
Mus musculus
Rehemtulla, A.; Kaufman, R.J.
Preferred sequence requirements for cleavage of pro-von Willebrand factor by propeptide-processing enzymes
Blood
79
2349-2355
1992
Homo sapiens, Mammalia, Mus musculus
Brennan, S.O.; Nakayama, K.
Furin has the proalbumin substrate specificity and serpin inhibitory properties of an in situ hepatic convertase
FEBS Lett.
338
147-151
1994
Mus musculus
Jean, F.; Basak, A.; Rondeau, N.; Benjannet, S.; Hendy, G.N.; Seidah, N.G.
Enzymic characterization of murine and human prohormone convertase-1 (mPC1 and hPC1) expressed in mammalian GH4C1 cells
Biochem. J.
292
891-900
1993
Homo sapiens, Mus musculus
Zhou, Y.; Lindberg, I.
Purification and characterization of the prohormone convertase PC1(PC3)
J. Biol. Chem.
268
5615-5623
1993
Mus musculus
Sarac, M.S.; Cameron, A.; Lindberg, I.
The furin inhibitor hexa-D-arginine blocks the activation of Pseudomonas aeruginosa exotoxin A in vivo
Infect. Immun.
70
7136-7139
2002
Mus musculus
Cameron, A.; Appel, J.; Houghten, R.A.; Lindberg, I.
Polyarginines are potent furin inhibitors
J. Biol. Chem.
275
36741-36749
2000
Homo sapiens, Mus musculus
Bowler, R.P.; Nicks, M.; Olsen, D.A.; Thogersen, I.B.; Valnickova, Z.; Hojrup, P.; Franzusoff, A.; Enghild, J.J.; Crapo, J.D.
Furin proteolytically processes the heparin-binding region of extracellular superoxide dismutase
J. Biol. Chem.
277
16505-16511
2002
Homo sapiens, Mus musculus, Rattus norvegicus
Henrich, S.; Cameron, A.; Bourenkov, G.P.; Kiefersauer, R.; Huber, R.; Lindberg, I.; Bode, W.; Than, M.E.
The crystal structure of the proprotein processing proteinase furin explains its stringent specificity
Nat. Struct. Biol.
10
520-526
2003
Mus musculus
Peinado, J.R.; Kacprzak, M.M.; Leppla, S.H.; Lindberg, I.
Cross-inhibition between furin and lethal factor inhibitors
Biochem. Biophys. Res. Commun.
321
601-605
2004
Mus musculus
Dey, A.; Norrbom, C.; Zhu, X.; Stein, J.; Zhang, C.; Ueda, K.; Steiner, D.F.
Furin and prohormone convertase 1/3 are major convertases in the processing of mouse pro-growth hormone-releasing hormone
Endocrinology
145
1961-1971
2004
Mus musculus
Rozan, L.; Krysan, D.J.; Rockwell, N.C.; Fuller, R.S.
Plasticity of extended subsites facilitates divergent substrate recognition by Kex2 and furin
J. Biol. Chem.
279
35656-35663
2004
Mus musculus
Anders, L.; Mertins, P.; Lammich, S.; Murgia, M.; Hartmann, D.; Saftig, P.; Haass, C.; Ullrich, A.
Furin-, ADAM 10-, and gamma-secretase-mediated cleavage of a receptor tyrosine phosphatase and regulation of beta-catenins transcriptional activity
Mol. Cell. Biol.
26
3917-3934
2006
Homo sapiens, Mus musculus
Guimont, P.; Grondin, F.; Dubois, C.M.
Sox9-dependent transcriptional regulation of the proprotein convertase furin
Am. J. Physiol. Cell Physiol.
293
C172-C183
2007
Homo sapiens, Mus musculus
Guo, X.L.; Li, L.; Wei, D.Q.; Zhu, Y.S.; Chou, K.C.
Cleavage mechanism of the H5N1 hemagglutinin by trypsin and furin
Amino Acids
35
375-382
2008
Mus musculus
Kurmanova, A.; Llorente, A.; Polesskaya, A.; Garred, O.; Olsnes, S.; Kozlov, J.; Sandvig, K.
Structural requirements for furin-induced cleavage and activation of Shiga toxin
Biochem. Biophys. Res. Commun.
357
144-149
2007
Homo sapiens, Mus musculus
Decha, P.; Rungrotmongkol, T.; Intharathep, P.; Malaisree, M.; Aruksakunwong, O.; Laohpongspaisan, C.; Parasuk, V.; Sompornpisut, P.; Pianwanit, S.; Kokpol, S.; Hannongbua, S.
Source of high pathogenicity of an Avian influenza virus H5N1: Why H5 is better cleaved by furin
Biophys. J.
95
128-134
2008
Mus musculus
Pesu, M.; Muul, L.; Kanno, Y.; OShea, J.J.
Proprotein convertase furin is preferentially expressed in T helper 1 cells and regulates interferon gamma
Blood
108
983-985
2006
Homo sapiens, Mus musculus
Silvestri, L.; Pagani, A.; Camaschella, C.
Furin-mediated release of soluble hemojuvelin: a new link between hypoxia and iron homeostasis
Blood
111
924-931
2008
Mus musculus
Shiryaev, S.A.; Remacle, A.G.; Ratnikov, B.I.; Nelson, N.A.; Savinov, A.Y.; Wei, G.; Bottini, M.; Rega, M.F.; Parent, A.; Desjardins, R.; Fugere, M.; Day, R.; Sabet, M.; Pellecchia, M.; Liddington, R.C.; Smith, J.W.; Mustelin, T.; Guiney, D.G.; Lebl, M.; Strongin, A.Y.
Targeting host cell furin proprotein convertases as a therapeutic strategy against bacterial toxins and viral pathogens
J. Biol. Chem.
282
20847-20853
2007
Homo sapiens, Mus musculus, Mus musculus C57BL/6
Veit, G.; Zimina, E.P.; Franzke, C.W.; Kutsch, S.; Siebolds, U.; Gordon, M.K.; Bruckner-Tuderman, L.; Koch, M.
Shedding of collagen XXIII is mediated by furin and depends on the plasma membrane microenvironment
J. Biol. Chem.
282
27424-27435
2007
Mus musculus
Bruns, J.B.; Carattino, M.D.; Sheng, S.; Maarouf, A.B.; Weisz, O.A.; Pilewski, J.M.; Hughey, R.P.; Kleyman, T.R.
Epithelial Na+ channels are fully activated by furin- and prostasin-dependent release of an inhibitory peptide from the gamma-subunit
J. Biol. Chem.
282
6153-6160
2007
Homo sapiens, Mus musculus
Blanchet, M.H.; Le Good, J.A.; Mesnard, D.; Oorschot, V.; Baflast, S.; Minchiotti, G.; Klumperman, J.; Constam, D.B.
Cripto recruits Furin and PACE4 and controls Nodal trafficking during proteolytic maturation
EMBO J.
27
2580-2591
2008
Mus musculus
Gagliardo, B.; Kubat, N.; Faye, A.; Jaouen, M.; Durel, B.; Deschemin, J.C.; Canonne-Hergaux, F.; Sari, M.A.; Vaulont, S.
Pro-hepcidin is unable to degrade the iron exporter ferroportin unless maturated by a furin-dependent process
J. Hepatol.
50
394-401
2009
Homo sapiens, Mus musculus
Gagnon, J.; Mayne, J.; Mbikay, M.; Woulfe, J.; Chretien, M.
Expression of PCSK1 (PC1/3), PCSK2 (PC2) and PCSK3 (furin) in mouse small intestine
Regul. Pept.
152
54-60
2009
Mus musculus
Dragulescu-Andrasi, A.; Liang, G.; Rao, J.
In vivo bioluminescence imaging of furin activity in breast cancer cells using bioluminogenic substrates
Bioconjug. Chem.
20
1660-1666
2009
Homo sapiens, Mus musculus
Cousin, C.; Bracquart, D.; Contrepas, A.; Corvol, P.; Muller, L.; Nguyen, G.
Soluble form of the (pro)renin receptor generated by intracellular cleavage by furin is secreted in plasma
Hypertension
53
1077-1082
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Tian, S.; Jianhua, W.
Comparative study of the binding pockets of mammalian proprotein convertases and its implications for the design of specific small molecule inhibitors
Int. J. Biol. Sci.
6
89-95
2010
Mus musculus
Pavlaki, M.; Zucker, S.; Dufour, A.; Calabrese, N.; Bahou, W.; Cao, J.
Furin functions as a nonproteolytic chaperone for matrix metalloproteinase-28: MMP-28 propeptide sequence requirement
Biochem. Res. Int.
2011
630319
2011
Mus musculus
Kuester, M.; Becker, G.L.; Hardes, K.; Lindberg, I.; Steinmetzer, T.; Than, M.E.
Purification of the proprotein convertase furin by affinity chromatography based on PC-specific inhibitors
Biol. Chem.
392
973-981
2011
Mus musculus
Essalmani, R.; Susan-Resiga, D.; Chamberland, A.; Abifadel, M.; Creemers, J.W.; Boileau, C.; Seidah, N.G.; Prat, A.
In vivo evidence that furin from hepatocytes inactivates PCSK9
J. Biol. Chem.
286
4257-4263
2011
Mus musculus
Hajdin, K.; DAlessandro, V.; Niggli, F.K.; Schaefer, B.W.; Bernasconi, M.
Furin targeted drug delivery for treatment of rhabdomyosarcoma in a mouse model
PLoS ONE
5
e10445
2010
Homo sapiens, Mus musculus
Zhou, Z.; Zhang, Q.; Lu, X.; Wang, R.; Wang, H.; Wang, Y.L.; Zhu, C.; Lin, H.Y.; Wang, H.
The proprotein convertase furin is required for trophoblast syncytialization
Cell Death Dis.
4
e593-e602
2013
Mus musculus, Homo sapiens (P09958), Homo sapiens
Bessonnard, S.; Mesnard, D.; Constam, D.
PC7 and the related proteases Furin and Pace4 regulate E-cadherin function during blastocyst formation
J. Cell Biol.
210
1185-1197
2015
Mus musculus (P23188)
EXTERNAL LINKS (specific for EC-Number 3.4.21.75)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
