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
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membrane-type
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subtilase
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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 (Engineering
Engineering on EC 3.4.21.75 - Furin
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D153N
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is catalytically inert, is efficiently synthesized but inefficiently processed and secreted and therefore is difficult to be purified. Is incapable of self-activation, is less active than the wild-type
D4K
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is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
G
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is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
G5
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is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
G6
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is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
H6
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is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
H66L
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profurin mutant, shows no measurable effect on propeptide excision relative to the control (65% mature furin). No effect on the pH-triggered activation and propeptide release or on the trypsin-mediated unmasking of furin
H69K
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profurin mutant, 80% reduced efficiency of propeptide excision, fails to be activated by acidic pH or trypsinolysis
H69L
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profurin mutant, 70% reduced efficiency of propeptide excision. Completely blocked ability of acid pH to trigger furin activation and propeptide cleavage but shows no effect on the trypsin-mediated activation step. Propeptide fails to dissociate from mature furin
K117P
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mutation does not affect the efficiency of autocatalytic processing and the resulting secretory mutants are capable of prodomain processing at the primary cleavage site Arg-Thr-Lys-Arg107-Asp108. Is readily isolated from the medium using metal-chelating chromatography, is less active than the wild-type
K74G/R75G
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secondary cleavage sites are inactivated, is incapable of self-activation
R1584A/R1585A
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mutations efficiently protect the C-propeptide cleavage from furin activity. In absence of furin activity, bone morphogenetic protein-1 is capable of processing the C-propeptide even though less efficiently than furin
R75A
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profurin mutant, substitution at the P1 position of the internal cleavage site, which blocks profurin activation but not propeptide excision or endoplasmic reticulum export of the furin-propeptide complex. No effect on the folding of the catalytic domain but blocked sensitivity of the furin-propeptide complex to acid pH
R89G
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efficiency of self-activation of the mutant in which the tertiary cleavage site (Arg-Leu-Gln-Arg89Q-Glu90) is inactivated, is significantly reduced compared to that of wild-type furin
DELTA759-780
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furin mutant lacking both the YKGL motif and the acidic cluster, shows low-affinity interactions with Mint3
DELTA769-780
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furin mutant with a deleted acidic cluster, shows low-affinity interactions with Mint3
R138A
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mutation of the furin cleavage site in the gamma subunit, gamma furin site mutation interfers with protein synthesis and/or degradation
R205A/R231A
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mutation of the furin cleavage site in the alpha subunit, eliminates the appearance of the 65-kDa cleavage product at the cell surface
additional information
additional information
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in furin-deficient DF11 cells, release of Borna disease virus particles induced by the treatment of Borna disease virus-infected cells with hypertonic buffer is not significantly affected, while virion infectivity is dramatically impaired, correlating with the decreased incorporation of Borna disease virus glycoprotein species into viral particles
additional information
loss of furin A function causes only a partial loss of endothelin 1 function. Furin A mutants typically have wild-type looking anterior arch ventral cartilages that are abnormally fused to dorsal cartilages. Cartilages of the posterior arches are also typically wild type, with a low penetrance of cartilage reduction observed in the third and fourth arches. Shape changes and bony fusions between the opercle and posterior branchiostegal ray, and altered muscle insertion points near joint domains. Arches fail to correctly undergo ventral elongation before skeletogenesis begins. Furin A mutants have defects in intermediate domain elements of the pharyngeal skeleton and mildly ruffled fins. Expression of endothelin 1-dependent genes is downregulated. Later in development, expression of most of these genes recovers to near wild-type levels
additional information
loss of furin A function causes only a partial loss of endothelin 1 function. Furin A mutants typically have wild-type looking anterior arch ventral cartilages that are abnormally fused to dorsal cartilages. Cartilages of the posterior arches are also typically wild type, with a low penetrance of cartilage reduction observed in the third and fourth arches. Shape changes and bony fusions between the opercle and posterior branchiostegal ray, and altered muscle insertion points near joint domains. Arches fail to correctly undergo ventral elongation before skeletogenesis begins. Furin A mutants have defects in intermediate domain elements of the pharyngeal skeleton and mildly ruffled fins. Expression of endothelin 1-dependent genes is downregulated. Later in development, expression of most of these genes recovers to near wild-type levels
additional information
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loss of furin A function causes only a partial loss of endothelin 1 function. Furin A mutants typically have wild-type looking anterior arch ventral cartilages that are abnormally fused to dorsal cartilages. Cartilages of the posterior arches are also typically wild type, with a low penetrance of cartilage reduction observed in the third and fourth arches. Shape changes and bony fusions between the opercle and posterior branchiostegal ray, and altered muscle insertion points near joint domains. Arches fail to correctly undergo ventral elongation before skeletogenesis begins. Furin A mutants have defects in intermediate domain elements of the pharyngeal skeleton and mildly ruffled fins. Expression of endothelin 1-dependent genes is downregulated. Later in development, expression of most of these genes recovers to near wild-type levels
additional information
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the zebrafish craniofacial mutant sturgeon in the proprotein convertase FurinA displays mild blisters in the median fin folds
additional information
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FD11 cell line, deficient in furin protease, processing of furin-site-containing glycoproteins is abrogated
additional information
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furin cleavage-site mutant, neither trifluoperazine-induced nor basal shedding causes P-stalk accumulation
additional information
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point mutations of sites A, B and C of furin P1A promoter. Mutations of site A and more importantly site B decreases Sox9-induced promoter activity, while mutations of both A and B sites result in only slight but nonsignificant additional inhibition. Mutation of site C does not reduce Sox9 activity
additional information
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construction of an immunoproapoptotic molecule with antitumor activity: Her2-antigen e23sFv-TD-tBID with a 10-amino acid residue furin cleavage sequence. Purified e23sFv-TD-tBID protein recognized breast cancer cells from patients and preserved the ability to kill HER2-positive tumor cells after incubation in human serum
additional information
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furin-deficient LoVo cells are uncapable to process pro-B-type natriuretic peptide, coexpression of human wild-type furin compensates and results in effective pro-B-type natriuretic peptide cleavage. Suppression of furin in HEK-293 cells by siRNA leads to the same result, overview
additional information
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knockdown of furin expression by siRNA significantly inhibits invasion and migration of HTR8/SVneo cells, with corresponding decrease of matrix metalloproteinase-9, MMP-9, activities. In contrast, overexpression of furin markedly increases cell invasion and migration, accompanied by significant increase of MMP-9 activities. Furthermore, furin siRNA significantly increases the levels of both tissue inhibitors of MMPs, TIMP-1 and -2, overview. Proliferation of HTR8/SVneo cells is inhibited by furin siRNA
additional information
enhancement of productive IBV infection by knockin of furin in A-549 cells
additional information
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enhancement of productive IBV infection by knockin of furin in A-549 cells
additional information
furin siRNA efficiently inhibits furin expression, expression of enzyme-specific siRNA in choriocarcinoma cells inhibits cell fusion
additional information
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furin siRNA efficiently inhibits furin expression, expression of enzyme-specific siRNA in choriocarcinoma cells inhibits cell fusion
additional information
knockdown of the enzyme expression in C8161.9, MelJuSo, and HeLa cells by shRNA
additional information
engineering of the human furin gene for expression in plants, the production of a functional active recombinant truncated human furin in Nicotiana benthamiana plants. The signal peptide (amino acids 1-25) is removed from the furin sequence, and Nicotiana tabacum PR-1a signal peptide (MGFVLFSQLPSFLLVSTLLLFLVISHSCRA) is added to the N-terminus. The KDEL sequence (the endoplasmic reticulum retention signal) and the His6 tag (the affinity purification tag) are added to the C-terminus. A truncated form of furin (amino acids 26-595) is expressed with a PR-1a signal peptide at N-terminus and His6-KDEL at C-terminus
additional information
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engineering of the human furin gene for expression in plants, the production of a functional active recombinant truncated human furin in Nicotiana benthamiana plants. The signal peptide (amino acids 1-25) is removed from the furin sequence, and Nicotiana tabacum PR-1a signal peptide (MGFVLFSQLPSFLLVSTLLLFLVISHSCRA) is added to the N-terminus. The KDEL sequence (the endoplasmic reticulum retention signal) and the His6 tag (the affinity purification tag) are added to the C-terminus. A truncated form of furin (amino acids 26-595) is expressed with a PR-1a signal peptide at N-terminus and His6-KDEL at C-terminus
additional information
expression and purification of nonglycosylated human furin using the BacMam technology and site-directed mutagenesis of the glycosylation sites. Recombinant nonglycosylated furin produced using this system retains full proteolytic activity indistinguishable from that of the glycosylated protein
additional information
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expression and purification of nonglycosylated human furin using the BacMam technology and site-directed mutagenesis of the glycosylation sites. Recombinant nonglycosylated furin produced using this system retains full proteolytic activity indistinguishable from that of the glycosylated protein
additional information
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LoVo/neo cells lacking functional furin are unable to activate both wild type Shiga toxin and mutant Shiga-2D toxin
additional information
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deletion of the cysteine-rich domain and the cytoplasmic tail of furin does not abolish binding to cripto
additional information
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production of lentiviruses carrying shRNA for furin and infection of blastocyststage embryos with the viruses, along with lentiviruses expressing EGFP
additional information
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the binding efficiency of the furin mutants LI/AN Y/A and LI/AN F/N Y/A to Mint3 decrease
additional information
truncated mutant, lacking Cys-rich repeated segments
additional information
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truncated mutant, lacking Cys-rich repeated segments
additional information
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furin antisense expression leading to furin depletionin oocytes is accompanied by a corresponding decrease in the levels of both the fully cleaved prodomain and mature BMP4
