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 (Localization
Localization on EC 3.4.21.75 - Furin
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LOCALIZATION 
ORGANISM
UNIPROT
COMMENTARY 
GeneOntology No.
LITERATURE
SOURCE
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furin-propeptide complex is restricted to the endoplasmic reticulum by a PACS-2- and COPI-dependent mechanism. His69 is a pH sensor that allows enzyme activation following transport of the furin-propeptide complex from the endoplasmic reticulum to the mildly acidic TGN/endosomal system
the enzyme contains a signal peptide (amino acids 1-25) and is secreted
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additional information
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hypoxia triggers relocalization of furin from the trans-Golgi network to endosomomal compartments and the cell surface in cancer cells
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furin localizes to endosomes when Mint3 expression is knocked down
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hypoxia triggers relocalization of furin from the trans-Golgi network to endosomomal compartments and the cell surface in cancer cells
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furin is primarily located in the Golgi and trans-Golgi network, and it can also circulate between the cell surface and the trans-Golgi network
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interaction between the phosphotyrosine-binding domain of Mint3 and the acidic peptide signal in the cytoplasmic domain of furin regulates the specific localization of furin in the trans-Golgi network. The phosphotyrosine-binding domain of Mint3 is essential for furin-Mint3 interaction
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the membrane-bound enzyme undergoes post-translational processing to produce a soluble form of the enzyme that can be secreted
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cleavage of the furin propeptide occurs in the endoplasmic reticulum and is necessary but not sufficient for transport of furin out of this compartment
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cleavage of the furin propeptide occurs in the endoplasmic reticulum and is necessary but not sufficient for transport of furin out of this compartment
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human, mainly, the enzyme can translocate between the cell surface and the trans-Golgi network
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knockdown of Mint3 increases the distribution of furin at the membrane
additional information
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furin is present both in the intracellular secretory pathway and at the cell surface
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additional information
furin is a protease localized in the trans-Golgi network and in late endocytic compartments
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additional information
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furin is a protease localized in the trans-Golgi network and in late endocytic compartments
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additional information
complementary subcellular distribution of bioactive furin and proprotein convertase PC7. Furin activity in endosomes is 10fold less inhibited by decanoyl-RVKR-chloromethylketone and enriched over 3fold in endosomes compared to the trans-Golgi network. Development of targeted compartment-specific biosensors. Endogenous PC7, which resists the inhibitor, is active in distinct vesicles. The distribution of proprotein convertase activities at the tissue level are monitored by introduction of biosensor CLIP (cell-linked indicator of proteolysis). CLIP v.3 is suitable for ratiometric imaging without interference by FRET and can estimate PC activity in exocytic compartments, whereas CLIP v.4 can be used as a FRET-based biosensor to quantify PC activities in specific intracellular vesicles. Fusion to the cytosolic tail of PC7 directs CLIP v.4 to compartments that harbor furin activity, but not full-length PC7
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additional information
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localization of furin predominantly outside lipid rafts
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