FURIN report

I. Expression across cell types

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of FURIN at tissue level.

III. Associated gene sets

GO_0006465Biological processsignal peptide processing
GO_0032804Biological processnegative regulation of low-density lipoprotein particle receptor catabolic process
GO_0009966Biological processregulation of signal transduction
GO_0042176Biological processregulation of protein catabolic process
GO_0051044Biological processpositive regulation of membrane protein ectodomain proteolysis
GO_0032374Biological processregulation of cholesterol transport
GO_0019081Biological processviral translation
GO_0034369Biological processplasma lipoprotein particle remodeling
GO_0016486Biological processpeptide hormone processing
GO_0030198Biological processextracellular matrix organization
GO_0016485Biological processprotein processing
GO_0022617Biological processextracellular matrix disassembly
GO_0046598Biological processpositive regulation of viral entry into host cell
GO_0043043Biological processpeptide biosynthetic process
GO_0032911Biological processnegative regulation of transforming growth factor beta1 production
GO_0002862Biological processnegative regulation of inflammatory response to antigenic stimulus
GO_0030574Biological processcollagen catabolic process
GO_0031638Biological processzymogen activation
GO_0090472Biological processdibasic protein processing
GO_0032940Biological processsecretion by cell
GO_1990000Biological processamyloid fibril formation
GO_0032904Biological processnegative regulation of nerve growth factor production
GO_0019082Biological processviral protein processing
GO_0019058Biological processviral life cycle
GO_0140447Biological processcytokine precursor processing
GO_0001825Biological processblastocyst formation
GO_0007179Biological processtransforming growth factor beta receptor signaling pathway
GO_0032902Biological processnerve growth factor production
GO_0052548Biological processregulation of endopeptidase activity
GO_0051604Biological processprotein maturation
GO_0005615Cellular componentextracellular space
GO_0005576Cellular componentextracellular region
GO_0005886Cellular componentplasma membrane
GO_0045121Cellular componentmembrane raft
GO_0016020Cellular componentmembrane
GO_0005796Cellular componentGolgi lumen
GO_0070062Cellular componentextracellular exosome
GO_0005802Cellular componenttrans-Golgi network
GO_0009986Cellular componentcell surface
GO_0000139Cellular componentGolgi membrane
GO_0005783Cellular componentendoplasmic reticulum
GO_0030140Cellular componenttrans-Golgi network transport vesicle
GO_0010008Cellular componentendosome membrane
GO_0008201Molecular functionheparin binding
GO_0008233Molecular functionpeptidase activity
GO_0004175Molecular functionendopeptidase activity
GO_0042277Molecular functionpeptide binding
GO_0004867Molecular functionserine-type endopeptidase inhibitor activity
GO_1904399Molecular functionheparan sulfate binding
GO_0002020Molecular functionprotease binding
GO_0008236Molecular functionserine-type peptidase activity
GO_0046872Molecular functionmetal ion binding
GO_0048406Molecular functionnerve growth factor binding
GO_0005515Molecular functionprotein binding
GO_0004252Molecular functionserine-type endopeptidase activity

IV. Literature review

[source]
Gene nameFURIN
Protein nameFurin (EC 3.4.21.75) (Dibasic-processing enzyme) (Paired basic amino acid residue-cleaving enzyme) (PACE)
furin (EC 3.4.21.75) (Dibasic-processing enzyme) (Paired basic amino acid residue-cleaving enzyme)
Furin, paired basic amino acid cleaving enzyme
SynonymsPCSK3
PACE
FUR
DescriptionFUNCTION: Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif . Mediates processing of TGFB1, an essential step in TGF-beta-1 activation . Converts through proteolytic cleavage the non-functional Brain natriuretic factor prohormone into its active hormone BNP(1-32) . By mediating processing of accessory subunit ATP6AP1/Ac45 of the V-ATPase, regulates the acidification of dense-core secretory granules in islets of Langerhans cells (By similarity). .; FUNCTION: (Microbial infection) Cleaves and activates diphtheria toxin DT. .; FUNCTION: (Microbial infection) Cleaves and activates anthrax toxin protective antigen (PA). .; FUNCTION: (Microbial infection) Cleaves and activates HIV-1 virus Envelope glycoprotein gp160. .; FUNCTION: (Microbial infection) Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin. .; FUNCTION: (Microbial infection) Able to cleave S.pneumoniae serine-rich repeat protein PsrP. .; FUNCTION: (Microbial infection) Facilitates human coronaviruses EMC and SARS-CoV-2 infections by proteolytically cleaving the spike protein at the monobasic S1/S2 cleavage site. This cleavage is essential for spike protein-mediated cell-cell fusion and entry into human lung cells. .; FUNCTION: (Microbial infection) Facilitates mumps virus infection by proteolytically cleaving the viral fusion protein F. .

AccessionsENST00000681865.1
A0A7P0T9X7
A0A7P0T8U2
ENST00000268171.8
ENST00000680687.1
H0YNB5
ENST00000558794.1
ENST00000680053.1
P09958
ENST00000681804.1
ENST00000610579.4
ENST00000618099.4
A0A7P0T8P1