FURIN
entrez
5045
canonical
uniprot
P09958
canonical
ensembl
ENSG00000140564
resolver
ensp
ENSP00000268171
resolver
ensp
ENSP00000483552
resolver
ensp
ENSP00000484952
resolver
ensp
ENSP00000506143
resolver
ensp
ENSP00000523440
resolver
ensp
ENSP00000523443
resolver
ensp
ENSP00000523444
resolver
ensp
ENSP00000586081
resolver
ensp
ENSP00000586087
resolver
ensp
ENSP00000586088
resolver
ensp
ENSP00000794697
resolver
enst
ENST00000268171
resolver
enst
ENST00000610579
resolver
enst
ENST00000618099
resolver
enst
ENST00000680053
resolver
enst
ENST00000853381
resolver
enst
ENST00000853384
resolver
enst
ENST00000853385
resolver
enst
ENST00000916022
resolver
enst
ENST00000916028
resolver
enst
ENST00000916029
resolver
genesymbol
FURIN
resolver
genesymbol_syn
FUR
resolver
genesymbol_syn
PACE
resolver
genesymbol_syn
PCSK3
resolver
hgnc
HGNC:8568
resolver
uniprot
Q14336
resolver
uniprot
Q6LBS3
resolver
uniprot
Q9UCZ5
resolver
uniprot_entry
FURIN_HUMAN
resolver
uniprot_sec
Q14336
resolver
uniprot_sec
Q6LBS3
resolver
uniprot_sec
Q9UCZ5
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by the not secondly cleaved propeptide (PubMed:11799113, PubMed:9130696). Inhibited by m-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine (m-guanidinomethyl-Phac-RVR-Amb) and 4-guanidinomethyl-phenylacetyl-Arg-Tle-Arg-4-amidinobenzylamide (MI-1148) (PubMed:24666235, PubMed:25974265). Inhibited by Decanoyl-Arg-Val-Lys-Arg-chloromethylketone (decanoyl-RVKR-CMK) (PubMed:32362314). Inhibited by heparin/heparan sulfate-binding (PubMed:2408021). {ECO:0000269|PubMed:11799113, ECO:0000269|PubMed:2408021, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0000269|PubMed:32362314, ECO:0000269|PubMed:9130696}.
uniprot
proteins
amino_acid_sequence
MELRPWLLWVVAATGTLVLLAADAQGQKVFTNTWAVRIPGGPAVANSVARKHGFLNLGQIFGDYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEANNYGTLTKFTLVLYGTAPEGLPVPPESSGCKTLTSSQACVVCEEGFSLHQKSCVQHCPPGFAPQVLDTHYSTENDVETIRASVCAPCHASCATCQGPALTDCLSCPSHASLDPVEQTCSRQSQSSRESPPQQQPPRLPPEVEAGQRLRAGLLPSHLPEVVAGLSCAFIVLVFVTVFLVLQLRSGFSFRGVKVYTMDRGLISYKGLPPEAWQEECPSDSEEDEGRGERTAFIKDQSAL
uniprot
proteins
ec_number
3.4.21.75
uniprot
proteins
function
FUNCTION: Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif (PubMed:11799113, PubMed:1629222, PubMed:1713771, PubMed:2251280, PubMed:24666235, PubMed:25974265, PubMed:7592877, PubMed:7690548, PubMed:9130696). Mediates processing of TGFB1, an essential step in TGF-beta-1 activation (PubMed:7737999). Converts through proteolytic cleavage the non-functional Brain natriuretic factor prohormone into its active hormone BNP(1-32) (PubMed:20489134, PubMed:21763278). 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). {ECO:0000250|UniProtKB:P23188, ECO:0000269|PubMed:11799113, ECO:0000269|PubMed:1629222, ECO:0000269|PubMed:1713771, ECO:0000269|PubMed:20489134, ECO:0000269|PubMed:21763278, ECO:0000269|PubMed:2251280, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0000269|PubMed:7592877, ECO:0000269|PubMed:7690548, ECO:0000269|PubMed:7737999, ECO:0000269|PubMed:9130696}.; FUNCTION: (Microbial infection) Cleaves and activates diphtheria toxin DT. {ECO:0000269|PubMed:8253774}.; FUNCTION: (Microbial infection) Cleaves and activates anthrax toxin protective antigen (PA). {ECO:0000269|PubMed:1438214, ECO:0000269|PubMed:1644824}.; FUNCTION: (Microbial infection) Cleaves and activates HIV-1 virus Envelope glycoprotein gp160. {ECO:0000269|PubMed:31091448}.; FUNCTION: (Microbial infection) Required for H7N1 and H5N1 influenza virus infection probably by cleaving hemagglutinin. {ECO:0000269|PubMed:25974265}.; FUNCTION: (Microbial infection) Able to cleave S.pneumoniae serine-rich repeat protein PsrP. {ECO:0000269|PubMed:27582320}.; 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. {ECO:0000269|PubMed:32362314, ECO:0000269|PubMed:32703818}.; FUNCTION: (Microbial infection) Facilitates mumps virus infection by proteolytically cleaving the viral fusion protein F. {ECO:0000269|PubMed:32295904}.
uniprot
proteins
mass_dalton
86678
uniprot
proteins
mutagenesis
MUTAGEN 72; /note="V->R: Loss of catalytic activity and propeptide second cleavage and removal. Abnormal accumulation in the early secretory pathway."; /evidence="ECO:0000269|PubMed:11799113"; MUTAGEN 75; /note="R->A: Loss of catalytic activity and, propeptide second cleavage and removal. Normal trafficking to the Golgi."; /evidence="ECO:0000269|PubMed:11799113"; MUTAGEN 153; /note="D->N: Loss of catalytic activity and propeptide first cleavage. Abnormal accumulation in the early secretory pathway."; /evidence="ECO:0000269|PubMed:11799113, ECO:0000269|PubMed:9130696"; MUTAGEN 773..775; /note="SDS->DDD: Phosphomimetic mutant. Localization in early endosome is increased."; /evidence="ECO:0000269|PubMed:8846780"; MUTAGEN 773; /note="S->A: Slight reduction in phosphorylation. Loss of phosphorylation and abnormal accumulation in the early secretory pathway; when associated with A-775."; /evidence="ECO:0000269|PubMed:8846780"; MUTAGEN 775; /note="S->A: Slight reduction in phosphorylation. Loss of phosphorylation and abnormal accumulation in the early secretory pathway; when associated with A-773."; /evidence="ECO:0000269|PubMed:8846780
uniprot
proteins
post_translational_modification
PTM: The inhibition peptide, which plays the role of an intramolecular chaperone, is autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound to furin as a potent autoinhibitor. Following transport to the trans Golgi, a second cleavage within the inhibition propeptide results in propeptide dissociation and furin activation. {ECO:0000269|PubMed:1629222, ECO:0000269|PubMed:9130696}.; PTM: Phosphorylation is required for TGN localization of the endoprotease. In vivo, exists as di-, mono- and non-phosphorylated forms. {ECO:0000269|PubMed:8846780}.
uniprot
proteins
protein_family
Furin subfamily
uniprot
proteins
protein_family
Peptidase S8 family
uniprot
proteins
pubmed
11331585
uniprot
proteins
pubmed
11799113
uniprot
proteins
pubmed
1438214
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1629222
uniprot
proteins
pubmed
1644824
uniprot
proteins
pubmed
1713771
uniprot
proteins
pubmed
20489134
uniprot
proteins
pubmed
21763278
uniprot
proteins
pubmed
2251280
uniprot
proteins
pubmed
2408021
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24666235
uniprot
proteins
pubmed
25974265
uniprot
proteins
pubmed
2674906
uniprot
proteins
pubmed
27582320
uniprot
proteins
pubmed
3023061
uniprot
proteins
pubmed
31091448
uniprot
proteins
pubmed
32295904
uniprot
proteins
pubmed
32362314
uniprot
proteins
pubmed
32703818
uniprot
proteins
pubmed
32867305
uniprot
proteins
pubmed
34699015
uniprot
proteins
pubmed
7592877
uniprot
proteins
pubmed
7690548
uniprot
proteins
pubmed
7737999
uniprot
proteins
pubmed
8020465
uniprot
proteins
pubmed
8253774
uniprot
proteins
pubmed
8846780
uniprot
proteins
pubmed
9130696
uniprot
proteins
pubmed
9412467
uniprot
proteins
sequence_length
794
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:11331585, ECO:0000269|PubMed:11799113, ECO:0000269|PubMed:8846780, ECO:0000269|PubMed:9130696, ECO:0000269|PubMed:9412467}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:11799113, ECO:0000269|PubMed:9130696, ECO:0000269|PubMed:9412467}; Single-pass type I membrane protein {ECO:0000305}. Secreted {ECO:0000305|PubMed:11799113}. Endosome membrane {ECO:0000269|PubMed:9412467}; Single-pass type I membrane protein {ECO:0000305}. Note=Shuttles between the trans-Golgi network and the cell surface (PubMed:11799113, PubMed:9412467). Propeptide cleavage is a prerequisite for exit of furin molecules out of the endoplasmic reticulum (ER). A second cleavage within the propeptide occurs in the trans Golgi network (TGN), followed by the release of the propeptide and the activation of furin (PubMed:11799113). {ECO:0000269|PubMed:11799113, ECO:0000269|PubMed:9412467}.
uniprot
proteins
transmembrane_region
TRANSMEM 716..738; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins