Furin
entrez
18550
canonical
uniprot
P23188
canonical
ensembl
ENSMUSG00000030530
resolver
ensp
ENSMUSP00000102985
resolver
ensp
ENSMUSP00000113370
resolver
ensp
ENSMUSP00000113793
resolver
ensp
ENSMUSP00000231106
resolver
ensp
ENSMUSP00000231107
resolver
ensp
ENSMUSP00000231113
resolver
ensp
ENSMUSP00000231114
resolver
enst
ENSMUST00000107362
resolver
enst
ENSMUST00000120753
resolver
enst
ENSMUST00000122232
resolver
genesymbol
Furin
resolver
genesymbol_syn
Fur
resolver
genesymbol_syn
Pcsk3
resolver
uniprot
Q6GTN6
resolver
uniprot_entry
FURIN_MOUSE
resolver
uniprot_sec
Q6GTN6
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by the not secondly cleaved propeptide. 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). Inhibited by Decanoyl-Arg-Val-Lys-Arg-chloromethylketone (decanoyl-RVKR-CMK). Inhibited by heparin/heparan sulfate-binding. {ECO:0000250|UniProtKB:P09958}.
uniprot
proteins
amino_acid_sequence
MELRSWLLWVVAAAGAVVLLAADAQGQKIFTNTWAVHIPGGPAVADRVAQKHGFHNLGQIFGDYYHFWHRAVTKRSLSPHRPRHSRLQREPQVKWLEQQVAKRRAKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKEAWAQGFTGHGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNADDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIVEILVEPKDIGKRLEVRKAVTACLGEPNHITRLEHVQARLTLSYNRRGDLAIHLISPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPAGEWVLEIENTSEANNYGTLTKFTLVLYGTAPEGLSTPPESSGCKTLTSSQACVVCEEGYSLHQKSCVQHCPPGFIPQVLDTHYSTENDVEIIRASVCTPCHASCATCQGPAPTDCLSCPSHASLDPVEQTCSRQSQSSRESRPQQQPPALRPEVEMEPRLQAGLASHLPEVLAGLSCLIIVLIFGIVFLFLHRCSGFSFRGVKVYTMDRGLISYKGLPPEAWQEECPSDSEEDEGRGERTAFIKDQSAL
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:18713856). Mediates processing of TGFB1, an essential step in TGF-beta-1 activation (By similarity). Converts through proteolytic cleavage the non-functional Brain natriuretic factor prohormone into its active hormone BNP(1-45) (By similarity). 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 (PubMed:18713856). {ECO:0000250|UniProtKB:P09958, ECO:0000269|PubMed:18713856}.
uniprot
proteins
mass_dalton
86772
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:0000250|UniProtKB:P09958}.; PTM: Phosphorylation is required for TGN localization of the endoprotease. In vivo, exists as di-, mono- and non-phosphorylated forms. {ECO:0000250|UniProtKB:P09958}.
uniprot
proteins
protein_family
Furin subfamily
uniprot
proteins
protein_family
Peptidase S8 family
uniprot
proteins
pubmed
12794637
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18713856
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
2266110
uniprot
proteins
pubmed
9412467
uniprot
proteins
sequence_length
793
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P09958}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P09958}; Single-pass type I membrane protein {ECO:0000305}. Secreted {ECO:0000250|UniProtKB:Q28193}. Endosome membrane {ECO:0000250|UniProtKB:P09958}; Single-pass type I membrane protein {ECO:0000305}. Note=Shuttles between the trans-Golgi network and the cell surface. 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. {ECO:0000250|UniProtKB:P09958}.
uniprot
proteins
transmembrane_region
TRANSMEM 715..735; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins