Furin
entrez
54281
canonical
uniprot
P23377
canonical
ensembl
ENSRNOG00000011352
resolver
ensp
ENSRNOP00000015521
resolver
enst
ENSRNOT00000015521
resolver
genesymbol
Furin
resolver
genesymbol_syn
Fur
resolver
genesymbol_syn
Pcsk3
resolver
uniprot
G3V7I9
resolver
uniprot_entry
FURIN_RAT
resolver
uniprot_entry
G3V7I9_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by the not secondly cleaved propeptide (By similarity). 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) (By similarity). Inhibited by Decanoyl-Arg-Val-Lys-Arg-chloromethylketone (decanoyl-RVKR-CMK) (PubMed:9252368). Inhibited by heparin/heparan sulfate-binding (By similarity). {ECO:0000250|UniProtKB:P09958, ECO:0000269|PubMed:9252368}.
uniprot
proteins
amino_acid_sequence
MELRPWLLWVVAAAGALVLLAAEARGQKIFTNTWAVHISGGPAVADSVARKHGFHNLGQIFGDYYHFWHRAVTKRSLSPHRPRHSRLQRVPQVKWLEQQVAKQRAKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKEAWAQGFTGRGIVVSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKCIIEILAEPKDIGKRLEVRKTVTACLGEPNHISRLEHVQARLTLSYNRRGDLAIHLISPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEANNYGTLTKFTLVLYGTASEGLSAPPESSGCKTLTSSQACVVCEEGFSLHQKSCVQRCPPGFTPQVLDTHYSTENDVEIIRASVCTPCHASCATCQGPAPTDCLSCPSHASLDPVEQTCSRQSQSSRESRPQQPPPALRPEVEVEPRLRAGLASHLPEVLAGLSCLIIALIFGIVFLFLHRCSGFSFRGVKVYTMDRGLISYKGLPPEAWQEECPSDSEEDEGRGERTAFIKDQSAL
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:9252368). 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) (PubMed:9252368). 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:P09958, ECO:0000250|UniProtKB:P23188, ECO:0000269|PubMed:9252368}.
uniprot
proteins
mass_dalton
86653
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
2251148
uniprot
proteins
pubmed
9252368
uniprot
proteins
pubmed
9695949
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