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Furin (EC 3.4.21.75) (Dibasic-processing enzyme) (Paired basic amino acid residue-cleaving enzyme) (PACE)

 FURIN_HUMAN             Reviewed;         794 AA.
P09958; Q14336; Q6LBS3; Q9UCZ5;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 2.
30-AUG-2017, entry version 211.
RecName: Full=Furin;
EC=3.4.21.75 {ECO:0000269|PubMed:11799113, ECO:0000269|PubMed:1629222, ECO:0000269|PubMed:1713771, ECO:0000269|PubMed:2251280, ECO:0000269|PubMed:25974265, ECO:0000269|PubMed:7592877, ECO:0000269|PubMed:7690548, ECO:0000269|PubMed:9130696};
AltName: Full=Dibasic-processing enzyme;
AltName: Full=Paired basic amino acid residue-cleaving enzyme;
Short=PACE;
Flags: Precursor;
Name=FURIN; Synonyms=FUR, PACE, PCSK3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Blood;
PubMed=2408021; DOI=10.1093/nar/18.3.664;
van den Ouweland A.M.W., van Duijnhoven H.L.P., Keizer G.D.,
Dorssers L.C.J., van de Ven W.J.M.;
"Structural homology between the human fur gene product and the
subtilisin-like protease encoded by yeast KEX2.";
Nucleic Acids Res. 18:664-664(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=2251280; DOI=10.1073/pnas.87.23.9378;
Wise R.J., Barr P.J., Wong P.A., Kiefer M.C., Brake A.J.,
Kaufman R.J.;
"Expression of a human proprotein processing enzyme: correct cleavage
of the von Willebrand factor precursor at a paired basic amino acid
site.";
Proc. Natl. Acad. Sci. U.S.A. 87:9378-9382(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
SPECIFICITY.
PubMed=1713771; DOI=10.1089/dna.1991.10.319;
Barr P.J., Mason O.B., Landsberg K.E., Wong P.A., Kiefer M.C.,
Brake A.J.;
"cDNA and gene structure for a human subtilisin-like protease with
cleavage specificity for paired basic amino acid residues.";
DNA Cell Biol. 10:319-328(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-280.
PubMed=2674906; DOI=10.1093/nar/17.17.7101;
Van den Ouweland A.M.W., van Groningen J.J.M., Roebrock A.J.M.,
Onnekink C., Van de Ven W.J.M.;
"Nucleotide sequence analysis of the human fur gene.";
Nucleic Acids Res. 17:7101-7102(1989).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 296-794.
PubMed=3023061;
Roebroek A.J.M., Schalken J.A., Leunissen J.A.M., Onnekink C.,
Bloemers H.P.J., van de Ven W.J.M.;
"Evolutionary conserved close linkage of the c-fes/fps proto-oncogene
and genetic sequences encoding a receptor-like protein.";
EMBO J. 5:2197-2202(1986).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 402-428, FUNCTION, AND CATALYTIC
ACTIVITY.
TISSUE=Colon carcinoma;
PubMed=7690548; DOI=10.1006/bbrc.1993.2146;
Takahashi S., Kasai K., Hatsuzawa K., Kitamura N., Misumi Y.,
Ikehara Y., Murakami K., Nakayama K.;
"A mutation of furin causes the lack of precursor-processing activity
in human colon carcinoma LoVo cells.";
Biochem. Biophys. Res. Commun. 195:1019-1026(1993).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 527-553, FUNCTION, CATALYTIC ACTIVITY,
AND VARIANT ARG-547.
TISSUE=Colon carcinoma;
PubMed=7592877; DOI=10.1074/jbc.270.44.26565;
Takahashi S., Nakagawa T., Kasai K., Banno T., Duguay S.J.,
Van de Ven W.J.M., Murakami K., Nakayama K.;
"A second mutant allele of furin in the processing-incompetent cell
line, LoVo. Evidence for involvement of the homo B domain in
autocatalytic activation.";
J. Biol. Chem. 270:26565-26569(1995).
[9]
FUNCTION, CATALYTIC ACTIVITY, AND PROTEOLYTIC PROCESSING.
PubMed=1629222;
Leduc R., Molloy S.S., Thorne B.A., Thomas G.;
"Activation of human furin precursor processing endoprotease occurs by
an intramolecular autoproteolytic cleavage.";
J. Biol. Chem. 267:14304-14308(1992).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
3D-STRUCTURE MODELING OF CATALYTIC DOMAIN.
PubMed=8020465; DOI=10.1111/j.1432-1033.1994.tb18864.x;
Siezen R.J., Creemers J.W.M., van de Ven W.J.M.;
"Homology modelling of the catalytic domain of human furin. A model
for the eukaryotic subtilisin-like proprotein convertases.";
Eur. J. Biochem. 222:255-266(1994).
[12]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-773 AND SER-775, MOTIF,
AND MUTAGENESIS OF SER-773 AND SER-775.
PubMed=8846780;
Jones B.G., Thomas L., Molloy S.S., Thulin C.D., Fry M.D., Walsh K.A.,
Thomas G.;
"Intracellular trafficking of furin is modulated by the
phosphorylation state of a casein kinase II site in its cytoplasmic
tail.";
EMBO J. 14:5869-5883(1995).
[13]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, PROTEOLYTIC
CLEAVAGE, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF
ASP-153.
PubMed=9130696; DOI=10.1093/emboj/16.7.1508;
Anderson E.D., VanSlyke J.K., Thulin C.D., Jean F., Thomas G.;
"Activation of the furin endoprotease is a multiple-step process:
requirements for acidification and internal propeptide cleavage.";
EMBO J. 16:1508-1518(1997).
[14]
SUBCELLULAR LOCATION.
PubMed=9412467; DOI=10.1083/jcb.139.7.1719;
Liu G., Thomas L., Warren R.A., Enns C.A., Cunningham C.C.,
Hartwig J.H., Thomas G.;
"Cytoskeletal protein ABP-280 directs the intracellular trafficking of
furin and modulates proprotein processing in the endocytic pathway.";
J. Cell Biol. 139:1719-1733(1997).
[15]
INTERACTION WITH PACS1, AND SUBCELLULAR LOCATION.
PubMed=11331585; DOI=10.1093/emboj/20.9.2191;
Crump C.M., Xiang Y., Thomas L., Gu F., Austin C., Tooze S.A.,
Thomas G.;
"PACS-1 binding to adaptors is required for acidic cluster motif-
mediated protein traffic.";
EMBO J. 20:2191-2201(2001).
[16]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, SUBCELLULAR LOCATION,
AND MUTAGENESIS OF VAL-72; ARG-75 AND ASP-153.
PubMed=11799113; DOI=10.1074/jbc.M108740200;
Anderson E.D., Molloy S.S., Jean F., Fei H., Shimamura S., Thomas G.;
"The ordered and compartment-specfific autoproteolytic removal of the
furin intramolecular chaperone is required for enzyme activation.";
J. Biol. Chem. 277:12879-12890(2002).
[17] {ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 108-574 IN COMPLEX WITH
CALCIUM AND INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, ENZYME
REGULATION, AND DISULFIDE BONDS.
PubMed=24666235; DOI=10.1021/cb500087x;
Dahms S.O., Hardes K., Becker G.L., Steinmetzer T., Brandstetter H.,
Than M.E.;
"X-ray structures of human furin in complex with competitive
inhibitors.";
ACS Chem. Biol. 9:1113-1118(2014).
[18] {ECO:0000244|PDB:4RYD}
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 108-574 IN COMPLEX WITH
CALCIUM AND INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, ENZYME
REGULATION, AND DISULFIDE BONDS.
PubMed=25974265; DOI=10.1002/cmdc.201500103;
Hardes K., Becker G.L., Lu Y., Dahms S.O., Kohler S., Beyer W.,
Sandvig K., Yamamoto H., Lindberg I., Walz L., von Messling V.,
Than M.E., Garten W., Steinmetzer T.;
"Novel Furin inhibitors with potent anti-infectious activity.";
ChemMedChem 10:1218-1231(2015).
-!- FUNCTION: Furin is likely to represent the ubiquitous endoprotease
activity within constitutive secretory pathways and capable of
cleavage at the RX(K/R)R consensus motif.
{ECO:0000269|PubMed:11799113, ECO:0000269|PubMed:1629222,
ECO:0000269|PubMed:1713771, ECO:0000269|PubMed:2251280,
ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265,
ECO:0000269|PubMed:7592877, ECO:0000269|PubMed:7690548,
ECO:0000269|PubMed:9130696}.
-!- FUNCTION: (Microbial infection) Probably cleaves and activates
anthrax and diphtheria toxins. Required for H7N1 and H5N1
influenza virus infection probably by cleaving hemagglutinin.
{ECO:0000269|PubMed:25974265}.
-!- CATALYTIC ACTIVITY: Release of mature proteins from their
proproteins by cleavage of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where
Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin,
complement component C3 and von Willebrand factor from their
respective precursors. {ECO:0000269|PubMed:11799113,
ECO:0000269|PubMed:1629222, ECO:0000269|PubMed:1713771,
ECO:0000269|PubMed:2251280, ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265, ECO:0000269|PubMed:7592877,
ECO:0000269|PubMed:7690548, ECO:0000269|PubMed:9130696}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265, ECO:0000269|PubMed:9130696};
Note=Binds 3 calcium ions per subunit.
{ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265,
ECO:0000269|PubMed:9130696};
-!- ENZYME REGULATION: Inhibited by the not secondly cleaved
propeptide (PubMed:9130696, PubMed:11799113). Inhibited by m-
guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine
(m-guanidinomethyl-Phac-RVR-Amb) and 4-guanidinomethyl-
phenylacteyl-Arg-Tle-Arg-4-amidinobenzylamide (MI-1148)
(PubMed:24666235, PubMed:25974265). {ECO:0000269|PubMed:11799113,
ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265,
ECO:0000269|PubMed:9130696}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6.0. {ECO:0000269|PubMed:9130696};
-!- SUBUNIT: Interacts with FLNA (By similarity). Binds to PACS1 which
mediates TGN localization and connection to clathrin adapters
(PubMed:11331585). {ECO:0000250|UniProtKB:P23188,
ECO:0000269|PubMed:11331585}.
-!- INTERACTION:
O14793:MSTN; NbExp=2; IntAct=EBI-1056807, EBI-8542977;
-!- 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:9412467, PubMed:11799113).
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}.
-!- TISSUE SPECIFICITY: Seems to be expressed ubiquitously.
{ECO:0000269|PubMed:1713771}.
-!- DOMAIN: Contains a cytoplasmic domain responsible for its TGN
localization and recycling from the cell surface.
{ECO:0000269|PubMed:8846780}.
-!- 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}.
-!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FURINID40646ch15q26.html";
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EMBL; X17094; CAA34948.1; -; mRNA.
EMBL; BC012181; AAH12181.1; -; mRNA.
EMBL; X15723; CAA33745.1; -; Genomic_DNA.
EMBL; X04329; CAA27860.1; -; Genomic_DNA.
CCDS; CCDS10364.1; -.
PIR; A39552; KXHUF.
RefSeq; NP_001276752.1; NM_001289823.1.
RefSeq; NP_001276753.1; NM_001289824.1.
RefSeq; NP_002560.1; NM_002569.3.
UniGene; Hs.513153; -.
PDB; 4OMC; X-ray; 2.30 A; A/B/C/D/E/F=108-574.
PDB; 4OMD; X-ray; 2.70 A; A/B/C/D/E/F=108-574.
PDB; 4RYD; X-ray; 2.15 A; A/B/C/D/E/F=108-574.
PDB; 4Z2A; X-ray; 1.89 A; A=110-574.
PDB; 5JMO; X-ray; 2.00 A; A/B=108-574.
PDB; 5JXG; X-ray; 1.80 A; A=108-574.
PDB; 5JXH; X-ray; 2.00 A; A=108-574.
PDB; 5JXI; X-ray; 2.00 A; A=108-574.
PDB; 5JXJ; X-ray; 2.00 A; A=108-574.
PDB; 5MIM; X-ray; 1.90 A; A=108-574.
PDBsum; 4OMC; -.
PDBsum; 4OMD; -.
PDBsum; 4RYD; -.
PDBsum; 4Z2A; -.
PDBsum; 5JMO; -.
PDBsum; 5JXG; -.
PDBsum; 5JXH; -.
PDBsum; 5JXI; -.
PDBsum; 5JXJ; -.
PDBsum; 5MIM; -.
ProteinModelPortal; P09958; -.
SMR; P09958; -.
BioGrid; 111082; 40.
DIP; DIP-29904N; -.
ELM; P09958; -.
IntAct; P09958; 11.
MINT; MINT-1209355; -.
STRING; 9606.ENSP00000268171; -.
BindingDB; P09958; -.
ChEMBL; CHEMBL2611; -.
DrugBank; DB03600; Decanoic Acid.
DrugBank; DB04951; Pirfenidone.
GuidetoPHARMACOLOGY; 2366; -.
MEROPS; S08.071; -.
iPTMnet; P09958; -.
PhosphoSitePlus; P09958; -.
BioMuta; FURIN; -.
DMDM; 120611; -.
OGP; P09958; -.
EPD; P09958; -.
MaxQB; P09958; -.
PaxDb; P09958; -.
PeptideAtlas; P09958; -.
PRIDE; P09958; -.
Ensembl; ENST00000268171; ENSP00000268171; ENSG00000140564.
Ensembl; ENST00000610579; ENSP00000484952; ENSG00000140564.
Ensembl; ENST00000618099; ENSP00000483552; ENSG00000140564.
GeneID; 5045; -.
KEGG; hsa:5045; -.
UCSC; uc002bpu.2; human.
CTD; 5045; -.
DisGeNET; 5045; -.
GeneCards; FURIN; -.
HGNC; HGNC:8568; FURIN.
HPA; CAB009499; -.
MIM; 136950; gene.
neXtProt; NX_P09958; -.
OpenTargets; ENSG00000140564; -.
PharmGKB; PA32894; -.
eggNOG; KOG3525; Eukaryota.
eggNOG; COG1404; LUCA.
eggNOG; COG4935; LUCA.
GeneTree; ENSGT00750000117358; -.
HOGENOM; HOG000192536; -.
HOVERGEN; HBG008705; -.
InParanoid; P09958; -.
KO; K01349; -.
OMA; PRPHDYS; -.
OrthoDB; EOG091G05HI; -.
PhylomeDB; P09958; -.
TreeFam; TF314277; -.
Reactome; R-HSA-1181150; Signaling by NODAL.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1566948; Elastic fibre formation.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-HSA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
Reactome; R-HSA-167060; NGF processing.
Reactome; R-HSA-171286; Synthesis and processing of ENV and VPU.
Reactome; R-HSA-186797; Signaling by PDGF.
Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi.
Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
Reactome; R-HSA-5210891; Uptake and function of anthrax toxins.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
Reactome; R-HSA-8963889; Assembly of active LPL and LIPC lipase complexes.
Reactome; R-HSA-977225; Amyloid fiber formation.
SignaLink; P09958; -.
SIGNOR; P09958; -.
ChiTaRS; FURIN; human.
GeneWiki; Furin; -.
GenomeRNAi; 5045; -.
PMAP-CutDB; P09958; -.
PRO; PR:P09958; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000140564; -.
CleanEx; HS_FURIN; -.
ExpressionAtlas; P09958; baseline and differential.
Genevisible; P09958; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IGI:BHF-UCL.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; IMP:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005802; C:trans-Golgi network; IDA:BHF-UCL.
GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:MGI.
GO; GO:0004175; F:endopeptidase activity; IDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0048406; F:nerve growth factor binding; IDA:BHF-UCL.
GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO; GO:0042277; F:peptide binding; IDA:BHF-UCL.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:BHF-UCL.
GO; GO:0008283; P:cell proliferation; IMP:BHF-UCL.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0090472; P:dibasic protein processing; IMP:UniProtKB.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0032804; P:negative regulation of low-density lipoprotein particle receptor catabolic process; IDA:HGNC.
GO; GO:0032911; P:negative regulation of transforming growth factor beta1 production; IMP:BHF-UCL.
GO; GO:0032455; P:nerve growth factor processing; TAS:Reactome.
GO; GO:0032902; P:nerve growth factor production; IDA:BHF-UCL.
GO; GO:0043043; P:peptide biosynthetic process; IDA:BHF-UCL.
GO; GO:0016486; P:peptide hormone processing; IDA:BHF-UCL.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IC:BHF-UCL.
GO; GO:0016485; P:protein processing; IDA:UniProtKB.
GO; GO:0052548; P:regulation of endopeptidase activity; IDA:BHF-UCL.
GO; GO:0051004; P:regulation of lipoprotein lipase activity; TAS:Reactome.
GO; GO:0045714; P:regulation of low-density lipoprotein particle receptor biosynthetic process; IEA:Ensembl.
GO; GO:0042176; P:regulation of protein catabolic process; IMP:BHF-UCL.
GO; GO:0009966; P:regulation of signal transduction; IEA:Ensembl.
GO; GO:0032940; P:secretion by cell; IDA:BHF-UCL.
GO; GO:0006465; P:signal peptide processing; IDA:HGNC.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO; GO:0019058; P:viral life cycle; IEP:BHF-UCL.
GO; GO:0019082; P:viral protein processing; TAS:Reactome.
GO; GO:0031638; P:zymogen activation; IMP:UniProtKB.
GO; GO:0097341; P:zymogen inhibition; IMP:UniProtKB.
CDD; cd04059; Peptidases_S8_Protein_converta; 1.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR008979; Galactose-bd-like.
InterPro; IPR009030; Growth_fac_rcpt_.
InterPro; IPR034182; Kexin/furin.
InterPro; IPR009020; Peptidase/Inhibitor_I9.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR023827; Peptidase_S8_Asp-AS.
InterPro; IPR022398; Peptidase_S8_His-AS.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR002884; PrprotnconvertsP.
InterPro; IPR032815; S8_pro-domain.
Pfam; PF01483; P_proprotein; 1.
Pfam; PF00082; Peptidase_S8; 1.
Pfam; PF16470; S8_pro-domain; 1.
PRINTS; PR00723; SUBTILISIN.
SMART; SM00261; FU; 2.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF52743; SSF52743; 1.
SUPFAM; SSF54897; SSF54897; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS51829; P_HOMO_B; 1.
PROSITE; PS00136; SUBTILASE_ASP; 1.
PROSITE; PS00137; SUBTILASE_HIS; 1.
PROSITE; PS00138; SUBTILASE_SER; 1.
1: Evidence at protein level;
3D-structure; Autocatalytic cleavage; Calcium; Cell membrane;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Endosome; Glycoprotein; Golgi apparatus; Hydrolase; Membrane;
Metal-binding; Phosphoprotein; Polymorphism; Protease;
Reference proteome; Repeat; Secreted; Serine protease; Signal;
Transmembrane; Transmembrane helix; Zymogen.
SIGNAL 1 26 {ECO:0000255}.
PROPEP 27 107 Inhibition peptide.
{ECO:0000269|PubMed:9130696}.
/FTId=PRO_0000027028.
CHAIN 108 794 Furin.
/FTId=PRO_0000027029.
TOPO_DOM 108 715 Lumenal. {ECO:0000305}.
TRANSMEM 716 738 Helical. {ECO:0000255}.
TOPO_DOM 739 794 Cytoplasmic. {ECO:0000305}.
DOMAIN 144 427 Peptidase S8. {ECO:0000255}.
DOMAIN 444 576 P/Homo B. {ECO:0000255|PROSITE-
ProRule:PRU01173}.
REPEAT 577 620 FU 1. {ECO:0000255}.
REPEAT 638 681 FU 2. {ECO:0000255}.
REGION 191 192 Substrate binding. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000305|PubMed:24666235,
ECO:0000305|PubMed:25974265}.
REGION 253 258 Substrate binding. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000305|PubMed:24666235,
ECO:0000305|PubMed:25974265}.
REGION 292 295 Substrate binding. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000305|PubMed:24666235,
ECO:0000305|PubMed:25974265}.
REGION 759 762 Cell surface signal.
{ECO:0000303|PubMed:9412467}.
MOTIF 498 500 Cell attachment site. {ECO:0000255}.
MOTIF 773 779 Trans Golgi network signal.
{ECO:0000269|PubMed:8846780}.
ACT_SITE 153 153 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10080}.
ACT_SITE 194 194 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10081}.
ACT_SITE 368 368 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10082}.
METAL 115 115 Calcium 1. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265}.
METAL 162 162 Calcium 1. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265}.
METAL 174 174 Calcium 2. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265}.
METAL 179 179 Calcium 2. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265}.
METAL 181 181 Calcium 2; via carbonyl oxygen.
{ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265}.
METAL 205 205 Calcium 1; via carbonyl oxygen.
{ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265}.
METAL 208 208 Calcium 1. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265}.
METAL 210 210 Calcium 1; via carbonyl oxygen.
{ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265}.
METAL 212 212 Calcium 1; via carbonyl oxygen.
{ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265}.
METAL 258 258 Calcium 3. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265}.
METAL 301 301 Calcium 3. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265}.
METAL 331 331 Calcium 3. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265}.
BINDING 154 154 Substrate. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000305|PubMed:24666235,
ECO:0000305|PubMed:25974265}.
BINDING 236 236 Substrate. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000305|PubMed:24666235,
ECO:0000305|PubMed:25974265}.
BINDING 264 264 Substrate. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000305|PubMed:24666235,
ECO:0000305|PubMed:25974265}.
BINDING 306 306 Substrate. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000305|PubMed:24666235,
ECO:0000305|PubMed:25974265}.
BINDING 308 308 Substrate. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000305|PubMed:24666235,
ECO:0000305|PubMed:25974265}.
BINDING 368 368 Substrate. {ECO:0000244|PDB:4OMC,
ECO:0000244|PDB:4OMD,
ECO:0000244|PDB:4RYD,
ECO:0000305|PubMed:24666235,
ECO:0000305|PubMed:25974265}.
SITE 75 76 Cleavage, second; by autolysis.
{ECO:0000269|PubMed:9130696}.
SITE 107 108 Cleavage, first; by autolysis.
{ECO:0000269|PubMed:1629222,
ECO:0000269|PubMed:9130696}.
MOD_RES 773 773 Phosphoserine; by CK2.
{ECO:0000269|PubMed:8846780}.
MOD_RES 775 775 Phosphoserine; by CK2.
{ECO:0000269|PubMed:8846780}.
CARBOHYD 387 387 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 440 440 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 553 553 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 211 360 {ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265}.
DISULFID 303 333 {ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265}.
DISULFID 450 474 {ECO:0000269|PubMed:24666235,
ECO:0000269|PubMed:25974265}.
VARIANT 43 43 A -> V (in dbSNP:rs16944971).
/FTId=VAR_051821.
VARIANT 547 547 W -> R (in cell line LoVo; does not
undergo autocatalytic activation and is
not transported to the Golgi apparatus).
{ECO:0000269|PubMed:7592877}.
/FTId=VAR_055343.
MUTAGEN 72 72 V->R: Loss of catalytic activity and
propeptide second cleavage and removal.
Abnormal accumulation in the early
secretory pathway.
{ECO:0000269|PubMed:11799113}.
MUTAGEN 75 75 R->A: Loss of catalytic activity and,
propeptide second cleavage and removal.
Normal trafficking to the Golgi.
{ECO:0000269|PubMed:11799113}.
MUTAGEN 153 153 D->N: Loss of catalytic activity and
propeptide first cleavage. Abnormal
accumulation in the early secretory
pathway. {ECO:0000269|PubMed:11799113,
ECO:0000269|PubMed:9130696}.
MUTAGEN 773 775 SDS->DDD: Phosphomimetic mutant.
Localization in early endosome is
increased. {ECO:0000269|PubMed:8846780}.
MUTAGEN 773 773 S->A: Slight reduction in
phosphorylation. Loss of phosphorylation
and abnormal accumulation in the early
secretory pathway; when associated with
A-775. {ECO:0000269|PubMed:8846780}.
MUTAGEN 775 775 S->A: Slight reduction in
phosphorylation. Loss of phosphorylation
and abnormal accumulation in the early
secretory pathway; when associated with
A-773. {ECO:0000269|PubMed:8846780}.
HELIX 118 120 {ECO:0000244|PDB:5JXG}.
TURN 122 124 {ECO:0000244|PDB:5JXG}.
STRAND 127 129 {ECO:0000244|PDB:5JMO}.
HELIX 134 139 {ECO:0000244|PDB:5JXG}.
STRAND 148 154 {ECO:0000244|PDB:5JXG}.
TURN 161 166 {ECO:0000244|PDB:5JXG}.
HELIX 169 171 {ECO:0000244|PDB:5JXG}.
TURN 175 178 {ECO:0000244|PDB:5JXG}.
HELIX 191 193 {ECO:0000244|PDB:5JXH}.
HELIX 194 203 {ECO:0000244|PDB:5JXG}.
STRAND 206 211 {ECO:0000244|PDB:5JXG}.
TURN 215 218 {ECO:0000244|PDB:5JXG}.
STRAND 219 225 {ECO:0000244|PDB:5JXG}.
STRAND 227 229 {ECO:0000244|PDB:5JXG}.
HELIX 233 240 {ECO:0000244|PDB:5JXG}.
TURN 244 246 {ECO:0000244|PDB:5JXG}.
STRAND 249 252 {ECO:0000244|PDB:5JXG}.
STRAND 259 261 {ECO:0000244|PDB:5JXG}.
HELIX 268 280 {ECO:0000244|PDB:5JXG}.
HELIX 282 284 {ECO:0000244|PDB:5JXG}.
STRAND 288 292 {ECO:0000244|PDB:5JXG}.
HELIX 297 299 {ECO:0000244|PDB:5JXG}.
HELIX 303 305 {ECO:0000244|PDB:5JXG}.
TURN 307 310 {ECO:0000244|PDB:5JXG}.
STRAND 314 320 {ECO:0000244|PDB:5JXG}.
STRAND 338 341 {ECO:0000244|PDB:5JXG}.
STRAND 351 355 {ECO:0000244|PDB:5JXG}.
TURN 356 358 {ECO:0000244|PDB:5JXG}.
STRAND 359 364 {ECO:0000244|PDB:5JXG}.
HELIX 367 384 {ECO:0000244|PDB:5JXG}.
HELIX 390 400 {ECO:0000244|PDB:5JXG}.
STRAND 419 421 {ECO:0000244|PDB:5JXG}.
TURN 422 424 {ECO:0000244|PDB:5JXG}.
HELIX 431 438 {ECO:0000244|PDB:5JXG}.
STRAND 448 453 {ECO:0000244|PDB:5JXG}.
STRAND 464 471 {ECO:0000244|PDB:5JXG}.
STRAND 482 496 {ECO:0000244|PDB:5JXG}.
HELIX 498 500 {ECO:0000244|PDB:5JXG}.
STRAND 501 506 {ECO:0000244|PDB:5JXG}.
STRAND 512 516 {ECO:0000244|PDB:5JXG}.
STRAND 528 535 {ECO:0000244|PDB:5JXG}.
TURN 537 540 {ECO:0000244|PDB:5JXG}.
STRAND 545 553 {ECO:0000244|PDB:5JXG}.
STRAND 555 557 {ECO:0000244|PDB:5JXG}.
STRAND 561 574 {ECO:0000244|PDB:5JXG}.
SEQUENCE 794 AA; 86678 MW; 10C44DD5892EF85D CRC64;
MELRPWLLWV VAATGTLVLL AADAQGQKVF TNTWAVRIPG GPAVANSVAR KHGFLNLGQI
FGDYYHFWHR GVTKRSLSPH RPRHSRLQRE PQVQWLEQQV AKRRTKRDVY QEPTDPKFPQ
QWYLSGVTQR DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP
DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL
GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH
DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC
TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV
SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH
ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD
EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE
EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHASCAT CQGPALTDCL
SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPEVVAGL
SCAFIVLVFV TVFLVLQLRS GFSFRGVKVY TMDRGLISYK GLPPEAWQEE CPSDSEEDEG
RGERTAFIKD QSAL


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