ID   FURIN_HUMAN             Reviewed;         794 AA.
AC   P09958; Q14336; Q6LBS3; Q9UCZ5;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   17-JUN-2020, entry version 239.
DE   RecName: Full=Furin;
DE            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};
DE   AltName: Full=Dibasic-processing enzyme;
DE   AltName: Full=Paired basic amino acid residue-cleaving enzyme;
DE            Short=PACE;
DE   Flags: Precursor;
GN   Name=FURIN; Synonyms=FUR, PACE, PCSK3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Blood;
RX   PubMed=2408021; DOI=10.1093/nar/18.3.664;
RA   van den Ouweland A.M.W., van Duijnhoven H.L.P., Keizer G.D.,
RA   Dorssers L.C.J., van de Ven W.J.M.;
RT   "Structural homology between the human fur gene product and the subtilisin-
RT   like protease encoded by yeast KEX2.";
RL   Nucleic Acids Res. 18:664-664(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=2251280; DOI=10.1073/pnas.87.23.9378;
RA   Wise R.J., Barr P.J., Wong P.A., Kiefer M.C., Brake A.J., Kaufman R.J.;
RT   "Expression of a human proprotein processing enzyme: correct cleavage of
RT   the von Willebrand factor precursor at a paired basic amino acid site.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:9378-9382(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=1713771; DOI=10.1089/dna.1991.10.319;
RA   Barr P.J., Mason O.B., Landsberg K.E., Wong P.A., Kiefer M.C., Brake A.J.;
RT   "cDNA and gene structure for a human subtilisin-like protease with cleavage
RT   specificity for paired basic amino acid residues.";
RL   DNA Cell Biol. 10:319-328(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-280.
RX   PubMed=2674906; DOI=10.1093/nar/17.17.7101;
RA   Van den Ouweland A.M.W., van Groningen J.J.M., Roebrock A.J.M.,
RA   Onnekink C., Van de Ven W.J.M.;
RT   "Nucleotide sequence analysis of the human fur gene.";
RL   Nucleic Acids Res. 17:7101-7102(1989).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 296-794.
RX   PubMed=3023061; DOI=10.1002/j.1460-2075.1986.tb04484.x;
RA   Roebroek A.J.M., Schalken J.A., Leunissen J.A.M., Onnekink C.,
RA   Bloemers H.P.J., van de Ven W.J.M.;
RT   "Evolutionary conserved close linkage of the c-fes/fps proto-oncogene and
RT   genetic sequences encoding a receptor-like protein.";
RL   EMBO J. 5:2197-2202(1986).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 402-428, FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Colon carcinoma;
RX   PubMed=7690548; DOI=10.1006/bbrc.1993.2146;
RA   Takahashi S., Kasai K., Hatsuzawa K., Kitamura N., Misumi Y., Ikehara Y.,
RA   Murakami K., Nakayama K.;
RT   "A mutation of furin causes the lack of precursor-processing activity in
RT   human colon carcinoma LoVo cells.";
RL   Biochem. Biophys. Res. Commun. 195:1019-1026(1993).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 527-553, FUNCTION, CATALYTIC ACTIVITY, AND
RP   VARIANT ARG-547.
RC   TISSUE=Colon carcinoma;
RX   PubMed=7592877; DOI=10.1074/jbc.270.44.26565;
RA   Takahashi S., Nakagawa T., Kasai K., Banno T., Duguay S.J.,
RA   Van de Ven W.J.M., Murakami K., Nakayama K.;
RT   "A second mutant allele of furin in the processing-incompetent cell line,
RT   LoVo. Evidence for involvement of the homo B domain in autocatalytic
RT   activation.";
RL   J. Biol. Chem. 270:26565-26569(1995).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PROTEOLYTIC PROCESSING.
RX   PubMed=1629222;
RA   Leduc R., Molloy S.S., Thorne B.A., Thomas G.;
RT   "Activation of human furin precursor processing endoprotease occurs by an
RT   intramolecular autoproteolytic cleavage.";
RL   J. Biol. Chem. 267:14304-14308(1992).
RN   [10]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=7737999; DOI=10.1074/jbc.270.18.10618;
RA   Dubois C.M., Laprise M.H., Blanchette F., Gentry L.E., Leduc R.;
RT   "Processing of transforming growth factor beta 1 precursor by human furin
RT   convertase.";
RL   J. Biol. Chem. 270:10618-10624(1995).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   3D-STRUCTURE MODELING OF CATALYTIC DOMAIN.
RX   PubMed=8020465; DOI=10.1111/j.1432-1033.1994.tb18864.x;
RA   Siezen R.J., Creemers J.W.M., van de Ven W.J.M.;
RT   "Homology modelling of the catalytic domain of human furin. A model for the
RT   eukaryotic subtilisin-like proprotein convertases.";
RL   Eur. J. Biochem. 222:255-266(1994).
RN   [13]
RP   SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-773 AND SER-775, MOTIF, AND
RP   MUTAGENESIS OF SER-773 AND SER-775.
RX   PubMed=8846780; DOI=10.1002/j.1460-2075.1995.tb00275.x;
RA   Jones B.G., Thomas L., Molloy S.S., Thulin C.D., Fry M.D., Walsh K.A.,
RA   Thomas G.;
RT   "Intracellular trafficking of furin is modulated by the phosphorylation
RT   state of a casein kinase II site in its cytoplasmic tail.";
RL   EMBO J. 14:5869-5883(1995).
RN   [14]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE,
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF ASP-153.
RX   PubMed=9130696; DOI=10.1093/emboj/16.7.1508;
RA   Anderson E.D., VanSlyke J.K., Thulin C.D., Jean F., Thomas G.;
RT   "Activation of the furin endoprotease is a multiple-step process:
RT   requirements for acidification and internal propeptide cleavage.";
RL   EMBO J. 16:1508-1518(1997).
RN   [15]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9412467; DOI=10.1083/jcb.139.7.1719;
RA   Liu G., Thomas L., Warren R.A., Enns C.A., Cunningham C.C., Hartwig J.H.,
RA   Thomas G.;
RT   "Cytoskeletal protein ABP-280 directs the intracellular trafficking of
RT   furin and modulates proprotein processing in the endocytic pathway.";
RL   J. Cell Biol. 139:1719-1733(1997).
RN   [16]
RP   INTERACTION WITH PACS1, AND SUBCELLULAR LOCATION.
RX   PubMed=11331585; DOI=10.1093/emboj/20.9.2191;
RA   Crump C.M., Xiang Y., Thomas L., Gu F., Austin C., Tooze S.A., Thomas G.;
RT   "PACS-1 binding to adaptors is required for acidic cluster motif-mediated
RT   protein traffic.";
RL   EMBO J. 20:2191-2201(2001).
RN   [17]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP   AND MUTAGENESIS OF VAL-72; ARG-75 AND ASP-153.
RX   PubMed=11799113; DOI=10.1074/jbc.m108740200;
RA   Anderson E.D., Molloy S.S., Jean F., Fei H., Shimamura S., Thomas G.;
RT   "The ordered and compartment-specfific autoproteolytic removal of the furin
RT   intramolecular chaperone is required for enzyme activation.";
RL   J. Biol. Chem. 277:12879-12890(2002).
RN   [18]
RP   FUNCTION (MICROBIAL INFECTION).
RX   PubMed=27582320; DOI=10.1038/srep32371;
RA   Schulte T., Mikaelsson C., Beaussart A., Kikhney A., Deshmukh M.,
RA   Wolniak S., Pathak A., Ebel C., Lofling J., Fogolari F.,
RA   Henriques-Normark B., Dufrene Y.F., Svergun D., Nygren P.A., Achour A.;
RT   "The BR domain of PsrP interacts with extracellular DNA to promote
RT   bacterial aggregation; structural insights into pneumococcal biofilm
RT   formation.";
RL   Sci. Rep. 6:32371-32371(2016).
RN   [19] {ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 108-574 IN COMPLEX WITH CALCIUM
RP   AND INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP   DISULFIDE BONDS.
RX   PubMed=24666235; DOI=10.1021/cb500087x;
RA   Dahms S.O., Hardes K., Becker G.L., Steinmetzer T., Brandstetter H.,
RA   Than M.E.;
RT   "X-ray structures of human furin in complex with competitive inhibitors.";
RL   ACS Chem. Biol. 9:1113-1118(2014).
RN   [20] {ECO:0000244|PDB:4RYD}
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 108-574 IN COMPLEX WITH CALCIUM
RP   AND INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP   DISULFIDE BONDS.
RX   PubMed=25974265; DOI=10.1002/cmdc.201500103;
RA   Hardes K., Becker G.L., Lu Y., Dahms S.O., Kohler S., Beyer W., Sandvig K.,
RA   Yamamoto H., Lindberg I., Walz L., von Messling V., Than M.E., Garten W.,
RA   Steinmetzer T.;
RT   "Novel Furin inhibitors with potent anti-infectious activity.";
RL   ChemMedChem 10:1218-1231(2015).
CC   -!- FUNCTION: Ubiquitous endoprotease within constitutive secretory
CC       pathways capable of cleavage at the RX(K/R)R consensus motif
CC       (PubMed:11799113, PubMed:1629222, PubMed:1713771, PubMed:2251280,
CC       PubMed:24666235, PubMed:25974265, PubMed:7592877, PubMed:7690548,
CC       PubMed:9130696). Mediates processing of TGFB1, an essential step in
CC       TGF-beta-1 activation (PubMed:7737999). {ECO:0000269|PubMed:11799113,
CC       ECO:0000269|PubMed:1629222, ECO:0000269|PubMed:1713771,
CC       ECO:0000269|PubMed:2251280, ECO:0000269|PubMed:24666235,
CC       ECO:0000269|PubMed:25974265, ECO:0000269|PubMed:7592877,
CC       ECO:0000269|PubMed:7690548, ECO:0000269|PubMed:7737999,
CC       ECO:0000269|PubMed:9130696}.
CC   -!- FUNCTION: (Microbial infection) Probably cleaves and activates anthrax
CC       and diphtheria toxins.
CC   -!- FUNCTION: (Microbial infection) Required for H7N1 and H5N1 influenza
CC       virus infection probably by cleaving hemagglutinin.
CC       {ECO:0000269|PubMed:25974265}.
CC   -!- FUNCTION: (Microbial infection) Able to cleave S.pneumoniae serine-rich
CC       repeat protein PsrP. {ECO:0000269|PubMed:27582320}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of mature proteins from their proproteins by cleavage
CC         of -Arg-Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and
CC         Yaa is Arg or Lys. Releases albumin, complement component C3 and von
CC         Willebrand factor from their respective precursors.; EC=3.4.21.75;
CC         Evidence={ECO:0000269|PubMed:11799113, ECO:0000269|PubMed:1629222,
CC         ECO:0000269|PubMed:1713771, ECO:0000269|PubMed:2251280,
CC         ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265,
CC         ECO:0000269|PubMed:7592877, ECO:0000269|PubMed:7690548,
CC         ECO:0000269|PubMed:7737999, ECO:0000269|PubMed:9130696};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265,
CC         ECO:0000269|PubMed:9130696};
CC       Note=Binds 3 calcium ions per subunit. {ECO:0000269|PubMed:24666235,
CC       ECO:0000269|PubMed:25974265, ECO:0000269|PubMed:9130696};
CC   -!- ACTIVITY REGULATION: Inhibited by the not secondly cleaved propeptide
CC       (PubMed:9130696, PubMed:11799113). Inhibited by m-guanidinomethyl-
CC       phenylacetyl-Arg-Val-Arg-(amidomethyl)-benzamidine (m-guanidinomethyl-
CC       Phac-RVR-Amb) and 4-guanidinomethyl-phenylacetyl-Arg-Tle-Arg-4-
CC       amidinobenzylamide (MI-1148) (PubMed:24666235, PubMed:25974265).
CC       {ECO:0000269|PubMed:11799113, ECO:0000269|PubMed:24666235,
CC       ECO:0000269|PubMed:25974265, ECO:0000269|PubMed:9130696}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:9130696};
CC   -!- SUBUNIT: Interacts with FLNA (By similarity). Binds to PACS1 which
CC       mediates TGN localization and connection to clathrin adapters
CC       (PubMed:11331585). {ECO:0000250|UniProtKB:P23188,
CC       ECO:0000269|PubMed:11331585}.
CC   -!- INTERACTION:
CC       P09958; P50281: MMP14; NbExp=3; IntAct=EBI-1056807, EBI-992788;
CC       P09958; Q9H239: MMP28; NbExp=3; IntAct=EBI-1056807, EBI-20858485;
CC       P09958; O14793: MSTN; NbExp=2; IntAct=EBI-1056807, EBI-8542977;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000269|PubMed:11331585, ECO:0000269|PubMed:11799113,
CC       ECO:0000269|PubMed:8846780, ECO:0000269|PubMed:9130696,
CC       ECO:0000269|PubMed:9412467}; Single-pass type I membrane protein
CC       {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:11799113,
CC       ECO:0000269|PubMed:9130696, ECO:0000269|PubMed:9412467}; Single-pass
CC       type I membrane protein {ECO:0000305}. Secreted
CC       {ECO:0000305|PubMed:11799113}. Endosome membrane
CC       {ECO:0000269|PubMed:9412467}; Single-pass type I membrane protein
CC       {ECO:0000305}. Note=Shuttles between the trans-Golgi network and the
CC       cell surface (PubMed:9412467, PubMed:11799113). Propeptide cleavage is
CC       a prerequisite for exit of furin molecules out of the endoplasmic
CC       reticulum (ER). A second cleavage within the propeptide occurs in the
CC       trans Golgi network (TGN), followed by the release of the propeptide
CC       and the activation of furin (PubMed:11799113).
CC       {ECO:0000269|PubMed:11799113, ECO:0000269|PubMed:9412467}.
CC   -!- TISSUE SPECIFICITY: Seems to be expressed ubiquitously.
CC       {ECO:0000269|PubMed:1713771}.
CC   -!- DOMAIN: Contains a cytoplasmic domain responsible for its TGN
CC       localization and recycling from the cell surface.
CC       {ECO:0000269|PubMed:8846780}.
CC   -!- PTM: The inhibition peptide, which plays the role of an intramolecular
CC       chaperone, is autocatalytically removed in the endoplasmic reticulum
CC       (ER) and remains non-covalently bound to furin as a potent
CC       autoinhibitor. Following transport to the trans Golgi, a second
CC       cleavage within the inhibition propeptide results in propeptide
CC       dissociation and furin activation. {ECO:0000269|PubMed:1629222,
CC       ECO:0000269|PubMed:9130696}.
CC   -!- PTM: Phosphorylation is required for TGN localization of the
CC       endoprotease. In vivo, exists as di-, mono- and non-phosphorylated
CC       forms. {ECO:0000269|PubMed:8846780}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/FURINID40646ch15q26.html";
DR   EMBL; X17094; CAA34948.1; -; mRNA.
DR   EMBL; BC012181; AAH12181.1; -; mRNA.
DR   EMBL; X15723; CAA33745.1; -; Genomic_DNA.
DR   EMBL; X04329; CAA27860.1; -; Genomic_DNA.
DR   CCDS; CCDS10364.1; -.
DR   PIR; A39552; KXHUF.
DR   RefSeq; NP_001276752.1; NM_001289823.1.
DR   RefSeq; NP_001276753.1; NM_001289824.1.
DR   RefSeq; NP_002560.1; NM_002569.3.
DR   PDB; 4OMC; X-ray; 2.30 A; A/B/C/D/E/F=108-574.
DR   PDB; 4OMD; X-ray; 2.70 A; A/B/C/D/E/F=108-574.
DR   PDB; 4RYD; X-ray; 2.15 A; A/B/C/D/E/F=108-574.
DR   PDB; 4Z2A; X-ray; 1.89 A; A=110-574.
DR   PDB; 5JMO; X-ray; 2.00 A; A/B=108-574.
DR   PDB; 5JXG; X-ray; 1.80 A; A=108-574.
DR   PDB; 5JXH; X-ray; 2.00 A; A=108-574.
DR   PDB; 5JXI; X-ray; 2.00 A; A=108-574.
DR   PDB; 5JXJ; X-ray; 2.00 A; A=108-574.
DR   PDB; 5MIM; X-ray; 1.90 A; A=108-574.
DR   PDB; 6A8Y; NMR; -; A=64-89.
DR   PDB; 6EQV; X-ray; 1.90 A; A=108-574.
DR   PDB; 6EQW; X-ray; 1.99 A; A=108-574.
DR   PDB; 6EQX; X-ray; 1.99 A; A=108-567.
DR   PDB; 6HLB; X-ray; 2.00 A; A=108-574.
DR   PDB; 6HLD; X-ray; 2.10 A; A=108-574.
DR   PDB; 6HLE; X-ray; 1.99 A; A=108-574.
DR   PDB; 6HZA; X-ray; 1.90 A; A=108-574.
DR   PDB; 6HZB; X-ray; 1.90 A; A=108-574.
DR   PDB; 6HZC; X-ray; 1.90 A; A=108-574.
DR   PDB; 6HZD; X-ray; 1.90 A; A=108-574.
DR   PDBsum; 4OMC; -.
DR   PDBsum; 4OMD; -.
DR   PDBsum; 4RYD; -.
DR   PDBsum; 4Z2A; -.
DR   PDBsum; 5JMO; -.
DR   PDBsum; 5JXG; -.
DR   PDBsum; 5JXH; -.
DR   PDBsum; 5JXI; -.
DR   PDBsum; 5JXJ; -.
DR   PDBsum; 5MIM; -.
DR   PDBsum; 6A8Y; -.
DR   PDBsum; 6EQV; -.
DR   PDBsum; 6EQW; -.
DR   PDBsum; 6EQX; -.
DR   PDBsum; 6HLB; -.
DR   PDBsum; 6HLD; -.
DR   PDBsum; 6HLE; -.
DR   PDBsum; 6HZA; -.
DR   PDBsum; 6HZB; -.
DR   PDBsum; 6HZC; -.
DR   PDBsum; 6HZD; -.
DR   SMR; P09958; -.
DR   BioGRID; 111082; 41.
DR   CORUM; P09958; -.
DR   DIP; DIP-29904N; -.
DR   ELM; P09958; -.
DR   IntAct; P09958; 20.
DR   MINT; P09958; -.
DR   STRING; 9606.ENSP00000483552; -.
DR   BindingDB; P09958; -.
DR   ChEMBL; CHEMBL2611; -.
DR   DrugBank; DB03600; Capric acid.
DR   DrugBank; DB04951; Pirfenidone.
DR   GuidetoPHARMACOLOGY; 2366; -.
DR   MEROPS; S08.071; -.
DR   iPTMnet; P09958; -.
DR   PhosphoSitePlus; P09958; -.
DR   SwissPalm; P09958; -.
DR   BioMuta; FURIN; -.
DR   DMDM; 120611; -.
DR   OGP; P09958; -.
DR   EPD; P09958; -.
DR   jPOST; P09958; -.
DR   MassIVE; P09958; -.
DR   MaxQB; P09958; -.
DR   PaxDb; P09958; -.
DR   PeptideAtlas; P09958; -.
DR   PRIDE; P09958; -.
DR   ProteomicsDB; 52283; -.
DR   ABCD; P09958; 1 sequenced antibody.
DR   Antibodypedia; 4013; 413 antibodies.
DR   Ensembl; ENST00000268171; ENSP00000268171; ENSG00000140564.
DR   Ensembl; ENST00000610579; ENSP00000484952; ENSG00000140564.
DR   Ensembl; ENST00000618099; ENSP00000483552; ENSG00000140564.
DR   GeneID; 5045; -.
DR   KEGG; hsa:5045; -.
DR   UCSC; uc002bpu.2; human.
DR   CTD; 5045; -.
DR   DisGeNET; 5045; -.
DR   EuPathDB; HostDB:ENSG00000140564.10; -.
DR   GeneCards; FURIN; -.
DR   HGNC; HGNC:8568; FURIN.
DR   HPA; ENSG00000140564; Group enriched (liver, placenta, salivary gland).
DR   MIM; 136950; gene.
DR   neXtProt; NX_P09958; -.
DR   OpenTargets; ENSG00000140564; -.
DR   PharmGKB; PA32894; -.
DR   eggNOG; KOG3525; Eukaryota.
DR   eggNOG; COG1404; LUCA.
DR   eggNOG; COG4935; LUCA.
DR   GeneTree; ENSGT00940000157220; -.
DR   HOGENOM; CLU_002976_4_0_1; -.
DR   InParanoid; P09958; -.
DR   KO; K01349; -.
DR   OMA; CLGEPTH; -.
DR   OrthoDB; 473018at2759; -.
DR   PhylomeDB; P09958; -.
DR   TreeFam; TF314277; -.
DR   Reactome; R-HSA-1181150; Signaling by NODAL.
DR   Reactome; R-HSA-1442490; Collagen degradation.
DR   Reactome; R-HSA-1566948; Elastic fibre formation.
DR   Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
DR   Reactome; R-HSA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR   Reactome; R-HSA-167060; NGF processing.
DR   Reactome; R-HSA-171286; Synthesis and processing of ENV and VPU.
DR   Reactome; R-HSA-186797; Signaling by PDGF.
DR   Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi.
DR   Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
DR   Reactome; R-HSA-5210891; Uptake and function of anthrax toxins.
DR   Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR   Reactome; R-HSA-8963889; Assembly of active LPL and LIPC lipase complexes.
DR   Reactome; R-HSA-977225; Amyloid fiber formation.
DR   SignaLink; P09958; -.
DR   SIGNOR; P09958; -.
DR   BioGRID-ORCS; 5045; 107 hits in 787 CRISPR screens.
DR   ChiTaRS; FURIN; human.
DR   GeneWiki; Furin; -.
DR   GenomeRNAi; 5045; -.
DR   Pharos; P09958; Tchem.
DR   PRO; PR:P09958; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; P09958; protein.
DR   Bgee; ENSG00000140564; Expressed in right lobe of liver and 222 other tissues.
DR   ExpressionAtlas; P09958; baseline and differential.
DR   Genevisible; P09958; HS.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0005783; C:endoplasmic reticulum; IGI:BHF-UCL.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0000139; C:Golgi membrane; IMP:UniProtKB.
DR   GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:BHF-UCL.
DR   GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:MGI.
DR   GO; GO:0004175; F:endopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048406; F:nerve growth factor binding; IDA:BHF-UCL.
DR   GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR   GO; GO:0042277; F:peptide binding; IDA:BHF-UCL.
DR   GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:BHF-UCL.
DR   GO; GO:0001825; P:blastocyst formation; IEA:Ensembl.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
DR   GO; GO:0070268; P:cornification; TAS:Reactome.
DR   GO; GO:0090472; P:dibasic protein processing; IMP:UniProtKB.
DR   GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0032804; P:negative regulation of low-density lipoprotein particle receptor catabolic process; IDA:HGNC-UCL.
DR   GO; GO:0032911; P:negative regulation of transforming growth factor beta1 production; IMP:BHF-UCL.
DR   GO; GO:0032455; P:nerve growth factor processing; TAS:Reactome.
DR   GO; GO:0032902; P:nerve growth factor production; IDA:BHF-UCL.
DR   GO; GO:0043043; P:peptide biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0016486; P:peptide hormone processing; IDA:BHF-UCL.
DR   GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IC:BHF-UCL.
DR   GO; GO:1901394; P:positive regulation of transforming growth factor beta1 activation; IDA:UniProtKB.
DR   GO; GO:0016485; P:protein processing; IDA:UniProtKB.
DR   GO; GO:0052548; P:regulation of endopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0051004; P:regulation of lipoprotein lipase activity; TAS:Reactome.
DR   GO; GO:0045714; P:regulation of low-density lipoprotein particle receptor biosynthetic process; IEA:Ensembl.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IMP:BHF-UCL.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:Ensembl.
DR   GO; GO:0032940; P:secretion by cell; IDA:BHF-UCL.
DR   GO; GO:0006465; P:signal peptide processing; IDA:HGNC-UCL.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0019058; P:viral life cycle; IEP:BHF-UCL.
DR   GO; GO:0019082; P:viral protein processing; TAS:Reactome.
DR   GO; GO:0031638; P:zymogen activation; IMP:UniProtKB.
DR   GO; GO:0097341; P:zymogen inhibition; IMP:UniProtKB.
DR   CDD; cd00064; FU; 2.
DR   CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 3.30.70.850; -; 1.
DR   Gene3D; 3.40.50.200; -; 1.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR034182; Kexin/furin.
DR   InterPro; IPR002884; P_dom.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR032815; S8_pro-domain.
DR   InterPro; IPR038466; S8_pro-domain_sf.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF16470; S8_pro-domain; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SMART; SM00261; FU; 2.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF52743; SSF52743; 1.
DR   SUPFAM; SSF57184; SSF57184; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Autocatalytic cleavage; Calcium; Cell membrane;
KW   Cleavage on pair of basic residues; Disulfide bond; Endosome; Glycoprotein;
KW   Golgi apparatus; Host-virus interaction; Hydrolase; Membrane;
KW   Metal-binding; Phosphoprotein; Polymorphism; Protease; Reference proteome;
KW   Repeat; Secreted; Serine protease; Signal; Transmembrane;
KW   Transmembrane helix; Zymogen.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   PROPEP          27..107
FT                   /note="Inhibition peptide"
FT                   /evidence="ECO:0000269|PubMed:9130696"
FT                   /id="PRO_0000027028"
FT   CHAIN           108..794
FT                   /note="Furin"
FT                   /id="PRO_0000027029"
FT   TOPO_DOM        108..715
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        716..738
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        739..794
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          121..435
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   DOMAIN          444..576
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT   REPEAT          577..620
FT                   /note="FU 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          638..681
FT                   /note="FU 2"
FT                   /evidence="ECO:0000255"
FT   REGION          191..192
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235,
FT                   ECO:0000305|PubMed:25974265"
FT   REGION          253..258
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235,
FT                   ECO:0000305|PubMed:25974265"
FT   REGION          292..295
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235,
FT                   ECO:0000305|PubMed:25974265"
FT   REGION          759..762
FT                   /note="Cell surface signal"
FT                   /evidence="ECO:0000303|PubMed:9412467"
FT   MOTIF           498..500
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   MOTIF           773..779
FT                   /note="Trans Golgi network signal"
FT                   /evidence="ECO:0000269|PubMed:8846780"
FT   ACT_SITE        153
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        194
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        368
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   METAL           115
FT                   /note="Calcium 1"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235,
FT                   ECO:0000269|PubMed:25974265"
FT   METAL           162
FT                   /note="Calcium 1"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235,
FT                   ECO:0000269|PubMed:25974265"
FT   METAL           174
FT                   /note="Calcium 2"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235,
FT                   ECO:0000269|PubMed:25974265"
FT   METAL           179
FT                   /note="Calcium 2"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235,
FT                   ECO:0000269|PubMed:25974265"
FT   METAL           181
FT                   /note="Calcium 2; via carbonyl oxygen"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235,
FT                   ECO:0000269|PubMed:25974265"
FT   METAL           205
FT                   /note="Calcium 1; via carbonyl oxygen"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235,
FT                   ECO:0000269|PubMed:25974265"
FT   METAL           208
FT                   /note="Calcium 1"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235,
FT                   ECO:0000269|PubMed:25974265"
FT   METAL           210
FT                   /note="Calcium 1; via carbonyl oxygen"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235,
FT                   ECO:0000269|PubMed:25974265"
FT   METAL           212
FT                   /note="Calcium 1; via carbonyl oxygen"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235,
FT                   ECO:0000269|PubMed:25974265"
FT   METAL           258
FT                   /note="Calcium 3"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235,
FT                   ECO:0000269|PubMed:25974265"
FT   METAL           301
FT                   /note="Calcium 3"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235,
FT                   ECO:0000269|PubMed:25974265"
FT   METAL           331
FT                   /note="Calcium 3"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235,
FT                   ECO:0000269|PubMed:25974265"
FT   BINDING         154
FT                   /note="Substrate"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235,
FT                   ECO:0000305|PubMed:25974265"
FT   BINDING         236
FT                   /note="Substrate"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235,
FT                   ECO:0000305|PubMed:25974265"
FT   BINDING         264
FT                   /note="Substrate"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235,
FT                   ECO:0000305|PubMed:25974265"
FT   BINDING         306
FT                   /note="Substrate"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235,
FT                   ECO:0000305|PubMed:25974265"
FT   BINDING         308
FT                   /note="Substrate"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235,
FT                   ECO:0000305|PubMed:25974265"
FT   BINDING         368
FT                   /note="Substrate"
FT                   /evidence="ECO:0000244|PDB:4OMC, ECO:0000244|PDB:4OMD,
FT                   ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235,
FT                   ECO:0000305|PubMed:25974265"
FT   SITE            75..76
FT                   /note="Cleavage, second; by autolysis"
FT                   /evidence="ECO:0000269|PubMed:9130696"
FT   SITE            107..108
FT                   /note="Cleavage, first; by autolysis"
FT                   /evidence="ECO:0000269|PubMed:1629222,
FT                   ECO:0000269|PubMed:9130696"
FT   MOD_RES         773
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000269|PubMed:8846780"
FT   MOD_RES         775
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000269|PubMed:8846780"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        440
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        553
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        211..360
FT                   /evidence="ECO:0000269|PubMed:24666235,
FT                   ECO:0000269|PubMed:25974265"
FT   DISULFID        303..333
FT                   /evidence="ECO:0000269|PubMed:24666235,
FT                   ECO:0000269|PubMed:25974265"
FT   DISULFID        450..474
FT                   /evidence="ECO:0000269|PubMed:24666235,
FT                   ECO:0000269|PubMed:25974265"
FT   VARIANT         43
FT                   /note="A -> V (in dbSNP:rs16944971)"
FT                   /id="VAR_051821"
FT   VARIANT         547
FT                   /note="W -> R (in cell line LoVo; does not undergo
FT                   autocatalytic activation and is not transported to the
FT                   Golgi apparatus)"
FT                   /evidence="ECO:0000269|PubMed:7592877"
FT                   /id="VAR_055343"
FT   MUTAGEN         72
FT                   /note="V->R: Loss of catalytic activity and propeptide
FT                   second cleavage and removal. Abnormal accumulation in the
FT                   early secretory pathway."
FT                   /evidence="ECO:0000269|PubMed:11799113"
FT   MUTAGEN         75
FT                   /note="R->A: Loss of catalytic activity and, propeptide
FT                   second cleavage and removal. Normal trafficking to the
FT                   Golgi."
FT                   /evidence="ECO:0000269|PubMed:11799113"
FT   MUTAGEN         153
FT                   /note="D->N: Loss of catalytic activity and propeptide
FT                   first cleavage. Abnormal accumulation in the early
FT                   secretory pathway."
FT                   /evidence="ECO:0000269|PubMed:11799113,
FT                   ECO:0000269|PubMed:9130696"
FT   MUTAGEN         773..775
FT                   /note="SDS->DDD: Phosphomimetic mutant. Localization in
FT                   early endosome is increased."
FT                   /evidence="ECO:0000269|PubMed:8846780"
FT   MUTAGEN         773
FT                   /note="S->A: Slight reduction in phosphorylation. Loss of
FT                   phosphorylation and abnormal accumulation in the early
FT                   secretory pathway; when associated with A-775."
FT                   /evidence="ECO:0000269|PubMed:8846780"
FT   MUTAGEN         775
FT                   /note="S->A: Slight reduction in phosphorylation. Loss of
FT                   phosphorylation and abnormal accumulation in the early
FT                   secretory pathway; when associated with A-773."
FT                   /evidence="ECO:0000269|PubMed:8846780"
FT   HELIX           66..68
FT                   /evidence="ECO:0000244|PDB:6A8Y"
FT   HELIX           73..77
FT                   /evidence="ECO:0000244|PDB:6A8Y"
FT   STRAND          78..80
FT                   /evidence="ECO:0000244|PDB:6A8Y"
FT   TURN            82..84
FT                   /evidence="ECO:0000244|PDB:6A8Y"
FT   HELIX           85..88
FT                   /evidence="ECO:0000244|PDB:6A8Y"
FT   HELIX           118..120
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   TURN            122..124
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          127..129
FT                   /evidence="ECO:0000244|PDB:5MIM"
FT   HELIX           134..139
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          148..154
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   TURN            161..166
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   HELIX           169..171
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   TURN            175..178
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   HELIX           191..193
FT                   /evidence="ECO:0000244|PDB:6EQV"
FT   HELIX           194..203
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          206..211
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   TURN            215..218
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          219..225
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          227..229
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   HELIX           233..240
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   TURN            244..246
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          249..252
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          259..261
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   HELIX           268..280
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   HELIX           282..284
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          288..292
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   HELIX           297..299
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   HELIX           303..305
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   TURN            307..310
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          314..320
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          338..341
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          351..355
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   TURN            356..358
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          359..364
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   HELIX           367..384
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   HELIX           390..400
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          419..421
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   TURN            422..424
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   HELIX           431..438
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          448..453
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          464..471
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          482..496
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   HELIX           498..500
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          501..506
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          512..516
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          528..535
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   TURN            537..540
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          545..553
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          555..557
FT                   /evidence="ECO:0000244|PDB:5JXG"
FT   STRAND          561..574
FT                   /evidence="ECO:0000244|PDB:5JXG"
SQ   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
//