| IED ID | IndEnz0002002039 |
| Enzyme Type ID | protease002039 |
| Protein Name |
Furin-1 EC 3.4.21.75 Dibasic-processing enzyme Paired basic amino acid residue-cleaving enzyme PACE |
| Gene Name | furin |
| Organism | Xenopus laevis (African clawed frog) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
| Enzyme Sequence | MDLSPSLLLMLWTLLSVLVEEITGQKVYTNTWAAHISGGSAEADRLCKKYGFINHGLIFEDHYHFSHRAVMKRSLTPKRTRQVLLKREPQVHWLEQQVAKKRKKRDIYTDPTDPKFMQQWYLLDTNRHDLHVKEAWEQGFTGKGIVVSILDDGIEKNHPDLQANYDPAASYDVNDQDPDPQPRYTQLNDNRHGTRCAGEVAAVANNGICGVGIAYNANIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPAKLAEEAFYRGVTQGRGGLGSIYVWASGNGGREHDSCNCDGYTNSIYTLSISSTTQMGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTDSHTGTSASAPLAAGIIALALEANKNLTWRDMQHLVVQTSNPAGLNANDWITNGVGRKVSHSYGYGLLDAGAMVAMAKTWVTVGPQRKYVIDILSEPKDIGKALEVRRKVEPCAGMSNYISTLEHVQARLSLSYNCRGDLAIYLTSPMGTRSCLLAPRPHDYSADGFNDWSFMTTHSWDEDPAGEWVLEIENVSNNNNYGTLTQFVLVLYGTASEGLSRKFDGDGSRNVASSQSCIVCEEGYFLHQKSCIKSCPQGFTSSIQNIHYTLDNNIEPLLVNVCVPCHVSCATCKGTTINDCLTCPAHSHYNLLDYSCTHQTQRSRESPTLKDSSHDYVARTSNLPFIVAILSCLFIIVVFGSIFLFLQLRSGGVLGRKRLYMLDSGIISYKGIPSGAWQEEGFSESETEETAAHSERTAFLKQQSTL |
| Enzyme Length | 783 |
| Uniprot Accession Number | P29119 |
| Absorption | |
| Active Site | ACT_SITE 151; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 192; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 366; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| 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). {ECO:0000250|UniProtKB:P09958}. |
| Binding Site | BINDING 152; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 234; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 262; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 304; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 306; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 366; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=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.; EC=3.4.21.75; Evidence={ECO:0000250|UniProtKB:P09958}; |
| DNA Binding | |
| EC Number | 3.4.21.75 |
| Enzyme Function | FUNCTION: Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif. {ECO:0000250|UniProtKB:P09958}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (6); Chain (1); Disulfide bond (2); Domain (2); Glycosylation (2); Metal binding (11); Motif (1); Propeptide (1); Region (6); Repeat (2); Signal peptide (1); Site (2); Topological domain (2); Transmembrane (1) |
| Keywords | Cell membrane;Cleavage on pair of basic residues;Disulfide bond;Endosome;Glycoprotein;Golgi apparatus;Hydrolase;Membrane;Metal-binding;Protease;Repeat;Secreted;Serine protease;Signal;Transmembrane;Transmembrane helix;Zymogen |
| Interact With | |
| Induction | |
| 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}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 496..498; /note=Cell attachment site; /evidence=ECO:0000255|PROSITE-ProRule:PRU00293 |
| Gene Encoded By | |
| Mass | 86,444 |
| Kinetics | |
| Metal Binding | METAL 113; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P09958; METAL 160; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P09958; METAL 172; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P09958; METAL 177; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P09958; METAL 179; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09958; METAL 203; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09958; METAL 206; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P09958; METAL 210; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09958; METAL 256; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P09958; METAL 299; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P09958; METAL 329; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P09958 |
| Rhea ID | |
| Cross Reference Brenda |