| IED ID | IndEnz0002007000 |
| Enzyme Type ID | protease007000 |
| Protein Name |
Furin-like protease kpc-1 EC 3.4.21.- CelfurPC protein |
| Gene Name | kpc-1 F11A6.1 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MSNISWYRHCSVRLQLVTLALFLLLGSASLGSAHIDEEFEDDVTTTISSIASPMRRTYTNEWAVRIAGGKVEEANRLANKYGYTNLGPIIPGDEYYLFRDDRKKSRSSRKTRSLSANQLQHEEDVMWMEQQVAKRRVKRGYRRIRRHTDDNDIFEEDDDGTQISKSRNRKHPDPNDPLWTDMWYLNRGEHHSDSTTRMDHNVKEAWDLGYTGKGVVVTILDDGLERTHPDISPNYDERASYDVNDRDNDPMPRYEFSDENRHGTRCAGEVAAIFNNSLCIVGIAYNANIGGIRMLDGDVTDAVEAASVGHNADYIDIYSASWGPDDDGRTVDGPAKLTRSAFEKGITMGRKGKGSIFVWASGNGGKDADSCNCDGYTNSIYTLSISSATENGNIPWYSEACSSTLATTYSSGATGEKMILTTDLHHACTNMHTGTSASAPLAAGIVALALEANPNLTWRDLQHIVIRTAKPINLRAGDWTTNGVGRNVSHSFGYGLMDAGAMVKLAKIWKKVDEQHRCRQFYPSRYKNIPNGNRLQLQLYSDGCYGGADENKVSYVEHVQAIVTLKAPKRGDLQIYLTSPSGTKSTLLTKRARDTSRSGFTDWAFMTTHNWGEQAAGLWILEIDNDGWDDAELVKWELVLYGTDRETGDFGGQHASPLAVRSVQMEATSSGTQYSIFHVITLVILTFSQILY |
| Enzyme Length | 692 |
| Uniprot Accession Number | O17798 |
| Absorption | |
| Active Site | ACT_SITE 221; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 262; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 436; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | |
| Binding Site | BINDING 222; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 304; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 332; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 374; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 376; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 436; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Furin-like protease which cleaves proproteins at the RX(K/R)R consensus motif (PubMed:24671950). During neuronal development, regulates the formation and extension of dendrite branches and cellular positioning of various type of neurons (PubMed:23932402, PubMed:25232734, PubMed:26974341, PubMed:28846083). Together with chin-1 and cdc-42, plays a role in the development of the neuropil and is required for the guidance of axons from neurons, including SubL pioneer neurons and AIY interneurons, into the nerve ring (PubMed:28846083). Its role in axon guidance in glia and pioneer neurons may be through ensuring the fmi-1 protein is correctly localized to the nerve ring (PubMed:28846083). Promotes the formation, extension and self-avoidance of dendritic branches of PVD and FLP mechanosensory neurons (PubMed:23932402, PubMed:25232734, PubMed:26974341). In PVD neurons, regulates plasma membrane levels of branching receptor dma-1 by targeting it to late endosomes and thus promotes normal dendrite branching and dendrite self-avoidance (PubMed:26974341). Also controls dendrite extension in AIY and D-type motoneurons, dendrite branching in AQR sensory neurons and VC4/5 motoneurons, the normal number of dendritic branches in AVL neurons and the positioning of HSN and ALM/PLM neurons (PubMed:25232734). Dispensable for maintaining dendrite branching in adults (PubMed:25232734). Also regulates dauer-specific dendritic branching of IL2 neurons and dauer-specific nictation behavior (PubMed:23932402). Under adverse environmental conditions, may promote dauer formation by processing insulin-like proteins ins-1 and ins-18, two daf-2/InsR antagonists (PubMed:24671950). {ECO:0000269|PubMed:23932402, ECO:0000269|PubMed:24671950, ECO:0000269|PubMed:25232734, ECO:0000269|PubMed:26974341, ECO:0000269|PubMed:28846083}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (6); Chain (1); Compositional bias (1); Disulfide bond (3); Domain (2); Glycosylation (4); Metal binding (12); Motif (1); Mutagenesis (8); Propeptide (1); Region (5); Sequence conflict (1); Signal peptide (1); Topological domain (1); Transmembrane (1) |
| Keywords | Calcium;Cell membrane;Cell projection;Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Protease;Reference proteome;Serine protease;Signal;Transmembrane;Transmembrane helix;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:26974341}; Single-pass type I membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:23932402}. Cell projection, axon {ECO:0000269|PubMed:23932402}. Note=In most neurons, localizes exclusively within the cell bodies, but in ventral cord neurons, localizes in both the neuronal cell bodies and processes. {ECO:0000269|PubMed:23932402}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..33; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10778742; 20610404; 21085631; 21177967; 21367940; 22267497; 22286215; 22560298; 23665919; 23800452; 24884423; 25487147; 6593563; |
| Motif | MOTIF 570..572; /note=Cell attachment site; /evidence=ECO:0000255|PROSITE-ProRule:PRU00293 |
| Gene Encoded By | |
| Mass | 77,125 |
| Kinetics | |
| Metal Binding | METAL 176; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P09958; METAL 230; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P09958; METAL 242; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P09958; METAL 247; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P09958; METAL 249; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09958; METAL 273; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09958; METAL 276; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P09958; METAL 278; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09958; METAL 280; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09958; METAL 326; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P09958; METAL 369; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P09958; METAL 399; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P09958 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.75; |