| IED ID | IndEnz0002018555 |
| Enzyme Type ID | protease018555 |
| Protein Name |
Endoprotease bli-4 EC 3.4.21.- Blisterase Blistered cuticle protein 4 |
| Gene Name | bli-4 kpc-4 K04F10.4 |
| 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 | MRISIGRIAWQILAVLIAVAFTIEHDSICDESIGACGEPIHTVIRLAKRDDELARRIAADHDMHVKGDPFLDTHYFLYHSETTRTRRHKRAIVERLDSHPAVEWVEEQRPKKRVKRDYILLDNDVHHSNPFRRSVLNRDGTRRAQRQQPQSPREIPSLPFPDPLYKDQWYLHGGAVGGYDMNVRQAWLQGYAGRNVSVSILDDGIQRDHPDLAANYDPLASTDINDHDDDPTPQNNGDNKHGTRCAGEVAALAGNNQCGVGVAFKAKIGGVRMLDGAVSDSVEAASLSLNQDHIDIYSASWGPEDDGKTFDGPGPLAREAFYRGIKNGRGGKGNIFVWASGNGGSRQDSCSADGYTTSVYTLSISSATYDNHRPWYLEECPSSIATTYSSADFRQPAIVTVDVPGGCTDKHTGTSASAPLAAGIIALALEANPELTWRDMQHLVLRTANWKPLENNPGWSRNGVGRMVSNKFGYGLIDGGALVNMAKTWKTVPEQHICTYEYRLANPNPRPIVGRFQLNFTLDVNGCESGTPVLYLEHVQVHATVRYLKRGDLKLTLFSPSGTRSVLLPPRPQDFNANGFHKWPFLSVQQWGEDPRGTWLLMVESVTTNPAATGTFHDWTLLLYGTADPAQSGDPVYSATPATSQGVLSRVHQLTSQVEESAPISFPDLTSAGNCHDECNGGCTESSSATSCFACKHLTQTLRNKGGSGFKCVQKCDDTYYLDGDKCKMCSSHCHTCTKAEVCETCPGSLLLIDVDNMPHYDHGKCVESCPPGLVADYESNLVQAKCIWRKDLCGDGYYINAVGKCDLCDSSCETCTAPGPMSCEKCSKGYGKGSIGYCRPCCPEGSTKSWQCEDCSKPDPTLLIDSNKSSGFGLMFWIVVSLIAACGICACKKCASETKSSNVEYAPLAQYNATNGAINLGAHTDDEDDDEDEVFVNPQIV |
| Enzyme Length | 942 |
| Uniprot Accession Number | P51559 |
| Absorption | |
| Active Site | ACT_SITE 202; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 241; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 415; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | |
| Binding Site | BINDING 203; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 283; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 311; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 353; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 355; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 415; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958 |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine endoprotease which cleaves proproteins at paired basic amino acids (Probable). Involved in cuticle biosynthesis probably by cleaving pro-collagen into its mature form. Acts in ASEL sensory neurons to regulate high salt chemotaxis responses probably by cleaving insulin-like protein ins-6 into its mature and active form (PubMed:24013594). Essential for embryonic and larval development (PubMed:7774813, PubMed:10903434, pubmed:19716386). isoform a, isoform e, isoform f, isoform g and isoform h are involved in cuticle biosynthesis but are dispensable for larval development (PubMed:7774813, PubMed:10903434). {ECO:0000269|PubMed:10903434, ECO:0000269|PubMed:19716386, ECO:0000269|PubMed:24013594, ECO:0000269|PubMed:7774813, ECO:0000305}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (18); Binding site (6); Chain (1); Disulfide bond (3); Domain (2); Frameshift (2); Glycosylation (3); Metal binding (12); Mutagenesis (6); Propeptide (1); Region (6); Repeat (3); Sequence conflict (7); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1) |
| Keywords | Alternative splicing;Calcium;Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Hydrolase;Membrane;Metal-binding;Protease;Reference proteome;Repeat;Serine protease;Signal;Transmembrane;Transmembrane helix;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10778742; 11099033; 11231151; 11381264; 12097347; 12619137; 14551910; 14704431; 15338614; 15489339; 15791247; 16122351; 17850180; 18023121; 18050450; 1936966; 20439776; 21085631; 21177967; 21367940; 22267497; 22286215; 2245913; 22560298; 23665919; 23800452; 24884423; 25487147; 25652260; 6593563; 7262541; 9230900; |
| Motif | |
| Gene Encoded By | |
| Mass | 103,015 |
| Kinetics | |
| Metal Binding | METAL 124; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P09958; METAL 211; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P09958; METAL 223; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P09958; METAL 228; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P09958; METAL 230; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09958; METAL 252; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09958; METAL 255; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P09958; METAL 257; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09958; METAL 259; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09958; METAL 305; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P09958; METAL 348; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P09958; METAL 378; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P09958 |
| Rhea ID | |
| Cross Reference Brenda |