| IED ID | IndEnz0002014592 |
| Enzyme Type ID | protease014592 |
| Protein Name |
Endoprotease bli EC 3.4.21.75 Blisterase |
| Gene Name | Bli |
| Organism | Onchocerca volvulus |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Spirurina Spiruromorpha Filarioidea Onchocercidae Onchocerca Onchocerca volvulus |
| Enzyme Sequence | MYWQLVRILVLFDCLQKILAIEHDSICIADVDDACPEPSHTVMRLRERNDKKAHLIAKQHGLEIRGQPFLDGKSYFVTHISKQRSRRRKREIISRLQEHPDILSIEEQRPRVRRKRDFLYPDIAHELAGSSTNIRHTGLISNTEPRIDFIQHDAPVLPFPDPLYKEQWYLNNGAQGGFDMNVQAAWLLGYAGRNISVSILDDGIQRDHPDLAANYDPLASTDINGHDDDPTPQDDGDNKHGTRCAGEVASIAGNVYCGVGVAFHAKIGGVRMLDGPVSDSVEAASLSLNRHHIDIYSASWGPEDDGRTFDGPGPLAREAFYRGVKAGRGGKGSIFVWASGNGGSRQDSCSADGYTTSVYTLSVSSATIDNRSPWYLEECPSTIATTYSSANMNQPAIITVDVPHGCTRSHTGTSASAPLAAGIIALALEANPNLTWRDMQHIVLRTANPVPLLNNPGWSVNGVGRRINNKFGYGLMDAGALVKLALIWKTVPEQHICTYDYKLEKPNPRPITGNFQMNFSLEVNGCESGTPVLYLEHVQVLATFRFGKRGDLKLTLFSPRGTSSVLLPPRPQDFNSNGIHKWPFLSVQTWGEDPRGKWTLMVESVSTNRNVGGTFHDWSLLLYGTAEPAQPNDPRHSSVVPSSVSAESPFDRITQHIASQEKKKKQRDSRDWQPKKVENKKSLLVSAQPELRV |
| Enzyme Length | 693 |
| Uniprot Accession Number | A0A044RE18 |
| Absorption | |
| Active Site | ACT_SITE 201; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 240; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 414; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the propeptide before the second cleavage. Inhibited by ethylenediaminetetraacetic acid (EDTA), ZnSO(4) and chloroketone DEC-RVKR-CMK. {ECO:0000269|PubMed:12855702}. |
| Binding Site | BINDING 202; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 282; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 310; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 352; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 354; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P09958; BINDING 414; /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:0000269|PubMed:12855702}; |
| DNA Binding | |
| EC Number | 3.4.21.75 |
| Enzyme Function | FUNCTION: Serine endoprotease which cleaves substrates at the RX(K/R)R consensus motif. {ECO:0000269|PubMed:12855702}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. Active from pH 7.0 to 8.5. {ECO:0000269|PubMed:12855702}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (6); Chain (1); Compositional bias (3); Disulfide bond (3); Domain (2); Glycosylation (3); Metal binding (12); Propeptide (1); Region (5); Sequence conflict (1); Signal peptide (1); Site (2) |
| Keywords | Autocatalytic cleavage;Calcium;Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:12855702}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:12855702}.; PTM: The inhibition peptide, which plays the role of an intramolecular chaperone, is probably autocatalytically removed in the endoplasmic reticulum (ER) and remains non-covalently bound as a potent autoinhibitor. Probably following transport to the trans Golgi, a second cleavage within the inhibition propeptide results in propeptide dissociation and bli activation. {ECO:0000269|PubMed:12855702}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 76,800 |
| Kinetics | |
| Metal Binding | METAL 161; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P09958; METAL 210; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P09958; METAL 222; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P09958; METAL 227; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P09958; METAL 229; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09958; METAL 251; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09958; METAL 254; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P09958; METAL 256; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09958; METAL 258; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P09958; METAL 304; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P09958; METAL 347; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P09958; METAL 377; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P09958 |
| Rhea ID | |
| Cross Reference Brenda |