| IED ID | IndEnz0002010997 |
| Enzyme Type ID | protease010997 |
| Protein Name |
Proclotting enzyme EC 3.4.21.86 Cleaved into: Proclotting enzyme light chain; Proclotting enzyme heavy chain |
| Gene Name | |
| Organism | Tachypleus tridentatus (Japanese horseshoe crab) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Chelicerata Merostomata (horseshoe crabs) Xiphosura Limulidae Tachypleus Tachypleus tridentatus (Japanese horseshoe crab) |
| Enzyme Sequence | MLVNNVFSLLCFPLLMSVVRCSTLSRQRRQFVFPDEEELCSNRFTEEGTCKNVLDCRILLQKNDYNLLKESICGFEGITPKVCCPKSSHVISSTQAPPETTTTERPPKQIPPNLPEVCGIHNTTTTRIIGGREAPIGAWPWMTAVYIKQGGIRSVQCGGALVTNRHVITASHCVVNSAGTDVMPADVFSVRLGEHNLYSTDDDSNPIDFAVTSVKHHEHFVLATYLNDIAILTLNDTVTFTDRIRPICLPYRKLRYDDLAMRKPFITGWGTTAFNGPSSAVLREVQLPIWEHEACRQAYEKDLNITNVYMCAGFADGGKDACQGDSGGPMMLPVKTGEFYLIGIVSFGKKCALPGFPGVYTKVTEFLDWIAEHMV |
| Enzyme Length | 375 |
| Uniprot Accession Number | P21902 |
| Absorption | |
| Active Site | ACT_SITE 172; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 228; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 326; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by intracellular coagulation inhibitor 2/LICI-2 and to a lesser extent by intracellular coagulation inhibitor 3/LICI-3. {ECO:0000269|PubMed:7822280, ECO:0000269|PubMed:8798603}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage of 18-Arg-|- and 47-Arg-|- bonds in coagulogen to form coagulin and fragments.; EC=3.4.21.86; Evidence={ECO:0000269|PubMed:977558, ECO:0000305|PubMed:4030738, ECO:0000305|PubMed:7822280, ECO:0000305|PubMed:7822328, ECO:0000305|PubMed:8798603}; |
| DNA Binding | |
| EC Number | 3.4.21.86 |
| Enzyme Function | FUNCTION: This enzyme is closely associated with an endotoxin-sensitive hemolymph coagulation system in limulus (PubMed:2266134). Its active form catalyzes the conversion of coagulogen to insoluble coagulin gel (PubMed:977558, PubMed:7822328). {ECO:0000269|PubMed:2266134, ECO:0000269|PubMed:7822328, ECO:0000269|PubMed:977558}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Disulfide bond (7); Domain (2); Glycosylation (3); Metal binding (4); Modified residue (1); Propeptide (1); Region (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Cleavage on pair of basic residues;Cytoplasmic vesicle;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemolymph clotting;Hydrolase;Metal-binding;Protease;Pyrrolidone carboxylic acid;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:2266134}. Secreted {ECO:0000269|PubMed:2266134}. Note=Secreted in hemolymph probably upon bacterial lipopolysaccharide (LPS) stimulation. {ECO:0000303|PubMed:2266134}. |
| Modified Residue | MOD_RES 30; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:2266134 |
| Post Translational Modification | PTM: Proteolytically cleaved into its mature active form by serine protease factor B (PubMed:2266134, PubMed:4030738). Cleavage produces a 25 kDa light chain containing the CLIP domain and a catalytic 31 kDa heavy chain which remain covalently associated through an interchain disulfide bond (PubMed:2266134, PubMed:4030738). Proteolytically cleaved by clotting factor G subunit beta (PubMed:7822328). {ECO:0000269|PubMed:2266134, ECO:0000269|PubMed:4030738, ECO:0000269|PubMed:7822328}.; PTM: Contains six O-linked carbohydrate chains in the N-terminal light chain. {ECO:0000269|PubMed:2266134, ECO:0000269|PubMed:4030738}. |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 41,592 |
| Kinetics | |
| Metal Binding | METAL 194; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O97366; METAL 196; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O97366; METAL 199; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O97366; METAL 202; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O97366 |
| Rhea ID | |
| Cross Reference Brenda |