| IED ID | IndEnz0002007655 |
| Enzyme Type ID | protease007655 |
| Protein Name |
Clotting factor G beta subunit EC 3.4.21.85 Cleaved into: Clotting factor G beta subunit light chain; Clotting factor G beta subunit 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 | MDISFLVFITLSMALFSSNVTGTSVTSRVRRGINEKHCGFRPVITRIIGGGIATPHSWPWMVGIFKVNPHRFLCGGSIINKVSVVTAAHCLVTQFGNRQNYSIFVRVGAHDIDNSGTNYQVDKVIVHQGYKHHSHYYDIGLILLSKPVEYNDKIQPVCIPEFNKPHVNLNNIKVVITGWGVTGKATEKRNVLRELELPVVTNEQCNKSYQTLPFSKLNRGITNDMICAGFPEGGKDACQGDSGGPLMYQNPTTGRVKIVGVVSFGFECARPNFPGVYTRLSSYVNWLQEITFGQSLASLFEVVPIFIPE |
| Enzyme Length | 309 |
| Uniprot Accession Number | Q27083 |
| Absorption | |
| Active Site | ACT_SITE 89; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 138; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 242; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274 |
| Activity Regulation | ACTIVITY REGULATION: Binding to (1->3)-beta-D-glucan to alpha subunit, induces autocatalysis and activation of beta subunit (PubMed:7822328). Inhibited by intracellular coagulation inhibitor 3/LICI-3 and to a lesser extend by intracellular coagulation inhibitor 2/LICI-2 (PubMed:7822328, PubMed:8798603). {ECO:0000269|PubMed:7822328, ECO:0000269|PubMed:8798603}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage of 98-Arg-|-Ile-99 bond in Limulus proclotting enzyme to form active clotting enzyme.; EC=3.4.21.85; Evidence={ECO:0000269|PubMed:7822328, ECO:0000269|PubMed:8798603}; |
| DNA Binding | |
| EC Number | 3.4.21.85 |
| Enzyme Function | FUNCTION: Component of the heterodimer clotting factor G which may play a role in defense mechanisms against fungi (Probable). Initiates a (1->3)-beta-glucan-sensing clotting pathway whereby the alpha subunit binds to glucans containing (1->3)-beta linkages, which are components of the fungal cell wall, and the beta subunit catalyzes the activation of proclotting enzyme (PubMed:7822328). {ECO:0000269|PubMed:7822328, ECO:0000305|PubMed:7822328}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Disulfide bond (4); Domain (1); Glycosylation (2); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Glycoprotein;Hemolymph clotting;Hydrolase;Protease;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..31; /evidence=ECO:0000269|PubMed:8288603 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 34,265 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |