| IED ID | IndEnz0002003909 |
| Enzyme Type ID | protease003909 |
| Protein Name |
Clotting factor C FC EC 3.4.21.84 Limulus factor C Cleaved into: Clotting factor C heavy chain; Clotting factor C light chain; Clotting factor C chain A; Clotting factor C chain B |
| 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 | MVLASFLVSGLVLGILAQQMRPVQSRGVDLGLCDETRFECKCGDPGYVFNVPMKQCTYFYRWRPYCKPCDDLEAKDICPKYKRCQECKAGLDSCVTCPPNKYGTWCSGECQCKNGGICDQRTGACTCRDRYEGAHCEILKGCPLLPSDSQVQEVRNPPDNPQTIDYSCSPGFKLKGVARISCLPNGQWSSFPPKCIRECAKVSSPEHGKVNAPSGNMIEGATLRFSCDSPYYLIGQETLTCQGNGQWSGQIPQCKKLVFCPDLDPVNHAEHQVKIGVEQKYGQFPQGTEVTYTCSGNYFLMGFNTLKCNPDGSWSGSQPSCVKVADREVDCDSKAVDFLDDVGEPVRIHCPAGCSLTAGTVWGTAIYHELSSVCRAAIHAGKLPNSGGAVHVVNNGPYSDFLGSDLNGIKSEELKSLARSFRFDYVSSSTAGRSGCPDGWFEVEENCVYVTSKQRAWERAQGVCTNMAARLAVLDKDLIPSSLTETLRGKGLTTTWIGLHRLDAEKPFVWELMDRSNVVLNDNLTFWASGEPGNETNCVYLDIRDQLQPVWKTKSCFQPSSFACMMDLSDRNKAKCDDPGPLENGHATLHGQSIDGFYAGSSIRYSCEVLHYLSGTETVTCTTNGTWSAPKPRCIKVITCQNPPVPSYGSVEIKPPSRTNSISRVGSPFLRLPRLPLPLARAAKPPPKPRSSQPSTVDLASKVKLPEGHYRVGSRAIYTCESRYYELLGSQGRRCDSNGNWSGRPASCIPVCGRSDSPRSPFIWNGNSTEIGQWPWQAGISRWLADHNMWFLQCGGSLLNEKWIVTAAHCVTYSATAEIIDPSQFKIYLGKYYRDDSRDDDYVQVREALEIHVNPNYDPGNLNFDIALIQLKTPVTLTTRVQPICLPTDITTREHLKEGTLAVVTGWGLNENNTYSEMIQQAVLPVVAASTCEEGYKEADLPLTVTENMFCAGYKKGRYDACSGDSGGPLVFADDSRTERRWVLEGIVSWGSPSGCGKANQYGGFTKVNVFLSWIRQFI |
| Enzyme Length | 1019 |
| Uniprot Accession Number | P28175 |
| Absorption | |
| Active Site | ACT_SITE 809; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 865; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 966; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274 |
| Activity Regulation | ACTIVITY REGULATION: Activated by Gram-negative bacterial lipopolysaccharides (PubMed:3512266). Inhibited by intracellular coagulation inhibitor 1/LICI-1 and to a lesser extent by intracellular coagulation inhibitors 2/LICI-2 and 3/LICI-3 (PubMed:8276848, PubMed:7822280, PubMed:8798603). Inhibited by the small molecule diisopropyl fluorophosphate (DFP) (PubMed:3512266). {ECO:0000269|PubMed:3512266, ECO:0000269|PubMed:7822280, ECO:0000269|PubMed:8276848, ECO:0000269|PubMed:8798603}. |
| Binding Site | BINDING 960; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage of 103-Arg-|-Ser-104 and 124-Ile-|-Ile-125 bonds in Limulus clotting factor B to form activated factor B. Cleavage of -Pro-Arg-|-Xaa- bonds in synthetic substrates.; EC=3.4.21.84; Evidence={ECO:0000269|PubMed:3512266, ECO:0000269|PubMed:7822280, ECO:0000269|PubMed:8276848, ECO:0000269|PubMed:8798603}; |
| DNA Binding | |
| EC Number | 3.4.21.84 |
| Enzyme Function | FUNCTION: This enzyme is closely associated with an endotoxin-sensitive hemolymph coagulation system which may play important roles in both hemostasis and host defense mechanisms (PubMed:3512266). Its active form catalyzes the activation of clotting factor B (PubMed:3512266). {ECO:0000269|PubMed:3512266}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Alternative sequence (2); Binding site (1); Chain (5); Disulfide bond (19); Domain (9); Glycosylation (6); Signal peptide (1) |
| Keywords | Alternative splicing;Cell adhesion;Direct protein sequencing;Disulfide bond;EGF-like domain;Glycoprotein;Hemolymph clotting;Hydrolase;Lectin;Protease;Repeat;Secreted;Serine protease;Signal;Sushi |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Note=Secreted in hemolymph (PubMed:2007602). Localizes in large granules of hemocytes (PubMed:2007602). {ECO:0000269|PubMed:2007602}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:3512266}.; PTM: Lipopolysaccharide (LPS) activates clotting factor C by inducing the proteolytic cleavage of the clotting factor C light chain into clotting factor C chains A and B (PubMed:3308457, PubMed:3512266). Clotting factor C chains heavy, A and B remain associated via interchain disulfide bonds (PubMed:3512266). {ECO:0000269|PubMed:3308457, ECO:0000269|PubMed:3512266}. |
| Signal Peptide | SIGNAL 1..25 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 112,346 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |