| IED ID | IndEnz0002004276 |
| Enzyme Type ID | protease004276 |
| Protein Name |
Limulus clotting factor C FC EC 3.4.21.84 Cleaved into: Limulus clotting factor C heavy chain; Limulus clotting factor C light chain; Limulus clotting factor C chain A; Limulus clotting factor C chain B |
| Gene Name | |
| Organism | Carcinoscorpius rotundicauda (Mangrove horseshoe crab) (Limulus rotundicauda) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Chelicerata Merostomata (horseshoe crabs) Xiphosura Limulidae Carcinoscorpius Carcinoscorpius rotundicauda (Mangrove horseshoe crab) (Limulus rotundicauda) |
| Enzyme Sequence | MVLASFLVSGLVLGLLAQKMRPVQSKGVDLGLCDETRFECKCGDPGYVFNIPVKQCTYFYRWRPYCKPCDDLEAKDICPKYKRCQECKAGLDSCVTCPPNKYGTWCSGECQCKNGGICDQRTGACACRDRYEGVHCEILKGCPLLPSDSQVQEVRNPPDNPQTIDYSCSPGFKLKGMARISCLPNGQWSNFPPKCIRECAMVSSPEHGKVNALSGDMIEGATLRFSCDSPYYLIGQETLTCQGNGQWNGQIPQCKNLVFCPDLDPVNHAEHKVKIGVEQKYGQFPQGTEVTYTCSGNYFLMGFDTLKCNPDGSWSGSQPSCVKVADREVDCDSKAVDFLDDVGEPVRIHCPAGCSLTAGTVWGTAIYHELSSVCRAAIHAGKLPNSGGAVHVVNNGPYSDFLGSDLNGIKSEELKSLARSFRFDYVRSSTAGKSGCPDGWFEVDENCVYVTSKQRAWERAQGVCTNMAARLAVLDKDVIPNSLTETLRGKGLTTTWIGLHRLDAEKPFIWELMDRSNVVLNDNLTFWASGEPGNETNCVYMDIQDQLQSVWKTKSCFQPSSFACMMDLSDRNKAKCDDPGSLENGHATLHGQSIDGFYAGSSIRYSCEVLHYLSGTETVTCTTNGTWSAPKPRCIKVITCQNPPVPSYGSVEIKPPSRTNSISRVGSPFLRLPRLPLPLARAAKPPPKPRSSQPSTVDLASKVKLPEGHYRVGSRAIYTCESRYYELLGSQGRRCDSNGNWSGRPASCIPVCGRSDSPRSPFIWNGNSTEIGQWPWQAGISRWLADHNMWFLQCGGSLLNEKWIVTAAHCVTYSATAEIIDPNQFKMYLGKYYRDDSRDDDYVQVREALEIHVNPNYDPGNLNFDIALIQLKTPVTLTTRVQPICLPTDITTREHLKEGTLAVVTGWGLNENNTYSETIQQAVLPVVAASTCEEGYKEADLPLTVTENMFCAGYKKGRYDACSGDSGGPLVFADDSRTERRWVLEGIVSWGSPSGCGKANQYGGFTKVNVFLSWIRQFI |
| Enzyme Length | 1019 |
| Uniprot Accession Number | Q26422 |
| Absorption | |
| Active Site | ACT_SITE 809; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 865; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 966; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Activated by Gram-negative bacterial lipopolysaccharides and chymotrypsin. {ECO:0000250}. |
| 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; |
| 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. Its active form catalyzes the activation of factor B. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Binding site (1); Chain (5); Disulfide bond (20); Domain (9); Glycosylation (6); Signal peptide (1) |
| Keywords | Cell adhesion;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. Note=Secreted in hemolymph. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 112,430 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.84; |