| IED ID | IndEnz0002010158 |
| Enzyme Type ID | protease010158 |
| Protein Name |
Snaclec coagulation factor X-activating enzyme light chain 2 Factor X activator LC2 Fragment |
| Gene Name | |
| Organism | Vipera aspis aspis (Aspic viper) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Lepidosauria (lepidosaurs) Squamata (squamates) Bifurcata (split-tongued squamates) Unidentata Episquamata Toxicofera Serpentes (snakes) Colubroidea Viperidae Viperinae (vipers) Vipera Vipera aspis (Aspic viper) Vipera aspis aspis (Aspic viper) |
| Enzyme Sequence | AFCCPSGWSAYDQ |
| Enzyme Length | 13 |
| Uniprot Accession Number | Q7LZ24 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Regulatory subunit of coagulation factor X-activating enzyme, a zinc-protease enzyme that impairs hemostasis in envenomed animal. Activates coagulation factor X (F10) in a calcium-dependent manner probably by cleaving the Arg-Ile bond at position 234. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Non-terminal residue (1) |
| Keywords | Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Lectin;Metal-binding;Secreted;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 1,435 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |