| IED ID | IndEnz0002011559 |
| Enzyme Type ID | protease011559 |
| Protein Name |
Factor X-activator 1 heavy chain VAFXA-I HC EC 3.4.24.- Snake venom metalloproteinase SVMP Fragment |
| Gene Name | |
| Organism | Vipera ammodytes ammodytes (Western sand 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 ammodytes (Nose-horned viper) Vipera ammodytes ammodytes (Western sand viper) |
| Enzyme Sequence | LVSVSPAFNGNYFVE |
| Enzyme Length | 15 |
| Uniprot Accession Number | P0C8I7 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Catalytic subunit of blood coagulation factor X-activating enzyme. Activates coagulation factor X (F10) in a calcium-dependent manner by cleaving at the '234-Arg-|-Ile-235' site. Weakly hydrolyzes insulin B chain (by cleaving at the '27-Asn-|-Gln-28' and '44-Gly-|-Glu-45' sites), fibrinogen and some components of the extracellular matrix in vitro. {ECO:0000269|PubMed:18760294}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Domain (1); Metal binding (3); Non-terminal residue (1) |
| Keywords | Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 1,643 |
| Kinetics | |
| Metal Binding | METAL 11; /note=Calcium; /evidence=ECO:0000250; METAL 13; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 15; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |