| IED ID | IndEnz0002009848 |
| Enzyme Type ID | protease009848 |
| Protein Name |
Vaa serine proteinase homolog 1 VaaSPH-1 Enzymatically inactive serine proteinase-like protein SPH-1 Snake venom serine protease homolog |
| 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 | MVLIRVLANLLVLQLSYAQKSSELVIGGDECNINEHPFLVALHTARSKRFYCAGTLINQEWVLTAARCDRKNIRIILGVHSKNVPNEDEQMRVPKEKFFCLSSKTYTRWDKDIMLIRLKRPVNDSTHIAPLSLPSSPPSVGSVCRIMGWGTITTTKVTYPDVPHCADINMFDYSVCQKVYRKLPEKSRTLCAGILQGGIDSCKVDNGGPLICNGQIQGIVSWGGYPCAQPHKPALYTNVFDYTDWIQSIIAGNITATCPP |
| Enzyme Length | 260 |
| Uniprot Accession Number | A0A1I9KNP0 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: This is the first member of the serine protease family that has strong anticoagulant activity and lacks enzymatic activity. It inhibits activities of three blood coagulation complexes: (1) prothrombinase complex (composed of blood coagulation factors Va and Xa (F5 and F10)) (IC(50)=164.1 nM), (2) intrinsic tenase complex (composed of factors VIIIa and IXa (F8 and F9)), and (3) extrinsic tenase complex (composed of tissue factor and factor VIIa (F7)). The toxin has also been observed to bind prothrombin, factor FVa, non-activated and activated forms of factors FVII (F7) (FVII and FVIIa), factor FVIIIa (F8), factors FIX and FIXa (F9) and factors FX and FXa (F10). The toxin inhibits the activity of the intrinsic tenase complex mainly by competing with FIXa (F9) for binding to FVIIIa (F8). {ECO:0000269|PubMed:30235482}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (6); Domain (1); Glycosylation (2); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Blood coagulation cascade inhibiting toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Pharmaceutical;Secreted;Serine protease homolog;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30235482}. |
| Modified Residue | |
| Post Translational Modification | PTM: N-glycosylated. The toxin exists in multiple glycoforms. {ECO:0000269|PubMed:30235482}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,928 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.74; |