| IED ID | IndEnz0002009956 |
| Enzyme Type ID | protease009956 |
| Protein Name |
Alpha-fibrinogenase VLAF EC 3.4.21.- Snake venom serine protease SVSP |
| Gene Name | |
| Organism | Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
| 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) Macrovipera Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
| Enzyme Sequence | MVLIRVLANLVMLHLSYGEKSSELVIGGRPCNINQHRSLALLYNSSGFLCGGTLINQQWVLSAAHCDMENMQIYLGLHNFSLPNMDQKRRVAEEKFFCLSNKSYTKWDKDIMLIKLNRRVKTSTHIAPLSLPSNPPRLRSVCRIMGWGSITSPRETLPYVPHCANIMILRYWVCRAIYGSLPAKSRTLCAGVPRRRIGSCLGDSGGPLICNGQIQGIASWGSDPCVNHGAPGVYTKVFDYNDWIQSIIAGNTAATCPP |
| Enzyme Length | 258 |
| Uniprot Accession Number | Q8JH85 |
| Absorption | |
| Active Site | ACT_SITE 65; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 110; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 204; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP) and PMSF, and partially by soybean trypsin inhibitor, but not by EDTA. {ECO:0000269|PubMed:3304428}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Degrades alpha chain of fibrinogen (FGA), and has strong caseinolytic activity. Cleaves oxidized insulin B-chain at '40-Tyr-|-Leu-41', '48-Phe-|-Phe-49' and '49-Phe-|-Tyr-50', and glucagon at the bonds '62-Tyr-|-Ser-63', 66-Leu-|-Asp-67' and '78-Leu-|-Met-79' bonds. {ECO:0000269|PubMed:11910177, ECO:0000269|PubMed:3304428}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (3); Propeptide (1); Signal peptide (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Sialic acid;Signal;Toxin;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylated. Contains 8.5% of hexoses, 5.8% of hexosamines and 0.8% of sialic acids. {ECO:0000269|PubMed:11602278}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 28,608 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.74; |