| IED ID | IndEnz0002010101 |
| Enzyme Type ID | protease010101 |
| Protein Name |
Alpha-fibrinogenase shedaoenase EC 3.4.21.- Snake venom serine protease SVSP |
| Gene Name | |
| Organism | Gloydius shedaoensis (Shedao island pit viper) (Agkistrodon shedaoensis) |
| 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 Crotalinae (pit vipers) Gloydius Gloydius shedaoensis (Shedao island pit viper) (Agkistrodon shedaoensis) |
| Enzyme Sequence | VIGGDECNINEHRFLVALYTSRFRTLFCGGTLINQEWVLTAAHCDRKNFRIKLGIHSKKVPNEDEQTRVPKEKFFCLSSKNYTLWDKDIMLIRLDSPVKNSTHIAPFSLPSSPPSVGSVCRIMGWGRISPTEETYPDVPHCVNINLLEYEMCRVPYPEFGLPATSRTLCAGILEGGKDTCRGDSGGPLICNGQFQGIASWGDDPCAQPHKPAAYTKVFDHLDWIKSIIAGNTDASCPP |
| Enzyme Length | 238 |
| Uniprot Accession Number | Q6T5L0 |
| Absorption | |
| Active Site | ACT_SITE 43; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 88; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 184; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Its activity is completely inhibited by PMSF, and almost not inhibited by EDTA. {ECO:0000269|PubMed:16331328}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Snake venom protease that shows fibrinogenolytic activities. Preferentially degrades the alpha-chain of human fibrinogen (FGA) and slowly degrades the beta-chain (FGB). Has no effect on the gamma-chain. Can hydrolyze fibrinogen without forming fibrin clots and also can degrade fibrin. Hydrolyzes the substrate of plasmin more potently than the substrate of thrombin. Shows a preferential cleavage at Lys-|-Xaa instead of Arg-|-Xaa bonds. {ECO:0000269|PubMed:16331328}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (6); Domain (1); Erroneous initiation (1); Glycosylation (2); Motif (1); Sequence conflict (1) |
| Keywords | Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16331328}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 181..183; /note=Cell attachment site; /evidence=ECO:0000255 |
| Gene Encoded By | |
| Mass | 26,416 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |