| IED ID | IndEnz0002012438 |
| Enzyme Type ID | protease012438 |
| Protein Name |
Thrombin-like enzyme cerastocytin SVTLE EC 3.4.21.- C.cerastes platelet proaggregant protein CC-PPP Factor VIII activator Fibrinogen-clotting enzyme Proaggregant serine proteinase Snake venom serine protease SVSP |
| Gene Name | |
| Organism | Cerastes cerastes (Horned desert 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) Cerastes Cerastes cerastes (Horned desert viper) |
| Enzyme Sequence | MVLISVLASLLVLQLSYAQKSSELVIGGAECNINEHRSLVLLYNSSRLFGGGTLINKEWVLSAAHCDGENMKIYLGLHHFRLPNKDRQIRVAKEKYFCRDRKSIVDKDIMLIKLNKPVNNSTHIAPLSLPSSPPSVGSDCRIMGWGTITSPNDTYPKVPHCANINILEHSLCERAYNDLSASSRTLCAGIEKGGIDTCKGDSGGPLICNGQIQGIVSWGDEVCGKPNKPGVYTKVFDYTDWIRNIIAGNTAATCPQ |
| Enzyme Length | 256 |
| Uniprot Accession Number | Q7SYF1 |
| Absorption | |
| Active Site | ACT_SITE 65; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 108; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 202; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | ACTIVITY REGULATION: Its platelets aggregating activity is inhibited by chlorpromazine, theophylline mepacrine. Its platelet aggregating activity and its amidolytic activity are inhibited by PMSF, TPCK, TLCK and soybean trypsin inhibitors. Is unaffected by hirudin or by antithrombin-III in the presence of heparin. {ECO:0000269|PubMed:7766651}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Thrombin-like snake venom serine protease which potently induces platelet aggregation and has fibrinogenolytic activities. Clots purified fibrinogen and hydrolyzes alpha-chains (FGA). High concentrations of this enzyme also cleave prothrombin (F2) and factor X (F10). Is also able to activate factor XIII (F8). {ECO:0000269|PubMed:12962484, ECO:0000269|PubMed:7766651, ECO:0000269|PubMed:9080583}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (5); Domain (1); Glycosylation (4); Propeptide (1); Sequence conflict (1); Signal peptide (1) |
| Keywords | Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Platelet aggregation activating toxin;Protease;Secreted;Serine protease;Signal;Toxin;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 27,974 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=309 uM for S-2238 {ECO:0000269|PubMed:12962484}; KM=850 uM for S-2251 {ECO:0000269|PubMed:12962484}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |