| IED ID | IndEnz0002010616 |
| Enzyme Type ID | protease010616 |
| Protein Name |
Thrombin-like enzyme ancrod-2 SVTLE EC 3.4.21.74 Fibrinogen-clotting enzyme Snake venom serine protease SVSP Venombin A |
| Gene Name | |
| Organism | Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma) |
| 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) Calloselasma Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma) |
| Enzyme Sequence | MVLIRVLANLVILQLSYAQKSSELVIGGDECNINEHRFLVALYDSTTRNFLCGGVLIHPEWVITAKHCNKKSMVLYLGKHKQSVKFDDEQERFPKEKHFIRCNKPRTRWGEDIMLIRLNKPVNNSEHIAPLSLPSNPPIVGSVCRVMGWGSINKYIDVLPDEPRCANINLYNYTVCRGVFPRIPKKSKILCAGDLQGRLDSCHCDSGGPLICSEEFHGIVYRGPNPCAQPDKPALYTNIFDHLHWILSIMAGNATCYP |
| Enzyme Length | 258 |
| Uniprot Accession Number | P47797 |
| Absorption | |
| Active Site | ACT_SITE 67; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 112; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 206; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme.; EC=3.4.21.74; |
| DNA Binding | |
| EC Number | 3.4.21.74 |
| Enzyme Function | FUNCTION: Thrombin-like snake venom serine protease. Cleaves fibrinogen (FGA) to split of fibrinopeptides AM, AO, and AY; the aberrant fibrinogen is then incapable of being cross-linked, forming easily dispersible clots. |
| 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 | Blood coagulation cascade activating toxin;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;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:0000250 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 29,145 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |