| IED ID | IndEnz0002013333 |
| Enzyme Type ID | protease013333 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like ecarin EC 3.4.24.- Snake venom metalloproteinase SVMP |
| Gene Name | |
| Organism | Echis carinatus (Saw-scaled 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) Echis Echis carinatus (Saw-scaled viper) |
| Enzyme Sequence | MIQILLVIICLAVFPYQGCSIILGSGNVNDYEVVYPQKVTALPKGAVQQPEQKYEDAMQYEFEVKGEPVVLHLEKNKELFSEDYSETHYSSDDREITTNPSVEDHCYYHGRIQNDAESTASISACNGLKGHFKLRGETYFIEPLKIPDSEAHAVYKYENIENEDEAPKMCGVTQDNWESDEPIKKTLGLIVPPHERKFEKKFIELVVVVDHSMVTKYNNDSTAIRTWIYEMLNTVNEIYLPFNIRVALVGLEFWCNGDLINVTSTADDTLHSFGEWRASDLLNRKRHDHAQLLTNVTLDHSTLGITFVYGMCKSDRSVELILDYSNITFNMAYIIAHEMGHSLGMLHDTKFCTCGAKPCIMFGKESIPPPKEFSSCSYDQYNKYLLKYNPKCILDPPLRKDIASPAVCGNEIWEEGEECDCGSPADCRNPCCDAATCKLKPGAECGNGECCDKCKIRKAGTECRPARDDCDVAEHCTGQSAECPRNEFQRNGQPCLNNSGYCYNGDCPIMLNQCIALFSPSATVAQDSCFQRNLQGSYYGYCTKEIGYYGKRFPCAPQDVKCGRLYCLDNSFKKNMRCKNDYSYADENKGIVEPGTKCEDGKVCINRKCVDVNTAY |
| Enzyme Length | 616 |
| Uniprot Accession Number | Q90495 |
| Absorption | |
| Active Site | ACT_SITE 338; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloproteinase that catalyzes the conversion of prothrombin (F2) to alpha-thrombin through formation of a thrombin intermediate. Has a low Km for prothrombin and a high kcat. Cleaves the 320-Arg-Ile-321 bond in prothrombin and produces meizothrombin which is ultimately converted to alpha-thrombin by autolysis. {ECO:0000269|PubMed:956136}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (17); Domain (2); Glycosylation (5); Metal binding (11); Motif (1); Propeptide (1); Signal peptide (1) |
| Keywords | Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Prothrombin activator;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7849037}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 469..471; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 69,463 |
| Kinetics | |
| Metal Binding | METAL 204; /note=Calcium 1; /evidence=ECO:0000250; METAL 288; /note=Calcium 1; /evidence=ECO:0000250; METAL 337; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 341; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 347; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 392; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 395; /note=Calcium 1; /evidence=ECO:0000250; METAL 410; /note=Calcium 2; /evidence=ECO:0000250; METAL 414; /note=Calcium 2; /evidence=ECO:0000250; METAL 417; /note=Calcium 2; /evidence=ECO:0000250; METAL 420; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.60; |