| IED ID | IndEnz0002012416 |
| Enzyme Type ID | protease012416 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like daborhagin-K EC 3.4.24.- Haemorrhagic metalloproteinase russelysin Snake venom metalloproteinase SVMP |
| Gene Name | |
| Organism | Daboia russelii (Russel's viper) (Vipera russelii) |
| 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) Daboia Daboia russelii (Russel's viper) (Vipera russelii) |
| Enzyme Sequence | MMQVLLVTICLAVFPYHGSSIILESGNVNDYEVVYPQKVTAMPKEAVKQPEQKYEDAMQYKFEVNGEPVLLHLEKNKDLFSEDYSETHYSPDGREITTKPLVQDHCYYHGHIQNDAHSSASISACNGLKGHFKLRGEMYLIEPLKLSDSEAHAVYKYENVEKEDEALKMCGVTQTNWESDEPIKKASLLVATSERNRYFNPYSYVELIITVDHSMVTKYKNDLTAIRTWVFELVNTINEIFKYLYIRVPLVGLEIWKNRDLINVTSAANVTLDLFGEWRKSYLLPRKIHDNSQLLTAIDLNGLTIGMAYVSTMCQSKYSVGVVQDHSKINLRVAVTMAHEIGHNLGLTHDGVYCTCGGYSCIMSAVLGDQPSKYFSNCSYNQYRRFLTEHNPECIINPPLRTDIVSPPACGNELLERGEECDCGSPENCRDPCCDAASCKLHSWVECESGKCCNQCRFKRAGTECRPARDECDKAEQCTGRSANCPVDEFHENGRPCLHNFGYCYNGKCPIMYHQCHALFGQNVTGVQDSCFQYNRLGVYYAYCRKENGRKIPCAPKDEKCGRLYCSYKSPGNQIPCLPYYIPSDENKGMVDHGTKCGDGKVCSNGQCVDLNIAY |
| Enzyme Length | 615 |
| Uniprot Accession Number | B8K1W0 |
| Absorption | |
| Active Site | ACT_SITE 340; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Addition of Mg(2+) or Ca(2+) increases the casein hydrolysis rate. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloprotease that possesses high hemorrhagic activity (minimum hemorrhagic dose (MHD)=0.82 ug) when subcutaneously injected into mice. May also potently degrade alpha chain of fibrinogen (FGA). |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (17); Domain (2); Glycosylation (4); Metal binding (12); Motif (1); Propeptide (1); Signal peptide (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 471..473; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 69,555 |
| Kinetics | |
| Metal Binding | METAL 206; /note=Calcium 1; /evidence=ECO:0000250; METAL 290; /note=Calcium 1; /evidence=ECO:0000250; METAL 339; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 343; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 349; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 394; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 397; /note=Calcium 1; /evidence=ECO:0000250; METAL 412; /note=Calcium 2; /evidence=ECO:0000250; METAL 414; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 416; /note=Calcium 2; /evidence=ECO:0000250; METAL 419; /note=Calcium 2; /evidence=ECO:0000250; METAL 422; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |