| IED ID | IndEnz0002013467 |
| Enzyme Type ID | protease013467 |
| Protein Name |
Zinc metalloproteinase/disintegrin Cleaved into: Snake venom metalloproteinase lebetase SVMP EC 3.4.24.- Fibrinolytic protease Le-3 Le3 Lebetase II Lebetase-2 ; Disintegrin VLE5A |
| Gene Name | |
| Organism | Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
| 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) Macrovipera Macrovipera lebetina (Levantine viper) (Vipera lebetina) |
| Enzyme Sequence | MIQVLLVTICLAVFPYQGSSKTLKSGNVNDYEVVNPQAVTGLPKGAVKQPEKKYEDTMQYEFEVNGEPVVLHLEKNRGLFSKDYSETHYSPDGREITTNPAVEDHCYYHGRIQNDADSTASISACNGLKGYFTLRGETYLIEPLKLPDSEAHAVYKYENIEKEDEAPKMCGVTQTNWASDEPIKKASQLNLTPEQQRFEPRYIELVIVADHAMVTKYNGDLAAITTWVHQLVNNINGFYRDLNVHITLSAVEVWTNGDLINVQPAASVTLNLFGEWRERDLLNRRMHDHAQLLTGIDLDDNIIGLAYDDSMCDPRYSVGIVQDHSAIIRLVAVTMAHELGHNLGMNHDGDQCNCGANGCVMSVVLIEQRSYQFSDCSKNKYQTYLTNRNPQCILNQPLRTDTVSTPVSGNELLQNSGNPCCDPVTCQPRRGEHCVSGKCCRNCKFLRAGTVCKRAVGDDMDDYCTGISSDCPRNPYKD |
| Enzyme Length | 478 |
| Uniprot Accession Number | Q98995 |
| Absorption | |
| Active Site | ACT_SITE 338; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Fibrinolytic and caseinolytic activities are inhibited by Cd(2+), Cu(2+) and Co(2+) ions. Not inhibited by Mg(2+), Ca(2+) and Ba(2+). Also inhibited by EDTA, EGTA and 1,10-phenanthroline. {ECO:0000269|PubMed:2065076, ECO:0000269|PubMed:9678676}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: [Snake venom metalloproteinase lebetase]: Fibrinolytic and fibrinogenolytic metalloproteinase that hydrolyzes the Aalpha-chain and more slowly the Bbeta-chain of fibrin and fibrinogen. Its fibrinolytic activity is direct, without any plasminogen activation. Also hydrolyzes casein and B-chain of oxidized insulin. Inhibits ADP-induced and collagen-induced platelet aggregation. Shows low hemorrhagic activity. Cleaves the plasma proteinase inhibitors alpha(2)-macroglobulin (A2M) and pregnancy zone protein (PZP), and is inhibited by them. The metalloprotease has no strict P1-P1' specificity requirement. Hydrolysis at sites with a Pro residue at P1 is observed with bradykinin, substance P, PZP and alpha chain fibrinogen (FGA) (PubMed:11910177). {ECO:0000269|PubMed:10556563, ECO:0000269|PubMed:10669797, ECO:0000269|PubMed:11910177, ECO:0000269|PubMed:2065076, ECO:0000269|PubMed:8694817, ECO:0000269|PubMed:9678676}.; FUNCTION: [Disintegrin VLE5A]: Poor inhibitor of platelet aggregation. The disintegrin inhibits the adhesion of the alpha-4/beta-1 (ITGA4/ITGB1) integrin to VCAM-1. Inhibition on alpha-2b/beta-3 (ITGA2B/ITGB3) is low (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Disulfide bond (7); Domain (2); Metal binding (7); Modified residue (1); Motif (1); Propeptide (2); Signal peptide (1) |
| Keywords | Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 195; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 456..458; /note=Cell attachment site; atypical (VGD) |
| Gene Encoded By | |
| Mass | 53,480 |
| Kinetics | |
| Metal Binding | METAL 204; /note=Calcium; /evidence=ECO:0000250; METAL 288; /note=Calcium; /evidence=ECO:0000250; METAL 337; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 341; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 347; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 392; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 395; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |