| IED ID | IndEnz0002010103 |
| Enzyme Type ID | protease010103 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like alborhagin EC 3.4.24.- Snake venom metalloproteinase SVMP Cleaved into: Disintegrin-like alborhagin-C Fragments |
| Gene Name | |
| Organism | Trimeresurus albolabris (White-lipped pit viper) (Cryptelytrops albolabris) |
| 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) Trimeresurus Trimeresurus albolabris (White-lipped pit viper) (Cryptelytrops albolabris) |
| Enzyme Sequence | RYIPYDQEDVKRQMVAAIGIEDKNTVTRANYYTLDLXIDTVTPDVNRNELKEK |
| Enzyme Length | 53 |
| Uniprot Accession Number | P0DJH2 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Alborhagin-induced platelet aggregation, but not shape change, is inhibited by EDTA, suggesting that the platelet activation (shape change) is independent of divalent cation or metalloproteinase activity. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: [Zinc metalloproteinase-disintegrin-like alborhagin]: Induces platelet activation and glycoprotein VI (GP6)-dependent platelet aggregation. Induces ectodomain cleavage of GP6 by activating endogenous platelet metalloproteinases (probably ADAM10). Has fibrinogenolytic activity against the alpha chain of fibrinogen (FGA). Recognizes distinct binding sites as convulxin, since alborhagin has minimal effect on convulxin binding to GPVI-expressing cells. {ECO:0000269|PubMed:18064326}.; FUNCTION: Disintegrin alborhagin-C: 42 kDa fragment of alborhagin autoproteolysed that does not show platelet activation. {ECO:0000269|PubMed:18064326}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (2); Non-adjacent residues (3); Non-terminal residue (2); Sequence uncertainty (4) |
| Keywords | Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation activating toxin;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | PTM: Contains numerous disulfide bonds. {ECO:0000250}.; PTM: Glycosylated. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 6,228 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |