| IED ID | IndEnz0002012737 |
| Enzyme Type ID | protease012737 |
| Protein Name |
Zinc metalloproteinase barnettlysin-1 EC 3.4.24.- Barnettlysin-I Snake venom metalloproteinase SVMP |
| Gene Name | |
| Organism | Bothrops barnetti (Barnett's lancehead) (Trimeresurus barnetti) |
| 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) Bothrops Bothrops barnetti (Barnett's lancehead) (Trimeresurus barnetti) |
| Enzyme Sequence | TPEQQRYVELFIVVDHGMFMKXXXXXXXXXXXIHQMVNIMKEAYRYLYIDILLTGVEIWSNKDLINVQPAAPQTLDSFGEWRXXXXXXXKSHDNAQLLTSTDFDGPTIGLAYVGSMCDPKRSTAVIQDHSEIDLLVAVTMDHELGHNLGIRHDTGSCSCGGYPCVMSPVISHDISKYFSDCSYIQCWDFIMKENPQCILNKR |
| Enzyme Length | 202 |
| Uniprot Accession Number | P86976 |
| Absorption | |
| Active Site | ACT_SITE 143; /evidence="ECO:0000250|UniProtKB:P60244, ECO:0000255|PROSITE-ProRule:PRU00276" |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Non-hemorrhagic metalloproteinase that hydrolyzes the alpha chains of fibrinogen and fibrin but has no activity on beta- and gamma-chains. Cleaves X-Leu bonds. Inhibits platelet aggregation induced by the von Willebrand factor (VWF) (IC(50) is 1.4 uM) and type I collagen (IC(50) is 3.2 uM). Acts by cleaving the vWF and its receptor GPIb, and by cleaving the collagen-binding Alpha-2A domain of the collagen receptor alpha-2/beta-1 integrin (ITGA2/ITGB1). Also degrades the extracellular matrix protein fibronectin (FN1), but has no effect on laminin and type I collagen. {ECO:0000269|PubMed:26723171}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (3); Domain (1); Metal binding (7) |
| Keywords | Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26723171}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 22,927 |
| Kinetics | |
| Metal Binding | METAL 9; /note="Calcium"; /evidence="ECO:0000250"; METAL 93; /note="Calcium"; /evidence="ECO:0000250"; METAL 142; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:P60244, ECO:0000255|PROSITE-ProRule:PRU00276"; METAL 146; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:P60244, ECO:0000255|PROSITE-ProRule:PRU00276"; METAL 152; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:P60244, ECO:0000255|PROSITE-ProRule:PRU00276"; METAL 197; /note="Calcium; via carbonyl oxygen"; /evidence="ECO:0000250"; METAL 200; /note="Calcium"; /evidence="ECO:0000250" |
| Rhea ID | |
| Cross Reference Brenda |