| IED ID | IndEnz0002010884 |
| Enzyme Type ID | protease010884 |
| Protein Name |
Zinc metalloproteinase/disintegrin Cleaved into: Snake venom metalloproteinase SVMP EC 3.4.24.- ; Disintegrin contortrostatin |
| Gene Name | |
| Organism | Agkistrodon contortrix contortrix (Southern copperhead) |
| 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) Agkistrodon Agkistrodon contortrix (Copperhead) Agkistrodon contortrix contortrix (Southern copperhead) |
| Enzyme Sequence | MIQVLLVTLCLAAFPYQGSSIILESGNVNDYEVLYPQKVTALPKGAVQPKYEDTMQYEFKVNGEPVVLHLEKNKGLFSKDYSETHYSSDGRKITTNPPVEDHCYYHGRIQNDADSTASISACNGLKGHFKLQGETYLIEPLKLSDSEAHAVYKYENVEKEDEAPKMCGVTQTNWESDEPIKKASQLNLTPEQQGFPQRYIELVVVADHRMFTKYNGNLNTIRIWVHELVNTMNVFYRPLNIRVSLTDLEVWSDQDLINVQPAAADTLEAFGDWRETVLLNRISHDNAQLLTAIELDGETIGLANRGTMCDPKLSTGIVQDHSAINLWVAVTMAHEMGHNLGISHDGNQCHCDANSCIMSEELREQLSFEFSDCSQNQYQTYLTDHNPQCMLNEPLRTDIVSTPVSGNELLETGEESDFDAPANPCCDAATCKLTTGSQCADGLCCDQCKFMKEGTVCRRARGDDLDDYCNGISAGCPRNPFHA |
| Enzyme Length | 483 |
| Uniprot Accession Number | Q9IAB0 |
| Absorption | |
| Active Site | ACT_SITE 335; /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 metalloproteinase]: Impairs hemostasis in the envenomed animal (By similarity). This product has not been identified in the venom. {ECO:0000250, ECO:0000269|PubMed:10700384}.; FUNCTION: [Disintegrin contortrostatin]: Inhibits ADP-induced platelet aggregation. Binds and inhibits integrins GPIIb/GPIIIa (ITGA2B/ITGB3), alpha-5/beta-1 (ITGA5/ITGB1), alpha-V/beta-3 (ITGAV/ITGB3), and alpha-V/beta-5 (ITGAV/ITGB5). It blocks cancer cell adhesion to fibronectin and vitronectin and thus prevents invasion of cancer cells. {ECO:0000269|PubMed:10700384}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Disulfide bond (7); Domain (2); Metal binding (7); Motif (1); Propeptide (2); Signal peptide (1) |
| Keywords | Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Secreted;Signal;Toxin;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 461..463; /note=Cell attachment site |
| Gene Encoded By | |
| Mass | 53,948 |
| Kinetics | |
| Metal Binding | METAL 201; /note=Calcium; /evidence=ECO:0000250; METAL 285; /note=Calcium; /evidence=ECO:0000250; METAL 334; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 338; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 344; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 389; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 392; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |