| IED ID | IndEnz0002012969 |
| Enzyme Type ID | protease012969 |
| Protein Name |
Zinc metalloproteinase/disintegrin Cleaved into: Snake venom metalloproteinase TM-3 SVMP EC 3.4.24.- Atrolysin e Fibrinlysin Trimutase ; Disintegrin trimucrin |
| Gene Name | |
| Organism | Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus) |
| 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) Protobothrops Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus) |
| Enzyme Sequence | MIEVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPRKVSALPKGAVQPKYEDAMQYEFKVNGEAVVLHLEKNKGLFSEDYSETHYSPDGREITTYPSVEDHCYYHGRIHNDADSTASISACDGLKGYFKLQGETYPIEPLELSDSEAHAVFKYENVEKEDEAPKMCGVTQNWESDESIKKASQLYLTPEQQRFPQRYIKLAIVVDHGMYTKYSSNFKKIRKRVHQMVSNINEMCRPLNIAITLALLDVWSEKDFITVQADAPTTAGLFGDWRERVLLKKKNHDHAQLLTDTNFARNTIGWAYVGRMCDEKYSVAVVKDHSSKVFMVAVTMTHELGHNLGMEHDDKDKCKCDTCIMSAVISDKQSKLFSDCSKDYYQTFLTNDNPQCILNAPLRTDTVSTPVSGNEFLEAGEECDCGSPENPCCDAATCKLRPGAQCAEGLCCDQCRFKKKRTICRRARGDNPDDRCTGQSADCPRNGLYG |
| Enzyme Length | 481 |
| Uniprot Accession Number | O57413 |
| Absorption | |
| Active Site | ACT_SITE 334; /evidence=ECO:0000255|PROSITE-ProRule:PRU00276 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA and 1,10-phenanthroline (PubMed:8193588). Is also inhibited by endogenous tripeptide inhibitors pyroGlu-Asn-Trp, pyroGlu-Gln-Trp, and pyroGlu-Lys-Trp (PubMed:9703966, PubMed:12071970). {ECO:0000269|PubMed:12071970, ECO:0000269|PubMed:8193588, ECO:0000269|PubMed:9703966}. |
| Binding Site | BINDING 357; /note="Tripeptide; endogneous tripeptide inhibitor"; /evidence="ECO:0000269|PubMed:12071970, ECO:0007744|PDB:1KUG, ECO:0007744|PDB:1KUK" |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: [Snake venom metalloproteinase TM-3]: Potent fibrinogenolytic protease which cleaves mainly the Aalpha chain of fibrinogen (FGA) and slightly the Bbeta (FGB) and the gamma (FGG) chains (PubMed:8193588, PubMed:7488093). May possess hemorrhagic activity (PubMed:7488093). Compared to other SVMP, the substrate-binding pocket is relatively shallow (PubMed:12077431). Is less susceptible to tripeptide inhibitors than TM-1 (AC U3KRG1) and TM-2 (PubMed:9703966). {ECO:0000269|PubMed:12077431, ECO:0000269|PubMed:7488093, ECO:0000269|PubMed:8193588, ECO:0000269|PubMed:9703966}.; FUNCTION: [Disintegrin trimucrin]: Inhibits platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3). {ECO:0000250|UniProtKB:P17349}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (6); Binding site (1); Chain (2); Disulfide bond (9); Domain (2); Erroneous initiation (1); Helix (9); Metal binding (3); Modified residue (1); Motif (1); Propeptide (2); Region (1); Sequence conflict (17); Signal peptide (1); Turn (3) |
| Keywords | 3D-structure;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Hemorrhagic 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 {ECO:0000269|PubMed:7488093, ECO:0000269|PubMed:8193588}. |
| Modified Residue | MOD_RES 190; /note="Pyrrolidone carboxylic acid (Glu)"; /evidence="ECO:0000305|PubMed:7488093, ECO:0000305|PubMed:8193588" |
| Post Translational Modification | PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7488093}. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (4) |
| Cross Reference PDB | 1KUF; 1KUG; 1KUI; 1KUK; |
| Mapped Pubmed ID | - |
| Motif | MOTIF 459..461; /note=Cell attachment site |
| Gene Encoded By | |
| Mass | 54,178 |
| Kinetics | |
| Metal Binding | METAL 333; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:12071970, ECO:0000269|PubMed:12077431, ECO:0007744|PDB:1KUF, ECO:0007744|PDB:1KUG, ECO:0007744|PDB:1KUI, ECO:0007744|PDB:1KUK"; METAL 337; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:12071970, ECO:0000269|PubMed:12077431, ECO:0007744|PDB:1KUF, ECO:0007744|PDB:1KUG, ECO:0007744|PDB:1KUI, ECO:0007744|PDB:1KUK"; METAL 343; /note="Zinc; catalytic"; /evidence="ECO:0000269|PubMed:12071970, ECO:0000269|PubMed:12077431, ECO:0007744|PDB:1KUF, ECO:0007744|PDB:1KUG, ECO:0007744|PDB:1KUI, ECO:0007744|PDB:1KUK" |
| Rhea ID | |
| Cross Reference Brenda |