| IED ID | IndEnz0002012550 |
| Enzyme Type ID | protease012550 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like HR1b EC 3.4.24.- Snake venom metalloproteinase SVMP Trimerelysin I Trimerelysin-1 Cleaved into: Disintegrin-like 1b |
| Gene Name | |
| Organism | Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis) |
| 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 flavoviridis (Habu) (Trimeresurus flavoviridis) |
| Enzyme Sequence | MIQVLLVTICLAVFPYQGSSIILESGNVNDYEVMYPQKVAALPKGAVQQKYEDTMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTNPPVEDHCYYHGRIQNDADSTASISACNGLKGHFKLQGEMYLIEPLKFSDSEAHAVYKYENVEKEEEAPKMCGVTQTNWESDEPIKKASKLVVTAEQQRFPRRYIKLAIVVDHGIVTKHHGNLKKIRKWIYQLVNTINNIYRSLNILVALVYLEIWSKQNKITVQSASNVTLDLFGDWRESVLLKQRSHDCAQLLTTIDFDGPTIGKAYTASMCDPKRSVGIVQDYSPINLVVAVIMTHEMGHNLGIPHDGNSCTCGGFPCIMSPMISDPPSELFSNCSKAYYQTFLTDHKPQCILNAPSKTDIVSPPVCGNELLEAGEECDCGSPENCQYQCCDAASCKLHSWVKCESGECCDQCRFRTAGTECRAAESECDIPESCTGQSADCPTDRFHRNGQPCLYNHGYCYNGKCPIMFYQCYFLFGSNATVAEDDCFNNNKKGDKYFYCRKENEKYIPCAQEDVKCGRLFCDNKKYPCHYNYSEDLDFGMVDHGTKCADGKVCSNRQCVDVNEAYKSTTVFSLI |
| Enzyme Length | 614 |
| Uniprot Accession Number | P20164 |
| 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: [Zinc metalloproteinase-disintegrin-like HR1b]: Zinc protease that induces hemorrhage. Has preference for Tyr, Leu, Arg, Met, and Phe at the P1 position, in descending order (in vitro). Shows equal preference for the sequences of Ala-Asp and Arg-Ile at the P3-P2 position with different enzyme cleavage sites across the P1 position: the N-terminus side for Ala-Asp and the C-terminus side for Arg-Ile. {ECO:0000269|PubMed:18256489}.; FUNCTION: [Disintegrin-like 1b]: Inhibits platelet aggregation induced by ADP, thrombin, platelet-activating factor and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors alpha-IIb/beta-3 (ITGA2B/ITGB3). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Disulfide bond (25); Domain (2); Glycosylation (4); Metal binding (9); Modified residue (1); Motif (1); Natural variant (2); Propeptide (3); Signal peptide (1) |
| Keywords | Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;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. |
| Modified Residue | MOD_RES 192; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:2398046 |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 466..468; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 69,129 |
| Kinetics | |
| Metal Binding | 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 404; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 407; /note=Calcium; /evidence=ECO:0000250; METAL 409; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 411; /note=Calcium; /evidence=ECO:0000250; METAL 414; /note=Calcium; /evidence=ECO:0000250; METAL 417; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |