| IED ID | IndEnz0002012475 |
| Enzyme Type ID | protease012475 |
| Protein Name |
Zinc metalloproteinase-disintegrin-like VAP2B EC 3.4.24.- Catrocollastatin Snake venom metalloproteinase SVMP Vascular apoptosis-inducing protein 2B VAP2B Cleaved into: Disintegrin-like catrocollastatin-C |
| Gene Name | |
| Organism | Crotalus atrox (Western diamondback rattlesnake) |
| 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) Crotalus Crotalus atrox (Western diamondback rattlesnake) |
| Enzyme Sequence | MIQVLLVTICLAAFPYQGSSIILESGNVNDYEVIYPRKVTALPKGAVQPKYEDAMQYELKVNGEPVVLHLGKNKGLFSKDYSETHYSPDGREITTYPLVEDHCYYHGRIENDADSTASISACNGLKGHFKLQGEMYLIEPLKLPDSEAHAVYKYENVEKEDEALKMCGVTQNWESYEPIKKASQLVVTAEHQKYNPFRFVELFLVVDKAMVTKNNGDLDKIKTRMYEIVNTVNEIYRYMYIHVALVGLEIWSNEDKITVKPEAGYTLNAFGEWRKTDLLTRKKHDNAQLLTAIDLDRVIGLAYVGSMCHPKRSTGIIQDYSEINLVVAVIMAHEMGHNLGINHDSGYCSCGDYACIMRPEISPEPSTFFSNCSYFECWDFIMNHNPECILNEPLGTDIISPPVCGNELLEVGEECDCGTPENCQNECCDAATCKLKSGSQCGHGDCCEQCKFSKSGTECRASMSECDPAEHCTGQSSECPADVFHKNGQPCLDNYGYCYNGNCPIMYHQCYDLFGADVYEAEDSCFERNQKGNYYGYCRKENGNKIPCAPEDVKCGRLYCKDNSPGQNNPCKMFYSNEDEHKGMVLPGTKCADGKVCSNGHCVDVATAY |
| Enzyme Length | 609 |
| Uniprot Accession Number | Q90282 |
| Absorption | |
| Active Site | ACT_SITE 334; /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 VAP2B]: Zinc metalloprotease that abolishes platelet aggregation induced by collagen, but has no effect on platelet aggregation induced by ADP or thromboxane analog. This inhibition may be due to its ability to bind collagen and block the binding site on collagen for platelets and/or to its ability to bind to the platelet alpha-2/beta-1 collagen receptor (ITGA2/ITGB1) to block its interaction with collagen and hence prevent platelet stimulation.; FUNCTION: Disintegrin catrocollastatin-C: abolishes platelet aggregation induced by collagen (IC(50)=66 nM) but not ADP-stimulated platelet aggregation. This inhibition may be due to its ability to bind collagen and block the binding site on collagen for platelets and/or to its ability to bind to the platelet alpha-2/beta-1 collagen receptor (ITGA2/ITGB1) to block its interaction with collagen and hence prevent platelet stimulation. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (21); Chain (2); Disulfide bond (25); Domain (2); Glycosylation (1); Helix (13); Metal binding (18); Modified residue (1); Motif (1); Propeptide (1); Region (1); Sequence conflict (12); Signal peptide (1); Turn (7) |
| Keywords | 3D-structure;Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;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:9210644}. |
| Modified Residue | MOD_RES 190; /note=Pyrrolidone carboxylic acid (Glu); /evidence=ECO:0000250|UniProtKB:O93523 |
| Post Translational Modification | PTM: The N-terminus is blocked. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 2DW0; 2DW1; 2DW2; |
| Mapped Pubmed ID | 16688218; 9578458; |
| Motif | MOTIF 465..467; /note=D/ECD-tripeptide |
| Gene Encoded By | |
| Mass | 68,248 |
| Kinetics | |
| Metal Binding | METAL 201; /note=Calcium 1; METAL 285; /note=Calcium 1; METAL 333; /note=Zinc; catalytic; METAL 337; /note=Zinc; catalytic; METAL 343; /note=Zinc; catalytic; METAL 388; /note=Calcium 1; via carbonyl oxygen; METAL 391; /note=Calcium 1; METAL 403; /note=Calcium 2; via carbonyl oxygen; METAL 406; /note=Calcium 2; METAL 408; /note=Calcium 2; via carbonyl oxygen; METAL 410; /note=Calcium 2; METAL 413; /note=Calcium 2; METAL 416; /note=Calcium 2; METAL 467; /note=Calcium 3; METAL 468; /note=Calcium 3; via carbonyl oxygen; METAL 470; /note=Calcium 3; METAL 482; /note=Calcium 3; METAL 483; /note=Calcium 3; via carbonyl oxygen |
| Rhea ID | |
| Cross Reference Brenda |