| IED ID | IndEnz0002012548 |
| Enzyme Type ID | protease012548 |
| Protein Name |
Zinc metalloproteinase/disintegrin Cleaved into: Snake venom metalloproteinase rhodostoxin SVMP EC 3.4.24.- Hemorrhagic protein ; Disintegrin rhodostomin RHO RHOD Disintegrin kistrin Platelet aggregation activation inhibitor |
| Gene Name | |
| Organism | Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma) |
| 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) Calloselasma Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma) |
| Enzyme Sequence | MIQVLLVTICLAAFPYQGSSIILESGNVNDYEVVYPRKVIALSEGAAQQKYEDTMQYEFKVNGEPVVLHLEKNKGLFAKDYSETHYSPDGTRITTYPSVEDHCYYQGRIHNDADSTASISACNGLKGHFKLQGETYFIEPMKLPDSEAHAVFKYENIEKEDESPKMCGVTETNWESDEPIKKVSQLNLNHEIKRHVDIVVVVDSRFCTKHSNDLEVIRKFVHEVVNAIIESYKYMHFGISLVNLETWCNGDLINVQEDSYETLKAFGKWRESDLIKHVNHSNAQFLMDMKFIKNIIGKAYLDSICDPERSVGIVQNYHGITLNVAAIMAHEMGHNLGVRHDGEYCTCYGSSECIMSSHISDPPSKYFSNCSYYQFWKYIENQNPQCILNKPLRTVSIPVSGNEHLEAGKECDCSSPENPCCDAATCKLRPGAQCGEGLCCEQCKFSRAGKICRIPRGDMPDDRCTGQSADCPRYHSHA |
| Enzyme Length | 478 |
| Uniprot Accession Number | P30403 |
| Absorption | |
| Active Site | ACT_SITE 331; /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 rhodostoxin]: Impairs hemostasis in the envenomed animal. {ECO:0000250}.; FUNCTION: [Disintegrin rhodostomin]: 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). |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (9); Chain (2); Disulfide bond (10); Domain (2); Glycosylation (2); Helix (1); Metal binding (3); Motif (1); Propeptide (3); Sequence conflict (1); Signal peptide (1); Turn (1) |
| Keywords | 3D-structure;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;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 | PTM: Glycans are composed of 4 GlcNAc, 3 Man, 2 Gal, 2 NeuAC and 1 Fuc residue. |
| Signal Peptide | SIGNAL 1..20; /evidence=ECO:0000255 |
| Structure 3D | NMR spectroscopy (10); X-ray crystallography (5) |
| Cross Reference PDB | 1N4Y; 1Q7I; 1Q7J; 2LJV; 2M75; 2M7F; 2M7H; 2PJF; 2PJG; 2PJI; 3UCI; 4M4C; 4R5R; 4R5U; 4RQG; |
| Mapped Pubmed ID | 19280603; |
| Motif | MOTIF 456..458; /note=Cell attachment site |
| Gene Encoded By | |
| Mass | 54,006 |
| Kinetics | |
| Metal Binding | METAL 330; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 334; /note=Zinc; catalytic; /evidence=ECO:0000305; METAL 340; /note=Zinc; catalytic; /evidence=ECO:0000305 |
| Rhea ID | |
| Cross Reference Brenda |