| IED ID | IndEnz0002012084 |
| Enzyme Type ID | protease012084 |
| Protein Name |
Snake venom metalloproteinase kistomin SVMP EC 3.4.24.- |
| 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 | MIEVLLVTICLAAFPYQGSSIILESGNVNDYEVVYPRKITALSEGAAQQKYEDTMQYEFKVNGEPVVLHLEKNKELFAKDYSETHYSPDGTRITTYPSVEDHCYYQGRIHNDADSTASISTCNGLKGHFKFHGERYFIEPLKLPGSEAHAVYKYENIEKEDETPKMCGVIQKWKSDELIKKPFRLNLTPQQQESPQAKVYLVIVADKSMVDKHNGNIKKIEEQGHQMVNTMNECYRPMGIIIIMAGIECWTTNDFFEVKSSAKETLYSFAKWRVEDLSKRKPHNDAQFLTNKDFDGNTVGLAFVGGICNEKYCAGVVQDHTKVPLLMAITMGHEIGHNLGMEHDEANCKCKACVMAPEVNNNPTKKFSDCSRNYYQKFLKDRKPECLFKKPLRTDTVSTPVSGNEPLEVITMDDFYA |
| Enzyme Length | 417 |
| Uniprot Accession Number | P0CB14 |
| Absorption | |
| Active Site | ACT_SITE 334; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA, and O-phenanthrolene. {ECO:0000269|PubMed:1477097, ECO:0000269|PubMed:17609416}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Snake venom zinc metalloprotease that inhibits platelet aggregation by binding specifically to platelet glycoprotein VI (GP6) and platelet glycoprotein Ib alpha (GP1BA). It inhibits the interaction between collagen and platelet GP6 by cleaving GP6 (at '225-Glu-|-Ala-226' and '238-Val-|-Phe-239' bonds), and inhibits vWF-induced platelet aggregation by cleaving GP1BA and vWF. Cleavage of GP1BA occurs at two distinct sites to generate two soluble fragments. It also cleaves alpha- (FGA) and subsequently the gamma-chain (FGG) of fibrinogen, leaving the beta-chain unaffected. It also inhibits collagen-, convulxin- and ristocetin-induced platelet aggregation. It blocks the adhesion of platelet to immobilized collagen, but only exerts a slight inhibition to fibrinogen. In vivo, it exerts potent antithrombotic effect. {ECO:0000269|PubMed:1477097, ECO:0000269|PubMed:17609416, ECO:0000269|PubMed:18624975, ECO:0000269|PubMed:8251530}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Disulfide bond (3); Domain (1); Metal binding (3); Propeptide (2); Signal peptide (1) |
| Keywords | 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 | |
| Gene Encoded By | |
| Mass | 47,446 |
| Kinetics | |
| Metal Binding | METAL 333; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 337; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 343; /note=Zinc; catalytic; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |