| IED ID | IndEnz0002012282 |
| Enzyme Type ID | protease012282 |
| Protein Name |
Zinc metalloproteinase-disintegrin bilitoxin-1 EC 3.4.24.- Snake venom metalloproteinase SVMP Cleaved into: Disintegrin |
| Gene Name | |
| Organism | Agkistrodon bilineatus (Cantil) (Tropical moccasin) |
| 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) Agkistrodon Agkistrodon bilineatus (Cantil) (Tropical moccasin) |
| Enzyme Sequence | QRYNPYKYIELFLVVDNRMVTKYNGDLDKIKTRIYELVNILNEIYRPLYIRVALVGIEFWCNKDLINVKSASSVTLASFANWRESVLPNRTSHDNAQLLTAIVFNRGVIGSAYPAGMCDPNRSVGTVQDHSEINLQVAITMAHEIGHNLGMGHDNNSCTCGGYSCIMLPALSDQPSKYFSNCSYIQYRDFIMNQDPQCILNEPSGTDIVSPPVCGNDILEVGEECDCGCPRNCQDPCCNAATCKKYSWVQCESGECCDQCRFKGAGTECRRAMGDDPGGRCTGQSADCPRN |
| Enzyme Length | 291 |
| Uniprot Accession Number | P0C6E3 |
| Absorption | |
| Active Site | ACT_SITE 144; /evidence="ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by EDTA and EGTA, but not by cysteine or soybean trypsin inhibitor (SBTI). {ECO:0000269|PubMed:2676645}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: This hemorrhagic toxin hydrolyzes the Aalpha-chain (FGA) and more slowly the Bbeta-chain (FGB) of fibrin and fibrinogen. Also hydrolyzes casein. It lacks platelet aggregation inhibitory activity. After intramuscular injection, it acts rapidly to disrupt the capillary endothelium without damaging the intercellular junctions, and also appears to damage skeletal muscle cells. Cleaves insulin B chain at '27-Asn-|-Gln-28', '34-His-|-Leu-35', '38-Ala-|-Leu-39', '40-Tyr-|-Leu-41', '46-Arg-|-Gly-47' and '48-Phe-|-Phe-49' bonds (PubMed:2676645). {ECO:0000269|PubMed:2219144, ECO:0000269|PubMed:2676645}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Disulfide bond (12); Domain (2); Glycosylation (3); Metal binding (12); Modified residue (1); Motif (1) |
| Keywords | Calcium;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Fibrinolytic toxin;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Myotoxin;Protease;Pyrrolidone carboxylic acid;Secreted;Sialic acid;Toxin;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | MOD_RES 1; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000269|PubMed:10871038 |
| Post Translational Modification | PTM: Glycosylated; glycans contain fucose, galactosamine, glucosamine, galactose, and mannose. Sialylated; 75% of the hemorrhagic activity of native bilitoxin-1 is lost upon removal of the sialic acid moieties of bilitoxin-1. {ECO:0000269|PubMed:10871038}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | MOTIF 273..275; /note=Cell attachment site; atypical (MGD) |
| Gene Encoded By | |
| Mass | 32,314 |
| Kinetics | |
| Metal Binding | METAL 10; /note=Calcium 1; /evidence=ECO:0000250; METAL 94; /note=Calcium 1; /evidence=ECO:0000250; METAL 143; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 147; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 153; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 198; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250; METAL 201; /note=Calcium 1; /evidence=ECO:0000250; METAL 213; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250; METAL 216; /note=Calcium 2; /evidence=ECO:0000250; METAL 220; /note=Calcium 2; /evidence=ECO:0000250; METAL 223; /note=Calcium 2; /evidence=ECO:0000250; METAL 226; /note=Calcium 2; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |