Detail Information for IndEnz0002011371
IED ID IndEnz0002011371
Enzyme Type ID protease011371
Protein Name Thrombin-like enzyme gyroxin B1.3
SVTLE gyroxin B1.3
EC 3.4.21.-
Fibrinogen-clotting enzyme
Snake venom serine protease
SVSP
Gene Name
Organism Crotalus durissus terrificus (South American 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 durissus (tropical rattlesnake) Crotalus durissus terrificus (South American rattlesnake)
Enzyme Sequence MVLIRVLANLLILQLSYAQKSSELVIGGDECNINEHNFLVALYEYWSQSFLCGGTLINGEWVLTAAHCDRKHILIYVGVHDRSVQFDKEQRRFPKEKYFFNCRNNFTKWDKDIMLIRLNKPVSYSEHIAPLSLPSSPPIVGSVCRVMGWGTIKSPQETLPDVPHCANINLLDYEVCRTAHPQFRLPATSRILCAGVLEGGIDTCHRDSGGPLICNGEFQGIVSWGDGPCAQPDKPALYSKVFDHLDWIQNIIAGSETVNCPS
Enzyme Length 262
Uniprot Accession Number B0FXM1
Absorption
Active Site ACT_SITE 67; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 112; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 208; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.21.-
Enzyme Function FUNCTION: Thrombin-like snake venom serine protease. Displays a specificity similar to trypsin. Releases only fibrinopeptide A in the conversion of fibrinogen to fibrin. Reversibly increases the permeability of the blood brain barrier (BBB) in mice (PubMed:11137545, PubMed:20637222). Induces the barrel rotation syndrome in mice, which is manifested by gyroxin-like, rapid rolling motions (PubMed:11137545, PubMed:20637222). This syndrome may be due to its effect on BBB permeability, and certainly also to other actions affecting endogenous substrates present in the endothelium, nervous tissues or blood (PubMed:11137545, PubMed:20637222). Also shows a moderate inhibitory activity on the human voltage-gated potassium channel Kv10.1/KCNH1/EAG1 (58% current inhibition at 5 uM) (PubMed:32161292). It blocks Kv10.1/KCNH1/EAG1 in a time and dose-dependent manner and with a mechanism independent of its enzymatic activity (By similarity). It may have a preference in interacting with Kv10.1/KCNH1/EAG1 in its closed state, since the inhibitory effect of the toxin is decreased at more depolarized potentials (By similarity). {ECO:0000250|UniProtKB:A0A0S4FKT4, ECO:0000269|PubMed:11137545, ECO:0000269|PubMed:20637222, ECO:0000269|PubMed:32161292}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Disulfide bond (6); Domain (1); Glycosylation (1); Propeptide (1); Signal peptide (1)
Keywords Blood coagulation cascade activating toxin;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Ion channel impairing toxin;Potassium channel impairing toxin;Protease;Secreted;Serine protease;Signal;Toxin;Voltage-gated potassium channel impairing toxin
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 29,347
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda