Detail Information for IndEnz0002012542
IED ID IndEnz0002012542
Enzyme Type ID protease012542
Protein Name Thrombin-like enzyme cerastotin
SVTLE
EC 3.4.21.-
Fibrinogen-clotting enzyme
Snake venom serine protease
SVSP
Fragments
Gene Name
Organism Cerastes cerastes (Horned desert viper)
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 Viperinae (vipers) Cerastes Cerastes cerastes (Horned desert viper)
Enzyme Sequence VIGGAECNINEHRSLVLLYYSSRLFGGGTLINKEWVLSAAHCDGENMKIIYXXXXXXXXXXKDRQIRVAKKYFCRDRKKSVIDKDIMLIKKPVNGSTH
Enzyme Length 98
Uniprot Accession Number P81038
Absorption
Active Site ACT_SITE 41; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 85; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation ACTIVITY REGULATION: Inhibited by PMSF. {ECO:0000269|PubMed:9249017}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.21.-
Enzyme Function FUNCTION: Thrombin-like snake venom serine protease that preferentially cleaves the alpha-chain of fibrinogen (FGA). Induce platelet aggregation in the presence of exogenous fibrinogen. Possesses esterase and amidolytic activities. {ECO:0000269|PubMed:9249017}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Domain (1); Glycosylation (1); Non-terminal residue (1)
Keywords Blood coagulation cascade activating toxin;Direct protein sequencing;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Platelet aggregation activating toxin;Protease;Secreted;Serine protease;Toxin
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 11,168
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda