Detail Information for IndEnz0002010299
IED ID IndEnz0002010299
Enzyme Type ID protease010299
Protein Name Zinc metalloproteinase carinactivase-1 catalytic subunit
CA-1 catalytic subunit
EC 3.4.24.-
Carinactivase-1 62 kDa subunit
Snake venom metalloproteinase
SVMP
Fragment
Gene Name
Organism Echis carinatus (Saw-scaled 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) Echis Echis carinatus (Saw-scaled viper)
Enzyme Sequence SRKQKFDKKFIKLVIVVDHSMVXKXNNDLIAI
Enzyme Length 32
Uniprot Accession Number Q9PRP9
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Calcium-dependent prothrombin (F2) activator. This protein may activate prothrombin via recognition by the regulatory subunit of the calcium ion bound conformation of its gamma-carboxyglutamic acid (GLA) domain, and the subsequent conversion of prothrombin to active thrombin is catalyzed by the catalytic subunit. {ECO:0000269|PubMed:8617803}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Domain (1); Non-terminal residue (1)
Keywords Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Prothrombin activator;Secreted;Toxin;Zinc
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 3,751
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda 3.4.24.49;