Detail Information for IndEnz0002013472
IED ID IndEnz0002013472
Enzyme Type ID protease013472
Protein Name Kunitz-type serine protease inhibitor DrKIn-I
Daboia russelii Kunitz Inhibitor-I
Gene Name
Organism Daboia russelii (Russel's viper) (Vipera russelii)
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) Daboia Daboia russelii (Russel's viper) (Vipera russelii)
Enzyme Sequence MSSGGLLLLLGLLTLWAELTPISGQDRPKFCNLAPESGRCRGHLRRIYYNPDSNKCEVFFYGGCGGNDNNFETRKKCRQTCGAPRKGRPT
Enzyme Length 90
Uniprot Accession Number H6VC05
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Serine protease inhibitor. Inhibits activated protein C (APC) with an IC(50) of 3.5 nM in the presence of heparin (to which it strongly binds) and an IC(50) of 88.9 nM in its absence. Other targets are also significantly inhibited in presence of heparin: trypsin (PRSS1) (45%), coagulation FXIa (F11) (40%), and plasmin (PLG) (70%). In vivo, synergizes with RVV-X in promoting coagulation in mice and by extension in Russell's viper bite patients. {ECO:0000269|PubMed:22416129}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Disulfide bond (3); Domain (1); Modified residue (1); Region (2); Signal peptide (1); Site (1)
Keywords Blood coagulation cascade activating toxin;Disulfide bond;Hemostasis impairing toxin;Protease inhibitor;Pyrrolidone carboxylic acid;Secreted;Serine protease inhibitor;Signal;Toxin
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue MOD_RES 25; /note=Pyrrolidone carboxylic acid; /evidence=ECO:0000250
Post Translational Modification
Signal Peptide SIGNAL 1..24
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 10,010
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda