| IED ID | IndEnz0002004559 |
| Enzyme Type ID | protease004559 |
| Protein Name |
Lopap EC 3.4.21.- Lipocalin-1/4 Prothrombin activator |
| Gene Name | |
| Organism | Lonomia obliqua (Moth) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Amphiesmenoptera Lepidoptera (butterflies and moths) Glossata Neolepidoptera Heteroneura Ditrysia Obtectomera Bombycoidea (hawk-moths) Saturniidae (emperor moths) Hemileucinae Lonomia Lonomia obliqua (Moth) |
| Enzyme Sequence | MKFFGLFLAILASTAADVVIDGACPDMKAVSKFDMNAYQGTWYEIKKFPVANEANGDCGSVEYTPDNGLLKVRAGHVEDDIEKFVVGVLTKNAGTSDAELTLSVVVGDYVRVAPLWIVSTDYDNYAIGYSCKDYKKSNQHRVNIWILSRTKTLNESSKSTVNKFLKEHSKEFDQSKFVETDFSEKACFFKKSHVYTVPFGA |
| Enzyme Length | 201 |
| Uniprot Accession Number | Q5ECE3 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Activated by calcium ions. Inhibited by EDTA, activity is recovered by the addition of calcium ions, but not magnesium or zinc ions. Inhibited by PMSF. {ECO:0000269|PubMed:11395128, ECO:0000269|PubMed:16734589}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.21.- |
| Enzyme Function | FUNCTION: Serine protease. Activates thrombin by cleavage of prothrombin. Does not activate factor X. When injected into rats, causes thrombus formation, fibrinogen depletion, uncoagulable blood, decreased platelet count, inhibition of collagen-induced platelet aggregation, leukocyte infiltration in lungs, congestion and hemorrhage in renal glomeruli and necrosis in renal distal tubules. Causes increase in surface expression of ICAM-1 and E-selectin on human umbilical vein endothelial cells (HUVEC), but does not affect expression of VCAM-1, or the expression of mediators involved in coagulation and fibrinolysis systems (TF, vWF and t-PA). Increases expression of the platelet activation inhibitors NO and PGI2. Increases viability of HUVEC, and inhibits apoptosis. {ECO:0000269|PubMed:11395128, ECO:0000269|PubMed:11395129, ECO:0000269|PubMed:11910193, ECO:0000269|PubMed:15963468, ECO:0000269|PubMed:16734589}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Disulfide bond (2); Glycosylation (1); Sequence conflict (9); Signal peptide (1) |
| Keywords | Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Prothrombin activator;Secreted;Serine protease;Signal;Toxin |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..16; /evidence="ECO:0000269|PubMed:11395128, ECO:0000269|PubMed:18342903" |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 22,432 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.5 uM for Abz-YQTFFNPRTGSQ-EDDnp {ECO:0000269|PubMed:11395128}; |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda | 3.4.21.60; |