IED ID | IndEnz0002015951 |
Enzyme Type ID | protease015951 |
Protein Name |
Hemolin EC 3.4.21.- Lonomia obliqua Stuart factor activator Losac |
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 | MASKSLVVLSACIIIGSAVPVEKLPVLKSQPAEVLFRESQPTVLECIIEGQEEGVKYTWTKDGKDFKWTEHNAAQRTNEGSLVFLSPQPSDEGHYQCFAQTAAGVASSRVISFKRTYLVAEPAKTHEKTPVEGKPFQLDCVIPNAYPKPEIFWKKSLSGADPNADSANLGRRVTAGPDGNLYFTTVEKEDVSDIYKYVCVAKSPAHDGEVRLVEYIIKEVTKDTSGYKGELVPQYLSKDIVAKVGSVTMIYCMYGGKPQGFPDYFKDGKDVNGDAGGRITRHNRTSGKRLLIKETLLEDQGTYTCEESNGVGKPVKHSLKVTVVSAPKYVKSPEKVIIAKQGQDVTIPCQVTGLPAPKVTWTHNAQPLSGGKTTVTESGLIIKGLQKGDKGYYGCRSTNEHGDEYVETLVQVN |
Enzyme Length | 413 |
Uniprot Accession Number | Q1HLC0 |
Absorption | |
Active Site | |
Activity Regulation | ACTIVITY REGULATION: Increased activity in presence of phospholipids (low concentrations) and calcium ions. Inhibited by PMSF. Not affected by EDTA and E-64. {ECO:0000269|PubMed:21177860}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.21.- |
Enzyme Function | FUNCTION: Bristle toxin involved in caterpillar defense by participating in hemorrhagic syndrome characterized by a consumptive coagulopathy (PubMed:21177860). Exhibits procoagulant activity through selective factor X proteolytic activation (PubMed:21177860). Activates factor X in a dose- and time-dependent manner but does not activate gamma-carboxyglutamic acid domainless factor X (PubMed:21177860). Its activity does not depend on calcium ions (PubMed:21177860). Also functions as a growth stimulator and an inhibitor of cellular death for endothelial cells (PubMed:16597435). In vitro, increases proliferation of human umbilical vein endothelial cells (HUVEC) and inhibits the apoptosis induced by starvation (PubMed:16597435). Also increases slightly the complement decay-accelerating factor (CD55), which protects cells from complement-mediated lysis (PubMed:16597435). On the other hand, does not alter the release or expression of von Willebrand factor (VWF), tissue factor (F3), intercellular adhesion molecule-1 (ICAM1), interleukin-8 (CXCL8), and prostacyclin (PubMed:16597435). Does not show fibrinolytic or fibrinogenolytic activities (PubMed:21177860). {ECO:0000269|PubMed:16597435, ECO:0000269|PubMed:21177860}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Chain (1); Disulfide bond (4); Domain (4); Glycosylation (1); Signal peptide (1) |
Keywords | Blood coagulation cascade activating toxin;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Immunoglobulin domain;Protease;Repeat;Secreted;Serine protease;Signal;Toxin |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000269|PubMed:21177860 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 45,114 |
Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=188 nM for factor X in presence of phospholipids and calcium ions {ECO:0000269|PubMed:21177860}; |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |