Detail Information for IndEnz0002015951
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