IED Industry Enzyme Database

Detail Information for IndEnz0002015547
IED ID IndEnz0002015547
Enzyme Type ID protease015547
Protein Name Drosomycin
Cysteine-rich peptide
Gene Name Drs CRP CG10810
Organism Drosophila melanogaster (Fruit fly)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly)
Enzyme Sequence MMQIKYLFALFAVLMLVVLGANEADADCLSGRYKGPCAVWDNETCRRVCKEEGRSSGHCSPSLKCWCEGC
Enzyme Length 70
Uniprot Accession Number P41964
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Possesses antifungal activity and is active against a relatively broad spectrum of filamentous fungi (PubMed:8808632, PubMed:12872120). It inhibits spore germination at high concentrations and at low concentrations delays growth of hyphae which subsequently exhibit abnormal morphology (PubMed:7806546). Spz C-106 in the hemolymph controls expression of the antifungal peptide by acting as a ligand of Tl and inducing an intracellular signaling pathway (PubMed:8808632). Part of a psh-dependent Toll pathway, which may function in activating the systematic immune response in response to localized melanization of the tracheal system (PubMed:18854145). {ECO:0000269|PubMed:12872120, ECO:0000269|PubMed:18854145, ECO:0000269|PubMed:7806546, ECO:0000269|PubMed:8808632}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (2); Chain (1); Disulfide bond (4); Helix (1); Propeptide (1); Signal peptide (1); Turn (2)
Keywords 3D-structure;Antimicrobial;Direct protein sequencing;Disulfide bond;Fungicide;Reference proteome;Secreted;Signal
Interact With
Induction INDUCTION: Up-regulated by septic injury caused by the Gram-positive bacteria M.luteus and the fungus C.albicans, and by M.luteus or E.faecalis-derived peptidoglycans and by B.subtilis or A.oryzae proteases (PubMed:19590012). Up-regulated by Gram-negative bacteria in the respiratory epithelium (PubMed:22022271). Up-regulated in the trachea and fat body in response to tracheal melanization, either by spontaneous melanization or melanization resulting from infection by bacteria (E.coli and M.luteus) or the fungus B.bassiana (PubMed:18854145). {ECO:0000269|PubMed:18854145, ECO:0000269|PubMed:19590012, ECO:0000269|PubMed:22022271}.
Subcellular Location SUBCELLULAR LOCATION: Secreted.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..20; /evidence=ECO:0000255
Structure 3D NMR spectroscopy (1)
Cross Reference PDB 1MYN;
Mapped Pubmed ID 10197979; 10334979; 10369678; 10409696; 10489372; 10602463; 10619029; 10636911; 10696585; 10725405; 10793472; 10802234; 10827089; 10843389; 10898983; 10921908; 10963608; 10980426; 11017107; 11050330; 11083062; 11114385; 11118328; 11156609; 11164335; 11252795; 11269502; 11283698; 11413042; 11435447; 11486054; 11560896; 11562344; 11606746; 11606776; 11703941; 11707335; 11733057; 11739510; 11742098; 11742378; 11742401; 11743586; 11751574; 11756545; 11854512; 11869341; 11872802; 11881810; 11912488; 11912489; 11943764; 12032070; 12098703; 12101100; 12217523; 12324974; 12359879; 12381665; 12408809; 12431377; 12433364; 12446795; 12464428; 12502740; 12513692; 12514104; 12524523; 12530956; 12543974; 12556495; 12692550; 12728280; 12967563; 12973300; 14557290; 14585960; 14602069; 14602922; 14603309; 14644493; 14651939; 14654000; 14673153; 14684822; 14722090; 14731387; 14731391; 14749722; 14985331; 15032585; 15037551; 15100306; 15118082; 15136717; 15157233; 15197269; 15199954; 15199956; 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Motif
Gene Encoded By
Mass 7,752
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda