Detail Information for IndEnz0002002987
IED ID IndEnz0002002987
Enzyme Type ID protease002987
Protein Name Modular serine protease
EC 3.4.21.-

Cleaved into: Modular serine protease non-catalytic chain; Modular serine protease catalytic chain
Gene Name modSP Ldlr CG31217
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 MQLISFLSNPLFFCALLLKFRTIFAACDSSQFECDNGSCISQYDVCNGEKNCPDGSDETALTCVSQRQHCTKPYFQCTYGACVIGTAGCNGVNECADGSDETRLRCGNEDDIRQHDRRLQGNCKENEFKCPSGICLDKSNFLCDGKDDCADGTGFDESVELCGHMECPAYSFKCGTGGCISGSLSCNGENDCYDGSDEAPLLCNTTKKVTTPVVTETPLELLGCPLPLGDERPILTGDGSRVLTGPITRGTVRFSCKQGYVLEGEESSYCAKNKWSTSTIPKCVKYCSTAGEFDGYSTKALCTHNGQQVECRKPFHPPGTEVKFVCSTGFKTLSPLPEMRCMKGGYWNRGRQRCEQDCGQLATPIKQFSSGGYTINNTVVPWHVGLYVWHNEKDYHFQCGGSLLTPDLVITAAHCVYDEGTRLPYSYDTFRVIAAKFYRNYGETTPEEKRRDVRLIEIAPGYKGRTENYYQDLALLTLDEPFELSHVIRPICVTFASFAEKESVTDDVQGKFAGWNIENKHELQFVPAVSKSNSVCRRNLRDIQADKFCIFTQGKSLACQGDSGGGFTSELPTNAFSTWNTARHFLFGVISNAPNADQCAHSLTVMTNIQHFEDMILNAMNRSVETRS
Enzyme Length 628
Uniprot Accession Number Q9VER6
Absorption
Active Site ACT_SITE 414; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 472; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 563; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.21.-
Enzyme Function FUNCTION: Serine protease that plays a key role in innate immunity by activating the Toll pathway in response to infection with Gram-positive bacteria and fungi (PubMed:19590012, PubMed:24794300). During Gram-positive infection, acts downstream of PGRP-SA and upstream of Grass and Spz, and therefore appears to function in a pathway that links detection of Gram-positive lysine-type peptidoglycans to Toll activation (PubMed:19590012). Functions in a separate pathway to the psh-mediated activation of the Toll pathway (PubMed:19590012). {ECO:0000269|PubMed:19590012, ECO:0000269|PubMed:24794300}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (2); Disulfide bond (17); Domain (7); Glycosylation (4); Signal peptide (1); Site (1)
Keywords Autocatalytic cleavage;Disulfide bond;Glycoprotein;Hydrolase;Immunity;Innate immunity;Protease;Reference proteome;Repeat;Secreted;Serine protease;Signal;Sushi;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19590012}. Note=Localizes at the membrane of lipid vesicles. Secreted from the fat body into the hemolymph at the surface of these lipid vesicles. {ECO:0000269|PubMed:19590012}.
Modified Residue
Post Translational Modification PTM: May be proteolytically cleaved via an autocatalytic mechanism. {ECO:0000269|PubMed:19590012}.
Signal Peptide SIGNAL 1..25; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11172718; 11733057; 12568721; 12906807; 14605208; 17188778; 17409189; 17987029; 17996400; 19914231; 20089584; 20220848; 21074052; 21209287; 21576362; 22724070; 23071443; 23519314; 23632253; 23868318; 23944235; 25082344; 25294943; 25312911; 25421701; 25901322; 26843333; 27172210; 27678375; 27815361; 28250052; 28874153; 29091025; 29707694; 30131599; 30146479; 30367934; 31018123; 31430488; 31564469; 32063902; 32188787; 32656090; 32866212; 33827210; 33914801; 33946849; 7667301; 9060438;
Motif
Gene Encoded By
Mass 69,433
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda