| IED ID | IndEnz0002008456 |
| Enzyme Type ID | protease008456 |
| Protein Name |
Spaetzle-processing enzyme EC 3.4.21.- Spatzle-processing enzyme Cleaved into: Spaetzle-processing enzyme light chain; Spaetzle-processing enzyme heavy chain |
| Gene Name | SPE c-SP4 SP4 CG16705 |
| 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 | MASTERNFLLLSLVVSALSGLVHRSDAAEISFGSCTPQQSDERGQCVHITSCPYLANLLMVEPKTPAQRILLSKSQCGLDNRVEGLVNRILVCCPQSMRGNIMDSEPTPSTRDALQQGDVLPGNDVCGFLFADRIFGGTNTTLWEFPWMVLLQYKKLFSETYTFNCGGALLNSRYVLTAGHCLASRELDKSGAVLHSVRLGEWDTRTDPDCTTQMNGQRICAPKHIDIEVEKGIIHEMYAPNSVDQRNDIALVRLKRIVSYTDYVRPICLPTDGLVQNNFVDYGMDVAGWGLTENMQPSAIKLKITVNVWNLTSCQEKYSSFKVKLDDSQMCAGGQLGVDTCGGDSGGPLMVPISTGGRDVFYIAGVTSYGTKPCGLKGWPGVYTRTGAFIDWIKQKLEP |
| Enzyme Length | 400 |
| Uniprot Accession Number | Q9VCJ8 |
| Absorption | |
| Active Site | ACT_SITE 181; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 249; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU00274; ACT_SITE 346; /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: Endopeptidase which plays a key role in innate immunity by cleaving Tl ligand spz and thereby activating the Toll pathway in response to fungal and Gram-positive bacterial infections (PubMed:16631589, PubMed:16399077, PubMed:18724373, PubMed:26843333, PubMed:16996061). Acts downstream of pathogen recognition receptors PGRP-SA and GNBP1 and protease grass in response to Gram-positive bacterial infection (PubMed:16399077). Acts downstream of protease psh in response to fungal infection (PubMed:16399077). {ECO:0000269|PubMed:16399077, ECO:0000269|PubMed:16631589, ECO:0000269|PubMed:16996061, ECO:0000269|PubMed:18724373, ECO:0000269|PubMed:26843333}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (2); Disulfide bond (8); Domain (2); Glycosylation (2); Metal binding (4); Mutagenesis (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Disulfide bond;Glycoprotein;Hydrolase;Immunity;Innate immunity;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen |
| Interact With | |
| Induction | INDUCTION: Up-regulated in response to fungal and Gram-positive bacterial infections. {ECO:0000269|PubMed:16399077, ECO:0000269|PubMed:16996061}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Note=Probably secreted in the hemolymph. {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved in response to Gram-negative bacterial or fungal infection; processing is likely to result in its activation (PubMed:16399077). Cleavage produces a light chain containing the CLIP domain and a catalytic heavy chain which remain covalently associated through an interchain disulfide bond (Probable). {ECO:0000269|PubMed:16399077, ECO:0000305|PubMed:16399077}. |
| Signal Peptide | SIGNAL 1..27; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11606746; 11742098; 12032070; 12364793; 12417656; 12431377; 12568721; 15556270; 15579698; 16277749; 17227774; 17588928; 17660749; 17996400; 18334252; 19218090; 19520911; 19546158; 19590012; 19740772; 19851448; 20220848; 20371351; 21074052; 21078848; 21203476; 21209287; 21264297; 21576362; 22227521; 22368770; 22590528; 22724070; 22912810; 23071443; 23519314; 23796791; 23868318; 23944235; 24002645; 24343480; 24443439; 24705267; 24981286; 25312911; 25421701; 25525791; 25530181; 25628309; 25687947; 25901322; 26241320; 26453810; 26494844; 26526100; 26551273; 27172210; 27894253; 29091025; 29198775; 29211760; 29268741; 29695493; 29707694; 30146479; 30367934; 30478194; 30684503; 31018123; 31562189; 31564469; 31722958; 32509789; 32656090; 32774336; 32866212; 32901612; 33561221; 33827210; |
| Motif | |
| Gene Encoded By | |
| Mass | 43,947 |
| Kinetics | |
| Metal Binding | METAL 202; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O97366; METAL 204; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O97366; METAL 207; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:O97366; METAL 210; /note=Calcium; /evidence=ECO:0000250|UniProtKB:O97366 |
| Rhea ID | |
| Cross Reference Brenda |