| IED ID | IndEnz0002001340 |
| Enzyme Type ID | protease001340 |
| Protein Name |
Serine protease inhibitor 27A Serpin 27A |
| Gene Name | Spn27A CG11331 |
| 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 | MTKMGGNLAVMLLSLFLSALATGNGNSIPTTTTPQGVFETRTDKLPGGAASVPSGAGIYDDIDTFVPFRSDSHDPFSWHLLKTVLQNETADKNVIISPFSVKLVLALLAEAAGAGTQTQVELANTQTDIRSQNNVREFYRKTLNSFKKENQLHETLSVRTKLFTDSFIETQQKFTATLKHFYDSEVEALDFTNPEAAADAINAWAANITQGRLQQLVAPDNVRSSVMLLTNLIYFNGLWRRQFATTFQGSFFRSKDDQSRAEFMEQTDYFYYTTSEKLKAQILRLPYKGKNSLFVLLPYALNGIHDLVKNLENDELKSAQWAMEEVKVKVTLPKFHFDYQQNLKETLRSLGVREIFEDSASLPGLTRGADVAGKVKVSNILQKAGINVNEKGTEAYAATVVEIENKFGGSTAIEEFNVNRPFVFFIEEESTGNILFAGKVHSPTTQN |
| Enzyme Length | 447 |
| Uniprot Accession Number | Q9V3N1 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Serine protease inhibitor that functions in embryonic dorsoventral patterning and the melanization immune response (PubMed:14654000, PubMed:14667416, PubMed:12408809, PubMed:12456640, PubMed:16861233, PubMed:16322759, PubMed:18801354, PubMed:22227521, PubMed:24260243, PubMed:24788090). Regulates dorsoventral axis formation during early development by inhibiting the serine protease easter, and is therefore important for restricting activity of the Toll signaling pathway to the ventral part of the embryo (PubMed:14654000, PubMed:14667416). Also plays an essential role in the melanization immune response to both physical wounding and septic infection using certain bacteria and fungi (PubMed:12408809, PubMed:12456640, PubMed:18801354, PubMed:22227521). Negatively regulates the Hayan-dependent prophenoloxidase 1 (PPO1)-activating cascade in the hemolymph by inhibiting the serine proteases MP1 and Sp7 (PubMed:12408809, PubMed:12456640, PubMed:16861233, PubMed:16322759, PubMed:18801354, PubMed:22227521, PubMed:24260243, PubMed:24788090). May be involved in negatively regulating the melanotic encapsulation around eggs of the parasite L. boulardi (PubMed:12408809, PubMed:15749104). {ECO:0000269|PubMed:12408809, ECO:0000269|PubMed:12456640, ECO:0000269|PubMed:14654000, ECO:0000269|PubMed:14667416, ECO:0000269|PubMed:15749104, ECO:0000269|PubMed:16322759, ECO:0000269|PubMed:16861233, ECO:0000269|PubMed:18801354, ECO:0000269|PubMed:22227521, ECO:0000269|PubMed:24260243, ECO:0000269|PubMed:24788090}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (2); Mutagenesis (2); Signal peptide (1); Site (1) |
| Keywords | Glycoprotein;Protease inhibitor;Reference proteome;Secreted;Serine protease inhibitor;Signal |
| Interact With | |
| Induction | INDUCTION: In adults, up-regulated between 0 and 3 hours after bacterial infection and fungal infection (PubMed:12408809). Then appears to be down-regulated in the hemolymph between 3 and 17 hours after bacterial infection (PubMed:12456640, PubMed:16322759). {ECO:0000269|PubMed:12408809, ECO:0000269|PubMed:12456640, ECO:0000269|PubMed:16322759}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12408809, ECO:0000269|PubMed:12456640, ECO:0000269|PubMed:14667416}. Note=Secreted into the hemolymph (PubMed:12456640). Detected in the perivitelline fluid of embryos (PubMed:14667416). {ECO:0000269|PubMed:12456640, ECO:0000269|PubMed:14667416}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11252055; 11606746; 11719534; 12032070; 12364793; 12728280; 14711428; 14734104; 15032585; 15199954; 15201320; 15538387; 16271864; 16566925; 17054780; 17356067; 17588928; 18613977; 18854145; 18927626; 19064709; 19109990; 19129115; 19557185; 19849829; 19851448; 19939842; 19951294; 20375588; 20605458; 21480662; 21683256; 21940639; 22724070; 23071443; 23583758; 23840627; 23944235; 24302569; 24475130; 24865556; 25312911; 25409104; 25609699; 26173477; 27603121; 28432215; 28450373; 28504247; 28578657; 29804808; 30992041; 31353314; 31722958; 31794428; 31959286; 32143742; 32598400; 32901612; 33723074; 33891900; 33914801; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,795 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |