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Def | Defensin (Def) encodes an antibacterial peptide with activity against Gram-positive bacteria. It is induced in the fat body during the systemic immune response and is expressed in various epithelia. The expression of Def is regulated at the transcriptional level by both the immune deficiency and Toll pathways; Belongs to the invertebrate defensin family. Type 1 subfamily. (92 aa) | ||||
Dsor1 | Dual specificity mitogen-activated protein kinase kinase dSOR1; Required downstream of Raf in the sevenless (sev), torso (tor), and Drosophila EGF receptor homolog (DER) signal transduction pathways. Involved in both positive regulation (at the posterior terminus) and negative regulation (at the anterior domain) of tll, as in other terminal class gene products, maybe via the ERK-A kinase. Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily. (396 aa) | ||||
Drsl2 | Drosomycin-like 2 (Drsl2) encodes a secreted peptide with homology to the antifungal peptide encoded by Drs. (70 aa) | ||||
Drsl3 | Drosomycin-like 3 (Drsl3) encodes a secreted peptide with homology to the antifungal peptide encoded by Drs. It is expressed in the gut under the control of the JAK-STAT pathway. (71 aa) | ||||
Drsl4 | Drosomycin-like 4 (Drsl4) encodes a secreted peptide with homology to the antifungal peptide encoded by Drs. (71 aa) | ||||
Drsl5 | Drosomycin-like 5 (Drsl5) encodes a secreted peptide with homology to the antifungal peptide encoded by Drs. (69 aa) | ||||
Drsl1 | Drosomycin-like C1; It is involved in the biological process described with: defense response to fungus. (69 aa) | ||||
PGRP-SA | Peptidoglycan-recognition protein SA; Peptidoglycan-recognition protein that plays a key role in innate immunity by binding to peptidoglycans (PGN) of Gram-positive bacteria and activating the Toll pathway upstream of spz activating enzyme SPE. Has no activity against Gram-negative bacteria and fungi. Shows some partial redundancy with PRPGP-SD in Gram-positive bacteria recognition. May act by forming a complex with GNBP1 that activates the proteolytic cleavage of Spatzle and the subsequent activation of Toll pathway. Binds to diaminopimelic acid-type tetrapeptide PGN (DAP-type PGN) an [...] (203 aa) | ||||
Fur2 | Furin-like protease 2; Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif. (1682 aa) | ||||
sphe | Spheroide (sphe) encodes a serine protein homologue, a serine protease with no catalytic activity. (249 aa) | ||||
psh | Serine protease persephone; Serine protease that plays a key role in innate immunity in response to Gram-positive bacterial and fungal proteases. Acts as a component of the Toll pathway upstream of protease spz processing enzyme SPE and Tl ligand spz. Nec regulates the cascade by inhibiting psh ; Belongs to the peptidase S1 family. CLIP subfamily. (394 aa) | ||||
GNBP1 | Gram-negative bacteria-binding protein 1; Plays a key role in innate immunity by acting as a pattern recognition receptor for beta-1,3-glucan from fungi and lipopolysaccharide from Gram-negative bacteria. Upon recognition of invading micro-organism-derived products, acts upstream of protease spz processing enzyme SPE to activate the Toll pathway and to induce the expression of antimicrobial peptides drosomycin, cecropin and attacin. Belongs to the insect beta-1,3-glucan binding protein family. (492 aa) | ||||
Ser12 | Serine protease 12; Serine-type endopeptidase activity. It is involved in the biological process described with: wound healing; proteolysis; Belongs to the peptidase S1 family. (245 aa) | ||||
Send2 | Spermathecal endopeptidase 2; Serine-type endopeptidase activity. It is involved in the biological process described with: proteolysis; Belongs to the peptidase S1 family. (239 aa) | ||||
modSP | Modular serine protease non-catalytic chain; 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. 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. Functions in a separate pathway to the psh-mediated activation of the Toll pathway. Belongs to the peptidase S1 family. (628 aa) | ||||
AttD | Attacin-D (AttD) encodes is an immune inducible peptide that shows homology to antibacterial peptides having activity against Gram-negative bacteria. (181 aa) | ||||
SPE | Spaetzle-processing enzyme heavy chain; 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. Acts downstream of pathogen recognition receptors PGRP-SA and GNBP1 and protease grass in response to Gram-positive bacterial infection. Acts downstream of protease psh in response to fungal infection. Belongs to the peptidase S1 family. CLIP subfamily. (400 aa) | ||||
spz | Protein spaetzle C-106; Spatzle (spz) encodes a secreted protein which, after cleavage by an extracellular serine protease (encoded by ea or SPE), can induce the dimerization of the product of Tl, and the subsequent activation of the Toll pathway. It contributes to function of the Toll signaling cascade, which plays a key role in various developmental and immune processes, notably embryonic dorso-ventral patterning and regulation of antimicrobial peptides. (326 aa) | ||||
CecA1 | Cecropin-A1; Cecropin A1 (CecA1) encodes an antibacterial peptide with activity against Gram-negative bacteria. It is expressed in the fat body during the systemic immune response and in various epithelia, and it is regulated at the transcriptional level, mostly by the immune deficiency pathway; Belongs to the cecropin family. (63 aa) | ||||
CecA2 | Cecropin A2 (CecA2) encodes an antibacterial peptide with activity against Gram-negative bacteria. It is expressed in the fat body during the systemic immune response and in various epithelia, and it is regulated at the transcriptional level by the immune deficiency pathway. (63 aa) | ||||
CecC | Cecropin-C; Cecropin C (CecC) encodes an antibacterial peptide with activity against Gram-negative bacteria. It is strongly expressed at the pupal stage. (63 aa) | ||||
CecB | Cecropin-B; Cecropin B (CecB) encodes an helicoidal antibacterial peptide with activity against Gram-negative bacteria. It is mostly expressed at the pupal stage; Belongs to the cecropin family. (63 aa) | ||||
DptA | Diptericin A (DptA) encodes an immune inducible antibacterial peptide with activity against Gram-negative bacteria. It is expressed in the fat body during the systemic immune response and in various epithelia. Its expression is regulated at the transcriptional level by the immune deficiency pathway; Belongs to the attacin/sarcotoxin-2 family. (106 aa) | ||||
Mtk | Metchnikowin (Mtk) encodes an antifungal peptide that is secreted from the fat body during the systemic immune response, and is produced by various epithelia. Its expression is regulated at the transcriptional level by the immune deficiency and/or Toll pathways. (52 aa) | ||||
PGRP-LC | Peptidoglycan-recognition protein LC; Major activator of the imd/Relish pathway and is likely to encode a pattern recognition molecule for the humoral immune response. Required for Relish processing and nuclear translocation following proteolytic cleavage. Involved in the response to lipopolysaccharide (LPS) and peptidoglycan of Gram-negative bacteria. The different isoforms probably display different recognition capabilities to various microbial patterns. [Isoform x]: Mediates the response to LPS, peptidoglycan and Gram-negative bacteria; Belongs to the N-acetylmuramoyl-L-alanine amid [...] (520 aa) | ||||
AttB | Attacin-B (AttB) encodes an immune inducible peptide that shows homology to antibacterial peptides having activity against Gram-negative bacteria; Belongs to the attacin/sarcotoxin-2 family. (218 aa) | ||||
inaD | Inactivation-no-after-potential D protein; Involved in the negative feedback regulation of the light- activated signaling cascade in photoreceptors through a calcium- mediated process. Interacts with tetrapeptide ligand located in C- terminal sequence of 3 key components of the visual cascade, tethering them and forming a macromolecular signaling phototransduction complex. (686 aa) | ||||
AttC | Immune-induced peptide 16; Attacin-C (AttC) encodes an immune inducible peptide that shows homology to antibacterial peptides having activity against Gram-negative bacteria; Belongs to the attacin/sarcotoxin-2 family. (241 aa) | ||||
PGRP-LE | Peptidoglycan-recognition protein LE; Peptidoglycan-recognition protein that plays a key role in innate immunity by binding to murein peptidoglycans (PGN) of Gram- negative bacteria and activating the imd/Relish pathway. Has no activity against on Gram-positive bacteria. Binds to diaminopimelic acid-type PGN (DAP-type PGN), an activator of the imd/Relish pathway. Functions synergistically with PGRP-LC in producing resistance to E.coli and B.megaterium infections, which have the DAP-type peptidoglycan. Acts both upstream and in parallel with PGRP-LC in the imd/Relish pathway, and is req [...] (345 aa) | ||||
Dro | Drosocin (Dro) encodes an o-Glycosylated antibacterial peptide with activity against Gram-negative and Gram-positive bacteria. It is expressed in the fat body during the systemic immune response and is expressed in various epithelia. The expression of Dro is regulated at the transcriptional level mostly by the immune deficiency pathway; Belongs to the drosocin family. (64 aa) | ||||
Fur1 | Furin-like protease 1, isoforms 1/1-X/2; Furin is likely to represent the ubiquitous endoprotease activity within constitutive secretory pathways and capable of cleavage at the RX(K/R)R consensus motif. (1478 aa) | ||||
imd | Protein immune deficiency; Essential for the imd/NF-kappa-B (Imd) humoral and epithelial immune response to Gram-negative bacteria. Functions as an adapter protein that transduces immunity signals from the activation of pathogen recognition receptors (PRRs) by bacterial infection to the Imd signaling pathway. Binding of diaminopimelic acid-type (DAP-type) bacterial peptidoglycans (PGN) causes multimerization or clustering of PGRP receptors which activate the Imd cascade probably by recruiting imd, Fadd and Dredd to the receptor complex. Once in proximity, Dredd cleaves imd in a Fadd-de [...] (273 aa) |