Iap2, DIAP-2, DIHA, DIAP, dILP
N-terminal baculovirus IAP repeat domain and C-terminal RING ubiquitin ligase domain protein - required for immune response to bacteria - promotes cytoplasmic cleavage and nuclear translocation of the NF-kappaB homolog Relish - controls the level of caspase activity by forming a covalent adduct with the catalytic machinery of drICE
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.50
Interacts with the caspase Strica (PubMed:11550090). Interacts (via BIR2 domain) with rpr and grim (PubMed:18166655). Interacts (via the BIR2 and BIR3 domains) with hid (PubMed:18166655). Interacts (via BIR3 domain) with Drice (PubMed:18166655). Interacts with Dredd; likely to bind Dredd simultaneously with Fadd to form a trimeric complex (PubMed:22549468).
Caspase-dependent cleavage is required for suppression of Drice-mediated cell death.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Diap2 using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\Diap2 in GBrowse 2
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Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
RNAi screen using dsRNA made from templates generated with primers directed against this gene causes a specific decrease in AttA activity in response to heat-killed E.coli when assayed in S2 cells. This effect is independent of ecdysone. Iap2 functions downstream of imd in the fat body, as shown by the ability of Iap2 dsRNA to inhibit transcriptional activation of Dpt by imd. Tab2 RNAi fails to prevent AttA activation by Iap2, indicating that Tab2 is upstream of Iap2 in the imd signalling pathway.
The product of Iap2 can inhibit mammalian cell death induced by overexpression of caspases 1 and 2.
Expression of death inducers rpr and W and the repression of death inhibitor Iap2 correlates with the onset of histolysis in the larval salivary gland, suggesting that programmed cell death may be coordinated by both inductive and repressive mechanisms.
Drosophila homolog of baculovirus iap is molecularly cloned.
The conservation of IAPs from humans to Drosophila suggests that they are important for the regulation of apoptosis.