Dcr2, Dicer, dmDcr-2, dcr
Gene model reviewed during 5.44
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.50
None of the polypeptides share 100% sequence identity.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Dcr-2 using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\Dcr-2 in GBrowse 2
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
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.
Source for identity of: Dcr-2 CG6493
The loqs-PD isoform is capable of associating with the Dcr-2 protein, but not with the Dcr-1 protein. The loqs-PB and loqs-PA isoforms can associate with the Dcr-1 protein, and also to some extent with Dcr-2 protein.
The loqs-PB isoform, and to a lesser extent the loqs-PA isoform, is capable of associating with the Dcr-1 protein. The loqs-PD isoform is capable of associating with the Dcr-2 protein, but not with the Dcr-1 protein.
The Dcr-2-r2d2 heterodimer acts as a gatekeeper for the assembly of AGO2 complexes, promoting the incorporation of siRNAs and disfavoring miRNAs as loading substrates for AGO2. A separate mechanism acts in parallel to favor miRNA/miRNA* duplexes and exclude siRNAs from assembly into AGO1 complexes.
Dcr-2 is required for maintenance of long-distance chromosomal interactions between endogenous PcG target loci.
Expression is enriched in embryonic gonads.
Dcr-2 is not required for repeat-associated small interfering RNA (rasiRNA) production
The orientation of the Dcr-2/r2d2 protein heterodimer on the siRNA duplex determines which siRNA strand associates with the core RISC (RNA-induced silencing complex) protein AGO2. r2d2 protein binds the siRNA end with the greatest double-stranded character, thereby orienting the Dcr-2/r2d2 heterodimer on the siRNA duplex. Strong binding by the r2d2 protein requires a 5'-phosphate on the siRNA strand that is excluded from the RISC.
Dcr-2 protein alone efficiently cleaves dsRNA into siRNA. This enzymatic activity is not affected by association with r2d2 protein. Dcr-2 protein alone does not bind siRNA, but the r2d2/Dcr-2 protein complex binds siRNA and also facilitates the loading of siRNA onto the RNA-initiated silencing complex (RISC). This latter activity is dependent on the dsRNA-binding domains of the r2d2 protein.