- Tools
- Downloads
- Links
- Community
- About
- Help
FB2026_01
,
released March 12, 2026
Dicer, Dcr1
ribonuclease III family, double-stranded RNA domain binding domain, DEAD/DEAH box helicase, PAZ domain - an enzyme involved in degrading RNA - involved in double-stranded RNA interference (RNAi) and post-transcriptional gene regulation (PTGS)
Please see the JBrowse view of Dmel\Dcr-1 for information on other features
To submit a correction to a gene model please use the Contact FlyBase form
AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.
Gene model reviewed during 5.47
Gene model reviewed during 5.53
There is only one protein coding transcript and one polypeptide associated with this gene
Component of the miRNA-directed RISC loading complex (miRLC), composed of at least Dcr-1, AGO1 and loqs, which processes pre-miRNAs and loads the resulting miRNAs into the Argonaute 1 (AGO1)-containing RNA-induced silencing complex (miRISC) (PubMed:15918769, PubMed:19451544). Interacts (via helicase domain) with dicing cofactor loqs isoform-PB (loqs-PB) (via DRBM 3 domain); this interaction enhances processing of pre-miRNAs by increasing substrate binding affinity of the dicer (PubMed:15985611, PubMed:17666393, PubMed:19635780, PubMed:36182693). Also able to interact with loqs isoforms PA and PC, however the relevance of such interactions are unclear in vivo (PubMed:17666393, PubMed:19635780). Different regions of the Dcr-1-loqs-PB heterodimer collaborate to recognize, bind and position the pre-miRNA for Dcr-1 mediated cleavage (PubMed:36182693). In the absence of authentic miRNA substrates, the heterodimer favors a closed, catalytically incompetent, conformation, whereas binding of authentic pre-miRNA substrates stabilizes the relatively rare open, catalytically competent, conformation of the heterodimer (PubMed:36182693). During substrate recognition, the Dcr-1 PAZ domain and pre-miRNA interact with the DRBM 1 domain of loqs-PB, which likely contributes to substrate recognition and stabilization (PubMed:36182693). At the miRNA binding stage, the Dcr-1 DRBM domain and loqs-PB DRBM domains then bind the pre-miRNA in tandem to form a tight 'belt' around the pre-miRNA stem, the pre-miRNA loop is docked in the loop-binding region formed by DUF283, DRBM and part of the N terminus of Dcr-1, and the loqs-PB DRBM 1 and the wing domain of Dcr-1 act together to bind the 5' and 3' pre-miRNA termini within the PAZ and platform domains of Dcr-1 (PubMed:36182693). These interactions between the proteins and their pre-miRNA substrate stabilize a distorted form of the pre-miRNA and position the scissile phosphodiester bonds of the pre-miRNA at the RNase III catalytic cleavage sites of Dcr-1 (PubMed:36182693). Following Dcr-1 mediated cleavage, the miRNA duplex remains bound to loqs-PB DRBM 1, which dissociates from the Dcr-1 RNase III 1 domain but remains in contact with the PAZ and wing domains, suggesting that the heterodimer presents the mature miRNA to Ago2 for loading into the RNA-induced silencing complex (miRISC) (PubMed:36182693). Interacts with AGO2 and Fmr1 to form a RNA-induced silencing complex (siRISC), a ribonucleoprotein (RNP) complex involved in translation regulation; other components of the complex are RpL5, RpL11, AGO2 and Rm62 (PubMed:11498593, PubMed:12368261). Interacts with piwi and vas; these interactions occur in the polar granules (PubMed:16949822).
The helicase domain is essential for substrate discrimination (PubMed:21926993). Probably identifies authentic miRNA substrates, by binding to the miRNA characteristic single-stranded terminal loop, checking the loop size, and measuring the distance between the terminal loop and the 3' overhanging (3'ovr) termini which is bound by the PAZ domain (PubMed:21926993).
The PAZ domain is important for substrate discrimination as it recognizes and binds the characteristic two-nucleotide, 3' overhanging (3'ovr) termini of pre-miRNA substrates prior to cleavage (PubMed:36182693). The PAZ and platform domains form a binding pocket that binds the 5' terminal nucleotide of the pre-miRNA (PubMed:36182693).
RNase III 1 domain is necessary for cleaving the 3' (bottom) strand of pre-miRNA hairpins (pri-let-7) (PubMed:17666393, PubMed:36182693). Together with the RNase III 2 domain forms a cleavage processing center with the RNase III 1 and RNase III 2 domains cutting the 3' (bottom) and 5' (top) strand respectively, excising the miRNA from the pre-miRNA pri-let-7 and creating the characteristic two-nucleotide 3' overhang terminus (PubMed:17666393, PubMed:36182693).
RNase III 2 domain is necessary for cleaving the 5' (top) strand of pre-miRNA hairpins (pri-let-7) (PubMed:17666393, PubMed:36182693). Together with the RNase III 1 domain forms a cleavage processing center with the RNase III 1 and RNase III 2 domains cutting the 3' (bottom) and 5' (top) strand respectively, excising the miRNA from the pre-miRNA pri-let-7 and creating the characteristic two-nucleotide 3' overhang terminus (PubMed:17666393, PubMed:36182693).
Within the closed conformation of the Dcr-1-loqs-PB heterodimer, the DRBM domain blocks access of pre-miRNA substrates to the RNase III active sites.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Dcr-1 using the Feature Mapper tool.
The testis specificity index was calculated from modENCODE tissue expression data by Vedelek et al., 2018 to indicate the degree of testis enrichment compared to other tissues. Scores range from -2.52 (underrepresented) to 5.2 (very high testis bias).
JBrowse - Visual display of RNA-Seq signals
View Dmel\Dcr-1 in JBrowse3-76
3-78.3
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 JBrowse 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.
monoclonal
polyclonal
Dcr-1 is required for normal projection neuron dendrite targeting and axon-terminal elaboration.
Expression is not enriched in embryonic gonads.
Dcr-1 is not required for repeat-associated small interfering RNA (rasiRNA) production
Source for identity of: Dcr-1 CG4792
