Ago-3, BEST:LD15785
cleaves transposon derived piwi-interacting RNAs to form an adaptive system for transposon control
Please see the JBrowse view of Dmel\AGO3 for information on other features
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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 5.55
Gene model reviewed during 5.45
Low-frequency RNA-Seq exon junction(s) not annotated.
Component of the ping-pong piRNA processing (4P) complex consisting of krimp, aub and AGO3 (PubMed:19959991, PubMed:26295961, PubMed:34210982). Interacts (via N-terminus when not methylated on arginine residues) with krimp (via non-canonical tudor domain); this interaction leads to symmetrical dimethylation on AGO3 arginine residues and its subsequent dissociation from krimp (PubMed:26212455, PubMed:26295961, PubMed:34210982). Krimp associated AGO3 is mostly free of piRNA binding and the interaction plays an important role in the loading of AGO3 with piRNAs; piRNA binding may stimulate dissociation of the two proteins (PubMed:26212455, PubMed:26295961). May form part of a piRNA processing complex consisting of tud, aub and AGO3 (PubMed:19959991). Interacts (when symmetrically dimethylated on arginine residues) with tud (PubMed:19959991, PubMed:26212455). Forms a complex with smg, twin, aub, nos mRNA and piRNAs that target the nos 3'-untranslated region, in early embryos (PubMed:20953170). Interacts (via the N-terminal region when symmetrically methylated on arginine residues) with papi (via C-terminus); this interaction is RNA-independent and may be required for AGO3 localization to the nuage (PubMed:21447556). Interacts with TER94 and tral (PubMed:21447556).
Symmetrically dimethylated on Arg-4, Arg-68 and Arg-70, most likely by csul/PRMT5/DART5 (PubMed:19377467, PubMed:19959991, PubMed:26212455). Methylation state probably functions as an indicator of its piRNA binding state (PubMed:34210982).
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\AGO3 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).
Comment: postgermarial
AGO3 protein is present in the cytoplasm of germline stem cells, gonialblasts, and spermatogonia.
JBrowse - Visual display of RNA-Seq signals
View Dmel\AGO3 in JBrowse3-47
3-44.1
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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 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.
polyclonal
monoclonal
Source for merge of: AGO3 CG40300
Source for merge of: AGO3 BEST:LD15785