Low-frequency RNA-Seq exon junction(s) not annotated.
Annotated transcripts do not represent all possible combinations of alternative exons and/or alternative promoters.
Gene model reviewed during 5.49
3.3 (northern blot)
None of the polypeptides share 100% sequence identity.
887 (aa); 97 (kD observed); 97 (kD predicted)
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\qua using the Feature Mapper tool.
In oocyte stages S8-S10A, qua protein colocalizes with the subcortical actin filament network in the nurse cells and the oocyte. It is also present in the cytoplasm of nurse cells. Occasionally, it localizes to ring canals. In stage S10B, the levels of qua protein rise significantly and it is found along the length of the newly assembled actin filament bundles in the nurse cell cytoplasm.
GBrowse - Visual display of RNA-Seq signalsView Dmel\qua in GBrowse 2
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: qua CG6433
Source for merge of qua anon-WO0140519.71 was sequence comparison ( date:051113 ).
dsRNA made from templates generated with primers directed against this gene tested in RNAi screen for effects on Kc167 and S2R+ cell morphology.
dsRNA made from templates generated with primers directed against this gene is tested in an RNAi screen for effects on actin-based lamella formation.
qua protein can bind and bundle filamentous actin in vitro, regardless of the concentration of calcium ions.
The villin-like product of the qua locus is required for the formation of cytoplasmic actin filament bundles in nurse cells, possibly by regulating both the polymerization and organization of actin filaments as has been demonstrated for vertebrate villin in vitro.
Mutations at the qua locus cause defects in midoogenesis.
Wieschaus and Nusslein-Volhard.