ALS, Dα1, nAcRalpha-96Aa, nAcRα-96Aa, Acr96Aa
Gene model reviewed during 5.47
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.44
Stop-codon suppression (UAG) postulated; FBrf0216884.
Gene model reviewed during 5.56
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\nAChRα1 using the Feature Mapper tool.
Transcript is detected in the larval fat body and in the clusters of cells in the pars intercerebralis corresponding to the medial neurosecretory cell clusters (m-NSCs) that express the insulin like protein genes.
GBrowse - Visual display of RNA-Seq signalsView Dmel\nAChRα1 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.
"nAcRα-96Ab" is a putative chimeric gene derived from the "nAcRα-96Aa" and "nAcRβ-64B" genes (where coding sequences of the two parental genes contribute to the coding sequence of the chimeric gene).
The distribution of nAcRα-96Aa protein in the developing and differentiated nervous system has been studied.
Antibodies raised against fusion constructs encompassing specific regions of the Acr64B and Acr96Aa proteins were used to investigate a potential association of these two polypeptides.
An alpha-like subunit that resemble ligand-binding subunits of vertebrate subunits.
Characterisation of toxin binding to the domain carrying the cholinergic binding sites of nAcRα-96Aa.
Structural gene encoding a Drosophila homologue of a subunit of vertebrate nicotinic acetylcholine receptors (nAChR); inferred to be homologous to neuronal α subunits based on the cystein doublet at amino-acid residues 201 and 202.