Low-frequency RNA-Seq exon junction(s) not annotated.
Supported by strand-specific RNA-Seq data.
Gene model reviewed during 5.52
2.0 (northern blot)
365 (aa); 41 (kD predicted)
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Gs2 using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\Gs2 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: Gs2 CG1743
Gs1 and Gs2 have been isolated and sequenced. Evolutionary analysis is in agreement with the hypothesis that the two genes are derived from a duplication event that occurred near the time of divergence between Insecta and Vertebrata. Both isoforms catalyse all reactions catalysed by other glutamine synthetases, but the different kinetic parameters and the different cellular compartmentalisation suggests strong functional specialisation. Gs1 and Gs2 gene products are essential for the early stages of embryonic development. Preliminary results show strikingly distinct spatial and temporal patterns of expression of the two isoforms at later stages of development.
Isolated from a genomic library using a DNA fragment comprising 80% of the coding region of glutamine synthetase from Chinese hamster ovary cells as a probe.
Structural gene for glutamine synthetase II. Completely separable from glutamine synthetase I by DEAE chromatography. The GSII protein was purified from adult Drosophila (Scalenghe and Ritossa, 1976) and was isolated by sequence identity with the hamster gene (De Pinto, Caggese, Prezioso and Ritossa, 1987). The enzyme is a multimer of a single subunit (MW 42,000). The complete enzyme has an approximate molecular weight of 360,000 and differs from the GSI enzyme in both subunit molecular weight and in isoelectric point. 90% of glutamine synthetase activity is due to GSII, which is the most abundant adult form.