trp-like, DmTRPL, trp-l
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.48
4.0 (northern blot)
1124 (aa); 128 (kD predicted)
Forms heteromultimers with Trpgamma and, to a lower extent, with trp. Interacts with Fkbp59 in vivo and is found in the inaD signaling complex.
Binding of calmodulin to binding site 1 is Ca(2+) dependent, whereas binding of calmodulin to site 2 is Ca(2+) independent.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\trpl using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\trpl 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.
trpl protein is translocated in a light-dependent manner between the rhabdomere photoreceptor membrane and an intracellular storage channel. The level of trpl protein in the rhabdomere is high in the dark and low in the light.
Shows particularly robust cycling of transcription in adult heads, as assessed by expression analysis using high density oligonucleotide arrays with probe generated during three 12-point time course experiments over the course of 6 days.
The trp and trpl channels are specific targets of metabolic stress; anoxia opens trp and trpl channels in the dark. Mitochondrial uncouplers and depletion of ATP activate the trp and trpl channels in the dark in situ.
The fact that the ability of non-inaD bound trp to contribute to photoreceptor responses depends on the presence of trpl suggests that there may be interactions between trpl and the non-inaD-bound trp protein.
The biophysical properties of trpl channels expressed in a stably transfected cell line are compared to those of trp. Results show that, for a wide range of properties, the native and expressed channels are functionally equivalent lending strong support to the proposal that channels encoded by trpl can completely account for the component of the light-sensitive conductance remaining in the trp mutant.
trpl expression is associated with the appearance of an outwardly rectifying, Ca2+ permeable, nonselective cation current that is constitutively active under nonstimulating conditions, giving rise to large increases in basal Ca2+.
Coexpression of trp and trpl leads to a store-operated, outwardly rectifying current distinct from that owing to either trp or trpl alone. trp and trpl proteins interact directly, indicating the trp-trpl-dependent current is mediated by heteromultimeric association between the two subunits.
trpl activity is masked by functional trp channels and together trp and trpl are essential components of the light-activated conductance. trp and trpl need not form heteromeric channels because trpl mutants only contain trp protein and trp mutants only have trpl protein. Since trp and trpl mutants respond to light activation then each channel on its own must be capable of sensing the intracellular messenger that gates the light activated conductance. Activation of one does not require prior activation of the other.
Analysis of trp-trpl fusion proteins suggests that the carboxy terminal domain of trpl plays an important role in determining constitutive activity of the protein, and the carboxy terminal domain of trp contains structural features necessary for activation by thapsigargin.
The C-terminal domain of the trpl protein contains two calmodulin-binding sites.
trpl expressed in Sf9 cells can be activated by hormonal factors after coinjection with recombinant viruses coding for various heptahelical, G-protein-coupled receptors.
trpl expression in Sf9 cells is associated with appearance of Ca2+ permeable, non-selective cation channels.
The calmodulin-binding and ankyrin-repeats have been investigated in vitro using fusion proteins.