Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.52
None of the polypeptides share 100% sequence identity.
674 (aa); 90 (kD observed); 80 (kD predicted)
Interacts with the C-terminus of trp, and with norpA and inaC to form the inaD signaling complex. Interacts with FKBP59, which together with trpl, rhodopsin and calmodulin may also be part of the inaD complex.
Phosphorylated by inaC.
Second PDZ domain is a type I PDZ domain that tethers type I PDZ ligand inaC by interaction with its C-terminus.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\inaD using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signalsView Dmel\inaD 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.
dsRNA made from templates generated with primers directed against this gene tested in RNAi screen for effects on Kc167 and S2R+ cell morphology.
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.
inaD functions as a master scaffold for subcellular compartmentalization of the phototransduction machinery.
inaD protein binds directly to norpA protein via two terminally positioned PDZ1 and PDZ5 domains. PDZ1 binds to the C-terminus of norpA, while PDZ5 binds to an internal region overlapping with the G-box homology region.
A novel tripeptide motif in the C terminus of norpA associates with inaD. Expression of transgenic norpA that displays no interaction with inaD reveals abnormal ERG with slow kinetics suggesting the association between inaD and norpA is important in the regulation of activation and deactivation of visual transduction.
The inaD protein is composed of five distinct PDZ domains and acts as an organising scaffold for photoreceptor signalling complexes in vivo.
Antibodies to the inaD protein co-precipitate trp gene product. The interaction has been mapped to the 19 amino acid C-terminus of trp and the PDZ domain of inaD. inaD functions as a regulatory subunit of the trp Ca2+ channel.