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FB2026_01
,
released March 12, 2026
dInR, insulin receptor, DIR, sprout, IR
receptor tyrosine kinase - a key component of an evolutionarily conserved signaling pathway that plays an essential role in controlling body, organ, and cell size
Please see the JBrowse view of Dmel\InR for information on other features
To submit a correction to a gene model please use the Contact FlyBase form
AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.
Gene model reviewed during 5.47
Gene model reviewed during 5.55
3.586 (longest cDNA)
11 (northern blot)
2146 (aa); 280, 170, 120, 90, 60 (kD observed)
2148 (aa)
The α subunit of InR protein is derived from
proteolytic processing of the 280kD proreceptor.
The β subunit of InR protein is derived from
proteolytic processing of the 280kD proreceptor.
The 90kD β subunit of InR protein is derived
from proteolytic processing of the larger 170kD β subunit after removal
of a 60kD carboxy-terminal free peptide.
The free 60kD carboxy terminus of InR protein
is produced from the 170kD β subunit by proteolytic processing.
InR protein includes a novel 400aa carboxyl-terminal extension with putative binding sites for SH2-domain containing signalling proteins.
An antibody prepared against a part of the human insulin receptor peptide that is conserved in the Drosophila sequence reacts with a 95kD polypeptide in Drosophila which is presumed to be an autophosphorylated β subunit of the receptor.
Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds (PubMed:37805602). The alpha chains contribute to the formation of the ligand-binding domain, while the beta chains carry the kinase domain (By similarity). Interacts (via C-terminal cytoplasmic region) with dock/dreadlocks (via SH2 and SH3 domains); when autophosphorylated (PubMed:12702880). May interact (via beta subunit) with chico/IRS-1; this interaction may lead to tyrosine phosphorylation of the insulin receptor substrate chico (PubMed:10455177). Interacts with Elp6; the interaction may stabilize Elp6 (PubMed:22645656).
The 280 kDa proreceptor is proteolytically processed to form a 120 kDa alpha subunit and a 170 kDa beta subunit. The beta subunit undergoes cell-specific cleavage to generate a 90 kDa beta subunit and a free 60 kDa C-terminal subunit. Both the 90 kDa and the 170 kDa beta subunits can assemble with the alpha subunits to form mature receptors.
Autophosphorylated on tyrosine residues, including Tyr-1549 and Tyr-1550, in response to exogenous insulin (PubMed:12702880, PubMed:18327897, PubMed:21707536, PubMed:3014506). Tyr-1549 and Tyr-1550 are dephosphorylated by Ptp61F recruited by the dock/dreadlocks adapter protein (PubMed:21707536).
Phosphorylation of Tyr-1354 is required for Chico-binding.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\InR using the Feature Mapper tool.
The testis specificity index was calculated from modENCODE tissue expression data by Vedelek et al., 2018 to indicate the degree of testis enrichment compared to other tissues. Scores range from -2.52 (underrepresented) to 5.2 (very high testis bias).
Comment: P3 expression
Comment: P3 expression
Comment: P1 expression
Comment: P1 expression
Comment: P1 expression
Comment: P3 expression
Isoform-specific expression is observed from three different InR promoters, P1, P2, and P3.
InR protein is abundant and widely distributed from the beginning of cellularization to the onset of gastrulation. It is found in all three germ layers in stage 9-11 embryos. It is particularly prominent in the posterior midgut primordium, epidermis and neuroblasts. By stage 12, strong expression is seen in the epidermis, the midgut, the hindgut, and in a segmentally repeated pattern in the ventral cord. In late embryonic stages, staining persists in both cell bodies and axons along the ventral nerve cord and in the supraoesophageal ganglion.
JBrowse - Visual display of RNA-Seq signals
View Dmel\InR in JBrowse
Maps to 3R.
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 JBrowse 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.
InR plays an important role in spermatogenesis, by stimulating germline stem cell proliferation and spermatocyte growth.
When dsRNA constructs are made and transiently transfected into S2 cells in RNAi experiments, a decrease in the ratio of cells in prometaphase and metaphase versus the total number of mitotic cells is seen.
dsRNA made from templates generated with primers directed against this gene tested in RNAi screen for effects on Kc167 and S2R+ cell morphology.
InR autonomously controls cell and organ size.
Phylogenetic analysis of the PTK family.
InR has a role in regulation of cell proliferation during development.
InR has been cloned, primary structure determined, functional expression of the predicted polypeptide analysed and mutations isolated. Loss of function mutations cause pleiotropic recessive phenotypes that lead to embryonic lethality. InR activity is required in the embryonic epidermis and nervous system.
InR has been cloned and sequenced.
Chimeric receptors containing either all or a portion of the cytoplasmic domain of Drosophila InR are indistinguishable from the human insulin receptor in terms of signalling when transfected into COS-7 or CHO cells.
InR carboxy terminus undergoes a conformational change during the activation-inactivation cycle of the kinase which can be sterically hindered by an antipeptide antibody against the carboxy terminus. Conformational changes have also been observed in the mammalian insulin receptor.
The temporal and spatial restriction of the InR protein to the developing neuromuscular junction suggests that it might be involved in the expansion and maturation of motor innervation during larval growth.
InR has high degree of similarity to the human insulin receptor.
A specific high affinity insulin binding protein, a membrane associated glycoprotein with an Mr of 300,000 to 400,000, has been found that binds bovine and porcine insulin.
High affinity insulin binding and insulin-dependent protein tyrosine kinase activity are found in membranes.
Insulin-dependent protein tyrosine kinase activity is differentially expressed during development, peaks during embryogenesis, suggesting that insulin may be involved in tissue and organ differentiation during embryogenesis.
Source for merge of: InR l(3)93Dj
Source for merge of: InR sprout
