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General Information
Symbol
Dmel\InR
Species
D. melanogaster
Name
Insulin-like receptor
Annotation Symbol
CG18402
Feature Type
FlyBase ID
FBgn0283499
Gene Model Status
Stock Availability
Gene Summary
Has a ligand-stimulated tyrosine-protein kinase activity. Required for cell survival. Regulates body size and organ size by altering cell number and cell size in a cell-autonomous manner. Involved in the development of the embryonic nervous system, and is necessary for axon guidance and targeting in the visual system. Also plays a role in life-span determination. (UniProt, P09208)
Contribute a Gene Snapshot for this gene.
Also Known As

dInR, insulin receptor, DIR, sprout, IR

Key Links
Genomic Location
Cytogenetic map
Sequence location
3R:21,570,248..21,619,321 [-]
Recombination map
3-72
RefSeq locus
NT_033777 REGION:21570248..21619321
Sequence
Other Genome Views
The following external sites may use different assemblies or annotations than FlyBase.
Function
GO Summary Ribbons
Gene Ontology (GO) Annotations (74 terms)
Molecular Function (8 terms)
Terms Based on Experimental Evidence (4 terms)
CV Term
Evidence
References
inferred from physical interaction with FLYBASE:Ilp5; FB:FBgn0044048
inferred from physical interaction with FLYBASE:Ilp2; FB:FBgn0036046
inferred from physical interaction with UniProtKB:Q9XTN2
(assigned by UniProt )
inferred from physical interaction with FLYBASE:Lar; FB:FBgn0000464
inferred from direct assay
(assigned by UniProt )
inferred from mutant phenotype
(assigned by UniProt )
Terms Based on Predictions or Assertions (6 terms)
CV Term
Evidence
References
enables ATP binding
(assigned by InterPro )
inferred from sequence or structural similarity with UniProtKB:P06213
(assigned by UniProt )
inferred from sequence or structural similarity with UniProtKB:P06213
(assigned by UniProt )
inferred from biological aspect of ancestor with PANTHER:PTN000699611
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN000699611
(assigned by GO_Central )
inferred from sequence or structural similarity with UniProtKB:P06213
(assigned by UniProt )
inferred from biological aspect of ancestor with PANTHER:PTN001230349
(assigned by GO_Central )
Biological Process (62 terms)
Terms Based on Experimental Evidence (57 terms)
CV Term
Evidence
References
involved_in aging
inferred from mutant phenotype
involved_in axon guidance
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
involved_in circadian rhythm
inferred from mutant phenotype
inferred from mutant phenotype
(assigned by UniProt )
inferred from mutant phenotype
inferred from mutant phenotype
inferred from expression pattern
(assigned by UniProt )
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
inferred from genetic interaction with FLYBASE:peb; FB:FBgn0003053
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
inferred from genetic interaction with FLYBASE:mir-305; FB:FBgn0262458
involved_in lipid homeostasis
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
(assigned by UniProt )
inferred from high throughput mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
(assigned by UniProt )
inferred from mutant phenotype
(assigned by UniProt )
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
(assigned by UniProt )
inferred from mutant phenotype
inferred from mutant phenotype
(assigned by UniProt )
inferred from genetic interaction with FLYBASE:Pdk1; FB:FBgn0020386
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
(assigned by UniProt )
inferred from mutant phenotype
inferred from mutant phenotype
involved_in response to anoxia
inferred from direct assay
inferred from genetic interaction with FLYBASE:EcR; FB:FBgn0000546
inferred from mutant phenotype
inferred from mutant phenotype
Terms Based on Predictions or Assertions (8 terms)
CV Term
Evidence
References
inferred from biological aspect of ancestor with PANTHER:PTN000699611
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN001230349
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN001230349
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN000699611
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN000699611
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN000699611
(assigned by GO_Central )
inferred from sequence or structural similarity with UniProtKB:P06213
(assigned by UniProt )
inferred from biological aspect of ancestor with PANTHER:PTN001230349
(assigned by GO_Central )
Cellular Component (4 terms)
Terms Based on Experimental Evidence (2 terms)
CV Term
Evidence
References
Terms Based on Predictions or Assertions (4 terms)
CV Term
Evidence
References
located_in axon
inferred from biological aspect of ancestor with PANTHER:PTN000699611
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN000699611
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN001230349
(assigned by GO_Central )
inferred from biological aspect of ancestor with PANTHER:PTN001230349
(assigned by GO_Central )
Gene Group (FlyBase)
Protein Family (UniProt)
Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily. (P09208)
Summaries
Pathway (FlyBase)
Insulin-like Receptor Signaling Pathway Core Components -
The Insulin-like Receptor (IR) signaling pathway in Drosophila is initiated by the binding of an insulin-like peptides to the Insulin-like receptor (InR). (Adapted from FBrf0232297, FBrf0230017 and FBrf0229989.)
Gene Group (FlyBase)
RECEPTOR TYROSINE KINASES -
Receptor tyrosine kinases (RTK) are single-pass transmembrane receptors expressed on the plasma membrane. Upon the binding of an extracellular signalling molecule (e.g. growth factors, hormones), RTKs dimerize leading to the activation of the intracellular tyrosine kinase domain and intermolecular phosphorylation. The phosphotyrosines function as specific sites for the assembly, phosphorylation and activation of downstream signaling molecules. (Adapted from PMID:20602996).
Protein Function (UniProtKB)
Has a ligand-stimulated tyrosine-protein kinase activity. Required for cell survival. Regulates body size and organ size by altering cell number and cell size in a cell-autonomous manner. Involved in the development of the embryonic nervous system, and is necessary for axon guidance and targeting in the visual system. Also plays a role in life-span determination.
(UniProt, P09208)
Phenotypic Description (Red Book; Lindsley and Zimm 1992)
Inr: Insulin receptor
Encodes the insulin-binding (α) and insulin-dependent protein tyrosine kinase (β) subunits of the insulin receptor of Drosophila melanogaster. In Drosophila cell lines the insulin receptor contains insulin-binding α subunits of 110 or 120 kd, a 95-kd β subunit that is phosphorylated on tyrosine in response to insulin, and a 170-kd protein that may be an incompletely processed receptor. All of the components are processed from a proreceptor, joined by disulfide bonds, and exposed on the cell surface (Petruzzelli et al., 1985a, 1985b, 1986; Fernandez-Almonacid and Rosen, 1987). Subunits in man and in Drosophila are similar both in molecular structure and in insulin-binding and protein tyrosine kinase activities; the latter activity is detected only during certain embryonic periods in Drosophila.
Summary (Interactive Fly)

receptor tyrosine kinase - a key component of an evolutionarily conserved signaling pathway that plays an essential role in controlling body, organ, and cell size

Gene Model and Products
Number of Transcripts
4
Number of Unique Polypeptides
1

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

Protein Domains (via Pfam)
Isoform displayed:
Pfam protein domains
InterPro name
classification
start
end
Protein Domains (via SMART)
Isoform displayed:
SMART protein domains
InterPro name
classification
start
end
Comments on Gene Model

Gene model reviewed during 5.47

Gene model reviewed during 5.55

Sequence Ontology: Class of Gene
Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Assoc. CDS (aa)
FBtr0084121
10706
2144
FBtr0290230
10696
2144
FBtr0290231
9997
2144
FBtr0290232
10063
2144
Additional Transcript Data and Comments
Reported size (kB)

3.586 (longest cDNA)

11 (northern blot)

Comments
External Data
Crossreferences
Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
RefSeq ID
GenBank
FBpp0083519
239.8
2144
6.89
FBpp0288669
239.8
2144
6.89
FBpp0288670
239.8
2144
6.89
FBpp0288671
239.8
2144
6.89
Polypeptides with Identical Sequences

The group(s) of polypeptides indicated below share identical sequence to each other.

2144 aa isoforms: InR-PA, InR-PB, InR-PC, InR-PD
Additional Polypeptide Data and Comments
Reported size (kDa)

2146 (aa); 280, 170, 120, 90, 60 (kD observed)

Comments

The InR protein juxtamembrane NPXY motif is needed for efficient phosphorylation of chico protein, and the InR C-terminal NPXY motifs are necessary for stable interaction with chico protein.

The 2146aa InR proreceptor is processed into the 120kD α and 170kD β InR subunits. The 170kD β subunit is further processed into a 90kD β subunit and a 60kD free carboxyl polypeptide. The subunits assemble into mature InR receptors with the structure α2170)2 and α290)2.

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.

External Data
Subunit Structure (UniProtKB)

Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains contribute to the formation of the ligand-binding domain, while the beta chains carry the kinase domain. When autophosphorylated, the beta-subunit binds the SH2 and SH3 domains of the adapter protein Dock. The beta subunit also binds and tyrosine phosphorylates the insulin receptor substrate Chico.

(UniProt, P09208)
Post Translational Modification

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 in response to exogenous insulin.

Phosphorylation of Tyr-1354 is required for Chico-binding.

(UniProt, P09208)
Linkouts
Sequences Consistent with the Gene Model
Mapped Features

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.

External Data
Crossreferences
Eukaryotic Promoter Database - A collection of databases of experimentally validated promoters for selected model organisms.
Linkouts
Expression Data
Expression Summary Ribbons
Colored tiles in ribbon indicate that expression data has been curated by FlyBase for that anatomical location. Colorless tiles indicate that there is no curated data for that location.
For complete stage-specific expression data, view the modENCODE Development RNA-Seq section under High-Throughput Expression below.
Transcript Expression
No Assay Recorded
Stage
Tissue/Position (including subcellular localization)
Reference
in situ
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data

Isoform-specific expression is observed from three different InR promoters, P1, P2, and P3.

Marker for
 
Subcellular Localization
CV Term
Polypeptide Expression
immunolocalization
Stage
Tissue/Position (including subcellular localization)
Reference
mass spectroscopy
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data

InR is specifically expressed in the fat body surrounding the brain but no expression is detected in the nervous system itself. InR protein is also expressed in the corpus allatum.

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.

Marker for
 
Subcellular Localization
CV Term
Evidence
References
Expression Deduced from Reporters
Reporter: TI{TI}InRV5.rLUC
Stage
Tissue/Position (including subcellular localization)
Reference
High-Throughput Expression Data
Associated Tools

GBrowse - Visual display of RNA-Seq signals

View Dmel\InR in GBrowse 2
RNA-Seq by Region - Search RNA-Seq expression levels by exon or genomic region
Reference
See Gelbart and Emmert, 2013 for analysis details and data files for all genes.
Developmental Proteome: Life Cycle
Developmental Proteome: Embryogenesis
External Data and Images
Linkouts
FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
Images
Alleles, Insertions, Transgenic Constructs, and Aberrations
Classical and Insertion Alleles ( 81 )
For All Classical and Insertion Alleles Show
 
Other relevant insertions
Transgenic Constructs ( 35 )
For All Alleles Carried on Transgenic Constructs Show
Transgenic constructs containing/affecting coding region of InR
Transgenic constructs containing regulatory region of InR
Aberrations (Deficiencies and Duplications) ( 20 )
Phenotypes
For more details about a specific phenotype click on the relevant allele symbol.
Lethality
Allele
Sterility
Allele
Other Phenotypes
Allele
Phenotype manifest in
Allele
photoreceptor cell & axon
photoreceptor cell & axon (with InR273)
photoreceptor cell & axon (with InR353)
Orthologs
Human Orthologs (via DIOPT v8.0)
Homo sapiens (Human) (4)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
12 of 15
Yes
Yes
10 of 15
No
Yes
1  
9 of 15
No
Yes
1 of 15
No
Yes
Model Organism Orthologs (via DIOPT v8.0)
Mus musculus (laboratory mouse) (4)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
12 of 15
Yes
Yes
10 of 15
No
Yes
8 of 15
No
Yes
1 of 15
No
Yes
Rattus norvegicus (Norway rat) (4)
10 of 13
Yes
Yes
7 of 13
No
Yes
6 of 13
No
Yes
1 of 13
No
Yes
Xenopus tropicalis (Western clawed frog) (3)
6 of 12
Yes
Yes
5 of 12
No
Yes
5 of 12
No
Yes
Danio rerio (Zebrafish) (5)
10 of 15
Yes
Yes
7 of 15
No
Yes
7 of 15
No
Yes
6 of 15
No
Yes
1 of 15
No
Yes
Caenorhabditis elegans (Nematode, roundworm) (2)
14 of 15
Yes
Yes
1 of 15
No
No
Arabidopsis thaliana (thale-cress) (33)
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
1 of 9
Yes
Yes
Saccharomyces cerevisiae (Brewer's yeast) (0)
No records found.
Schizosaccharomyces pombe (Fission yeast) (0)
No records found.
Ortholog(s) in Drosophila Species (via OrthoDB v9.1) ( EOG0919008C )
Organism
Common Name
Gene
AAA Syntenic Ortholog
Multiple Dmel Genes in this Orthologous Group
Drosophila suzukii
Spotted wing Drosophila
Drosophila simulans
Drosophila sechellia
Drosophila erecta
Drosophila yakuba
Drosophila ananassae
Drosophila pseudoobscura pseudoobscura
Drosophila persimilis
Drosophila willistoni
Drosophila virilis
Drosophila mojavensis
Drosophila grimshawi
Orthologs in non-Drosophila Dipterans (via OrthoDB v9.1) ( EOG091500Y9 )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Musca domestica
House fly
Musca domestica
House fly
Glossina morsitans
Tsetse fly
Glossina morsitans
Tsetse fly
Lucilia cuprina
Australian sheep blowfly
Mayetiola destructor
Hessian fly
Mayetiola destructor
Hessian fly
Aedes aegypti
Yellow fever mosquito
Aedes aegypti
Yellow fever mosquito
Anopheles darlingi
American malaria mosquito
Anopheles darlingi
American malaria mosquito
Anopheles gambiae
Malaria mosquito
Anopheles gambiae
Malaria mosquito
Culex quinquefasciatus
Southern house mosquito
Orthologs in non-Dipteran Insects (via OrthoDB v9.1) ( EOG090W00AX )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Bombyx mori
Silkmoth
Danaus plexippus
Monarch butterfly
Heliconius melpomene
Postman butterfly
Apis florea
Little honeybee
Apis florea
Little honeybee
Apis florea
Little honeybee
Apis mellifera
Western honey bee
Apis mellifera
Western honey bee
Bombus impatiens
Common eastern bumble bee
Bombus impatiens
Common eastern bumble bee
Bombus terrestris
Buff-tailed bumblebee
Bombus terrestris
Buff-tailed bumblebee
Linepithema humile
Argentine ant
Linepithema humile
Argentine ant
Megachile rotundata
Alfalfa leafcutting bee
Megachile rotundata
Alfalfa leafcutting bee
Nasonia vitripennis
Parasitic wasp
Dendroctonus ponderosae
Mountain pine beetle
Tribolium castaneum
Red flour beetle
Pediculus humanus
Human body louse
Cimex lectularius
Bed bug
Acyrthosiphon pisum
Pea aphid
Acyrthosiphon pisum
Pea aphid
Zootermopsis nevadensis
Nevada dampwood termite
Zootermopsis nevadensis
Nevada dampwood termite
Orthologs in non-Insect Arthropods (via OrthoDB v9.1) ( EOG090X00AD )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Strigamia maritima
European centipede
Ixodes scapularis
Black-legged tick
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Tetranychus urticae
Two-spotted spider mite
Tetranychus urticae
Two-spotted spider mite
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Daphnia pulex
Water flea
Orthologs in non-Arthropod Metazoa (via OrthoDB v9.1) ( None identified )
No non-Arthropod Metazoa orthologies identified
Paralogs
Paralogs (via DIOPT v8.0)
Drosophila melanogaster (Fruit fly) (20)
5 of 10
3 of 10
2 of 10
2 of 10
2 of 10
2 of 10
2 of 10
2 of 10
2 of 10
2 of 10
2 of 10
2 of 10
2 of 10
2 of 10
2 of 10
2 of 10
2 of 10
2 of 10
1 of 10
1 of 10
Human Disease Associations
FlyBase Human Disease Model Reports
Disease Model Summary Ribbon
Disease Ontology (DO) Annotations
Models Based on Experimental Evidence ( 6 )
Potential Models Based on Orthology ( 2 )
Human Ortholog
Disease
Evidence
References
Modifiers Based on Experimental Evidence ( 7 )
Disease Associations of Human Orthologs (via DIOPT v8.0 and OMIM)
Note that ortholog calls supported by only 1 or 2 algorithms (DIOPT score < 3) are not shown.
Functional Complementation Data
Functional complementation data is computed by FlyBase using a combination of the orthology data obtained from DIOPT and OrthoDB and the allele-level genetic interaction data curated from the literature.
Interactions
Summary of Physical Interactions
esyN Network Diagram
Show neighbor-neighbor interactions:
Select Layout:
Legend:
Protein
RNA
Selected Interactor(s)
Interactions Browser

Please see the Physical Interaction reports below for full details
protein-protein
Physical Interaction
Assay
References
RNA-protein
Physical Interaction
Assay
References
Summary of Genetic Interactions
esyN Network Diagram
esyN Network Key:
Suppression
Enhancement

Please look at the allele data for full details of the genetic interactions
Starting gene(s)
Interaction type
Interacting gene(s)
Reference
suppressible
Starting gene(s)
Interaction type
Interacting gene(s)
Reference
External Data
Subunit Structure (UniProtKB)
Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains contribute to the formation of the ligand-binding domain, while the beta chains carry the kinase domain. When autophosphorylated, the beta-subunit binds the SH2 and SH3 domains of the adapter protein Dock. The beta subunit also binds and tyrosine phosphorylates the insulin receptor substrate Chico.
(UniProt, P09208 )
Linkouts
BioGRID - A database of protein and genetic interactions.
InterologFinder - Protein-protein interactions (PPI) from both known and predicted PPI data sets.
MIST (genetic) - An integrated Molecular Interaction Database
MIST (protein-protein) - An integrated Molecular Interaction Database
Pathways
Signaling Pathways (FlyBase)
Insulin-like Receptor Signaling Pathway Core Components -
The Insulin-like Receptor (IR) signaling pathway in Drosophila is initiated by the binding of an insulin-like peptides to the Insulin-like receptor (InR). (Adapted from FBrf0232297, FBrf0230017 and FBrf0229989.)
Metabolic Pathways
External Data
Linkouts
Reactome - An open-source, open access, manually curated and peer-reviewed pathway database.
Genomic Location and Detailed Mapping Data
Chromosome (arm)
3R
Recombination map
3-72
Cytogenetic map
Sequence location
3R:21,570,248..21,619,321 [-]
FlyBase Computed Cytological Location
Cytogenetic map
Evidence for location
93E4-93E9
Experimentally Determined Cytological Location
Cytogenetic map
Notes
References
93E4-93E5
(determined by in situ hybridisation)
93E1-93E3
(determined by in situ hybridisation)
93E-93E
(determined by in situ hybridisation)
Experimentally Determined Recombination Data
Left of (cM)
Right of (cM)
Notes
Stocks and Reagents
Stocks (54)
Genomic Clones (36)
cDNA Clones (32)
 

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.

cDNA clones, fully sequenced
BDGP DGC clones
Other clones
    Drosophila Genomics Resource Center cDNA clones

    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.

    cDNA Clones, End Sequenced (ESTs)
    BDGP DGC clones
    RNAi and Array Information
    Linkouts
    GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
    Antibody Information
    Laboratory Generated Antibodies
     
    Commercially Available Antibodies
     
    Other Information
    Relationship to Other Genes
    Source for database identify of
    Source for database merge of

    Source for merge of: InR l(3)93Dj

    Source for merge of: InR sprout

    Additional comments
    Other Comments

    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 is required for photoreceptor cell axons to find their way from the retina to the brain during development of the visual system. This function is independent of chico.

    InR autonomously controls cell and organ size.

    The InR gene product functions downstream of peb in the germ band.

    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 is synthesized from a higher molecular weight precursor. Processed InR is an oligomer consisting of insulin binding subunits (α) and protein tyrosine kinase subunits (β).

    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.

    Origin and Etymology
    Discoverer
    Etymology
    Identification
    External Crossreferences and Linkouts ( 62 )
    Sequence Crossreferences
    NCBI Gene - Gene integrates information from a wide range of species. A record may include nomenclature, Reference Sequences (RefSeqs), maps, pathways, variations, phenotypes, and links to genome-, phenotype-, and locus-specific resources worldwide.
    GenBank Nucleotide - A collection of sequences from several sources, including GenBank, RefSeq, TPA, and PDB.
    GenBank Protein - A collection of sequences from several sources, including translations from annotated coding regions in GenBank, RefSeq and TPA, as well as records from SwissProt, PIR, PRF, and PDB.
    RefSeq - A comprehensive, integrated, non-redundant, well-annotated set of reference sequences including genomic, transcript, and protein.
    UniProt/Swiss-Prot - Manually annotated and reviewed records of protein sequence and functional information
    Other crossreferences
    Linkouts
    BioGRID - A database of protein and genetic interactions.
    FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
    Interactive Fly - A cyberspace guide to Drosophila development and metazoan evolution
    InterologFinder - Protein-protein interactions (PPI) from both known and predicted PPI data sets.
    MIST (genetic) - An integrated Molecular Interaction Database
    MIST (protein-protein) - An integrated Molecular Interaction Database
    Reactome - An open-source, open access, manually curated and peer-reviewed pathway database.
    Synonyms and Secondary IDs (55)
    Reported As
    Symbol Synonym
    Dir-a
    Dir-b
    InR
    (Kim and O'Connor, 2021, Álvarez-Rendón and Riesgo-Escovar, 2020, Bakshi and Joshi, 2020, Ceder et al., 2020, Eschment et al., 2020, Flatt, 2020, Ghosh et al., 2020, Ingaramo et al., 2020, Koliada et al., 2020, Koyama et al., 2020, Kwon et al., 2020, Lathen et al., 2020, Lin and Hsu, 2020, Luo et al., 2020, Ma et al., 2020, Manière et al., 2020, Nakamura et al., 2020, Neamtu et al., 2020, Newell et al., 2020, Nye et al., 2020, P et al., 2020, Rambur et al., 2020, Rani et al., 2020, Rust et al., 2020, Sanaki et al., 2020, Sênos Demarco et al., 2020, Sheard et al., 2020, Slankster et al., 2020, Strilbytska et al., 2020, Tang et al., 2020, Texada et al., 2020, Vega-Cuesta et al., 2020, Yuan et al., 2020, Yu et al., 2020, Zeng et al., 2020, Zhang et al., 2020, Ahlers et al., 2019, Bayliak et al., 2019, Birnbaum et al., 2019, Borreguero-Muñoz et al., 2019, Chakraborty et al., 2019, Chen and Read, 2019, Courgeon and Desplan, 2019, Dong et al., 2019, Dreyer and Shingleton, 2019, Durmaz et al., 2019, Evangelakou et al., 2019, Galenza and Foley, 2019, Gervais et al., 2019, Gumeni et al., 2019, Huang et al., 2019, Hudry et al., 2019, Hunt et al., 2019, Krittika and Yadav, 2019, Lang et al., 2019, Lehmann et al., 2019, Lenaerts et al., 2019, Lushchak et al., 2019, Manola et al., 2019, Mele and Johnson, 2019, Meltzer et al., 2019, Michalak et al., 2019, Mirth et al., 2019, Nikou et al., 2019, Pahl et al., 2019, Post et al., 2019, Raj and Sarkar, 2019, Raza et al., 2019, Scopelliti et al., 2019, Shinoda et al., 2019, Texada et al., 2019, Tozluoǧlu et al., 2019, Westfall et al., 2019, Westfall et al., 2019, Xu et al., 2019, Yoshinari et al., 2019, Zhang et al., 2019, Zheng et al., 2019, Álvarez-Rendón et al., 2018, Augustin et al., 2018, Ayala et al., 2018, Chaichanit et al., 2018, Clemson et al., 2018, Das et al., 2018, Funakoshi et al., 2018, Gáliková and Klepsatel, 2018, Henstridge et al., 2018, Ignesti et al., 2018, Im et al., 2018, Jung et al., 2018, Kang et al., 2018, Lehmann, 2018, Liu et al., 2018, Mattila et al., 2018, Merigliano et al., 2018, Musselman et al., 2018, Neuman and Bashirullah, 2018, Obata et al., 2018, Rossi and Fernandes, 2018, Setiawan et al., 2018, Sharma et al., 2018, Spéder and Brand, 2018, Tang et al., 2018, Tsai et al., 2018, Westfall et al., 2018, Augustin et al., 2017, Banerjee et al., 2017, Bolukbasi et al., 2017, Ecker et al., 2017, Fedina et al., 2017, Gerdøe-Kristensen et al., 2017, Hevia et al., 2017, Hoedjes et al., 2017, Hughes and Leips, 2017, Kang et al., 2017, Kashio et al., 2017, Lee et al., 2017, Liao et al., 2017, Li et al., 2017, Liu and Jin, 2017, Liu et al., 2017, Liu et al., 2017, Luhur et al., 2017, Moeller et al., 2017, Monyak et al., 2017, Murillo-Maldonado and Riesgo-Escovar, 2017, Neuert et al., 2017, Park et al., 2017, Song et al., 2017, Sun et al., 2017, Transgenic RNAi Project members, 2017-, Willoughby et al., 2017, Xiang et al., 2017, Zhu et al., 2017, Agrawal et al., 2016, Alfa and Kim, 2016, Ashton-Beaucage et al., 2016, Barry and Thummel, 2016, Bonfini et al., 2016, Brill et al., 2016, Cao et al., 2016, Clandinin and Owens, 2016-, Crocker et al., 2016, Danielsen et al., 2016, Di Cara and King-Jones, 2016, Dobson et al., 2016, Hirabayashi, 2016, Jiang et al., 2016, Jun et al., 2016, Kakanj et al., 2016, Kashio et al., 2016, Kaynar et al., 2016, Kuleesha et al., 2016, Mahoney et al., 2016, Maistrenko et al., 2016, Marmor-Kollet and Schuldiner, 2016, Musashe et al., 2016, Niwa and Niwa, 2016, Padash Barmchi et al., 2016, Sieber et al., 2016, Strigini and Leulier, 2016, Vinayagam et al., 2016, Wang et al., 2016, Wang et al., 2016, Wiemerslage et al., 2016, Williams et al., 2016, Woods et al., 2016, Wu and Storey, 2016, Yadav et al., 2016, Yaniv and Schuldiner, 2016, Zhan et al., 2016, Acevedo et al., 2015, Adrion et al., 2015, Aldrich and Maggert, 2015, Andreenkova et al., 2015, Andreenkova et al., 2015, Aradhya et al., 2015, Aradska et al., 2015, Balakrishnan et al., 2015, Bennett et al., 2015, Burn et al., 2015, Chambers et al., 2015, Chen et al., 2015, Das and Dobens, 2015, Fear et al., 2015, Garelli et al., 2015, Ghabrial, 2015.8.26, Gilboa, 2015, Grotewiel and Bettinger, 2015, Hall and Verheyen, 2015, Hsu et al., 2015, Ismail et al., 2015, Jia et al., 2015, Katzenberger et al., 2015, Kwon et al., 2015, Lebreton et al., 2015, Liu et al., 2015, Matsuda et al., 2015, Nie et al., 2015, Obata and Miura, 2015, Parker and Struhl, 2015, Schmitt et al., 2015, Sopko et al., 2015, Wang et al., 2015, Wang et al., 2015, Wei et al., 2015, Xie et al., 2015, Yan et al., 2015, Ashwal-Fluss et al., 2014, Bulat et al., 2014, Charroux and Royet, 2014, Chatterjee et al., 2014, Ghosh et al., 2014, Gündner et al., 2014, Guo et al., 2014, Homem et al., 2014, Ikmi et al., 2014, Kux and Pitsouli, 2014, Lam et al., 2014, Lanet and Maurange, 2014, Lee et al., 2014, Macagno et al., 2014, Mulakkal et al., 2014, Oliveira et al., 2014, Owusu-Ansah and Perrimon, 2014, Park et al., 2014, Radermacher et al., 2014, Radermacher et al., 2014, Rauschenbach et al., 2014, Rauschenbach et al., 2014, Ruiz et al., 2014, Sato-Miyata et al., 2014, Song et al., 2014, Sopko et al., 2014, Tchankouo-Nguetcheu et al., 2014, Truscott et al., 2014, Wang et al., 2014, Wang et al., 2014, Wong et al., 2014, Xu and Cherry, 2014, Almudi et al., 2013, Andersen et al., 2013, Ayyaz and Jasper, 2013, Bader et al., 2013, Buszard et al., 2013, Erion and Sehgal, 2013, Hahn et al., 2013, Hartman et al., 2013, Hirabayashi et al., 2013, Hyun, 2013, Itskov and Ribeiro, 2013, Karpac et al., 2013, Kayashima et al., 2013, Koyama et al., 2013, Lin et al., 2013, Neckameyer and Argue, 2013, Nowak et al., 2013, O'Farrell et al., 2013, Okamoto et al., 2013, Ozkan et al., 2013, Rauschenbach et al., 2013, Rera et al., 2013, Shim et al., 2013, Shingleton and Frankino, 2013, Sopko and Perrimon, 2013, Tamori and Deng, 2013, Tixier et al., 2013, Tixier et al., 2013, Walker et al., 2013, Wong et al., 2013, Yamanaka et al., 2013, Adamson and Lajeunesse, 2012, Avet-Rochex et al., 2012, Bolukbasi et al., 2012, Chakrabarti et al., 2012, Green and Extavour, 2012, Gurudatta et al., 2012, Hariharan, 2012, Hazelett et al., 2012, Homem and Knoblich, 2012, Hong et al., 2012, Jin et al., 2012, Kapuria et al., 2012, Kaun et al., 2012, Kayashima et al., 2012, Korenjak et al., 2012, Kuo et al., 2012, Lv et al., 2012, Mirth and Shingleton, 2012, Noebels et al., 2012, Papatheodorou et al., 2012, Pritchett and McCall, 2012, Rera et al., 2012, Tokusumi et al., 2012, Wang et al., 2012, Wang et al., 2012, Abruzzi et al., 2011, Apidianakis and Rahme, 2011, Bangi et al., 2011, Friedman et al., 2011, Friedman et al., 2011, Friedman et al., 2011, Glatter et al., 2011, Kamakura, 2011, Karpac et al., 2011, Klusza and Deng, 2011, Ling and Salvaterra, 2011, Liu et al., 2011, Luo et al., 2011, McClure et al., 2011, Murillo-Maldonado et al., 2011, Murillo-Maldonado et al., 2011, Parker, 2011, Powis and Macdougall, 2011, Ruaud et al., 2011, Schachter and Boulianne, 2011, Slack et al., 2011, Storelli et al., 2011, Tang et al., 2011, Wigby et al., 2011, Willecke et al., 2011, Zhang et al., 2011, Ables and Drummond-Barbosa, 2010, Ashton-Beaucage et al., 2010, Biteau et al., 2010, Chang and Neufeld, 2010, Chi et al., 2010, Djiane and Mlodzik, 2010, Kim et al., 2010, Kockel et al., 2010, Kühnlein, 2010, LaFever et al., 2010, Lee et al., 2010, Lee et al., 2010, Maynard et al., 2010, Paaby et al., 2010, Portela et al., 2010, Ribeiro and Dickson, 2010, Sabin et al., 2010, Siegrist et al., 2010, Tsuda et al., 2010, Xiang et al., 2010, Amcheslavsky et al., 2009, Demontis and Perrimon, 2009, Dworkin et al., 2009, Grandison et al., 2009, Guirao-Rico and Aguadé, 2009, Hull-Thompson et al., 2009, Kent et al., 2009, Lee et al., 2009, Mirth et al., 2009, Nuzhdin et al., 2009, Parrish et al., 2009, Qian and Bodmer, 2009, Schiess et al., 2009, Sims et al., 2009, Slaidina et al., 2009, Ueishi et al., 2009, Vigne et al., 2009, Werz et al., 2009, Witte et al., 2009, Yu et al., 2009, Carrera et al., 2008, Christensen et al., 2008.12.28, Christensen et al., 2008.12.28, Honegger et al., 2008, Krishnamoorthy, 2008, Lee et al., 2008, Paaby et al., 2008, Stofanko et al., 2008, Wang et al., 2008, Xu et al., 2008, Yu et al., 2008, Zhao et al., 2008, Ahrens et al., 2007, Belgacem and Martin, 2007, Casas-Tinto et al., 2007, Hoshizaki and Gibbs, 2007, Hsu et al., 2007, Lingo et al., 2007, Luo et al., 2007, Ocorr et al., 2007, Shcherbata et al., 2007, Shcherbata et al., 2007, Tountas and Fortini, 2007, Tseng et al., 2007, Zheng et al., 2007, Belgacem and Martin, 2006, Edgar, 2006, Friedman and Perrimon, 2006, Fuss et al., 2006, Manak et al., 2006, Martin-Pena et al., 2006, Bateman and McNeill, 2005, Coffman et al., 2005, Corl et al., 2005, Flatt et al., 2005, Goberdhan et al., 2005, Mikeladze-Dvali et al., 2005, Schmidt et al., 2005, Shingleton et al., 2005, Geiger-Thornsberry and Mackay, 2004, Hofmann et al., 2004, Tu and Tatar, 2003, Tu et al., 2002, Pickeral et al., 2000)
    Inr-α
    Inr-β
    insulin/insulin-like growth factor receptor
    l(3)93Dj
    l(3)er10
    Name Synonyms
    Drosophila Insulin Receptor
    Drosophila insulin receptor
    Insulin-receptor
    insulin receptor homologue
    insulin-like receptor tyrosine kinase
    insulin-receptor
    insulin/IGF receptor
    lethal(3)93Dj
    Secondary FlyBase IDs
    • FBgn0013984
    • FBgn0000456
    • FBgn0000457
    • FBgn0002393
    • FBgn0010868
    • FBgn0264663
    Datasets (1)
    Study focus (1)
    Experimental Role
    Project
    Project Type
    Title
    • bait_protein
    Interaction map generated by purification of receptor tyrosine kinase pathway factors, with identification of copurifying proteins by mass spectrometry.
    References (858)