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Protein

Insulin-like receptor

Gene

InR

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.6 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Cofactori

Mn2+By similarity

Enzyme regulationi

Autophosphorylation activates the kinase activity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1405 – 14051ATPPROSITE-ProRule annotation
Active sitei1519 – 15191Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1377 – 13859ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: FlyBase
  • identical protein binding Source: IntAct
  • insulin-activated receptor activity Source: FlyBase
  • insulin binding Source: UniProtKB
  • insulin-like growth factor binding Source: FlyBase
  • insulin receptor substrate binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • phosphatidylinositol 3-kinase binding Source: UniProtKB
  • protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  • aging Source: FlyBase
  • axon guidance Source: UniProtKB
  • carbohydrate metabolic process Source: FlyBase
  • cell growth Source: FlyBase
  • cellular response to DNA damage stimulus Source: FlyBase
  • circadian rhythm Source: FlyBase
  • determination of adult lifespan Source: UniProtKB
  • developmental growth Source: FlyBase
  • dorsal closure Source: FlyBase
  • embryo development Source: UniProtKB
  • embryonic development via the syncytial blastoderm Source: FlyBase
  • female germ-line stem cell asymmetric division Source: FlyBase
  • female gonad development Source: FlyBase
  • female mating behavior Source: FlyBase
  • germ-band shortening Source: FlyBase
  • germ-line stem-cell niche homeostasis Source: FlyBase
  • growth Source: FlyBase
  • imaginal disc growth Source: FlyBase
  • insulin receptor signaling pathway Source: FlyBase
  • intestinal stem cell homeostasis Source: FlyBase
  • lipid metabolic process Source: FlyBase
  • locomotory behavior Source: FlyBase
  • male germ-line stem cell asymmetric division Source: FlyBase
  • multicellular organism growth Source: FlyBase
  • myoblast fusion Source: FlyBase
  • negative regulation of autophagy Source: FlyBase
  • negative regulation of circadian sleep/wake cycle, sleep Source: FlyBase
  • negative regulation of feeding behavior Source: FlyBase
  • negative regulation of peptide hormone secretion Source: FlyBase
  • nervous system development Source: UniProtKB
  • neuron remodeling Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • peptidyl-tyrosine phosphorylation Source: GOC
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of cell size Source: FlyBase
  • positive regulation of multicellular organism growth Source: UniProtKB
  • positive regulation of organ growth Source: UniProtKB
  • primary spermatocyte growth Source: FlyBase
  • protein autophosphorylation Source: UniProtKB
  • protein heterotetramerization Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of cell proliferation Source: FlyBase
  • regulation of cell size Source: FlyBase
  • regulation of glucose metabolic process Source: FlyBase
  • regulation of multicellular organism growth Source: FlyBase
  • regulation of organ growth Source: FlyBase
  • regulation of reactive oxygen species metabolic process Source: FlyBase
  • response to anoxia Source: FlyBase
  • response to cocaine Source: FlyBase
  • response to nutrient Source: FlyBase
  • response to oxidative stress Source: FlyBase
  • somatic muscle development Source: FlyBase
  • trachea morphogenesis Source: FlyBase
  • vitellogenesis Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Differentiation, Growth regulation, Neurogenesis

Keywords - Ligandi

ATP-binding, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 1994.
ReactomeiR-DME-77387. Insulin receptor recycling.
SignaLinkiP09208.

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin-like receptor (EC:2.7.10.1)
Short name:
dIR
Short name:
dInr
Alternative name(s):
dIRH
Cleaved into the following 3 chains:
Gene namesi
Name:InR
Synonyms:dinr, Dir-a, Inr-a
ORF Names:CG18402
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0283499. InR.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1086 – 1310225ExtracellularSequence analysisAdd
BLAST
Transmembranei1311 – 133121HelicalSequence analysisAdd
BLAST
Topological domaini1332 – 2144813CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell-cell junction Source: FlyBase
  • insulin receptor complex Source: FlyBase
  • integral component of plasma membrane Source: FlyBase
  • plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1467 – 14671R → C in allele 353; reduction in head size. 1 Publication
Mutagenesisi1539 – 15391G → E in allele 339; strong reduction in head size. 1 Publication
Mutagenesisi1599 – 15991G → R in allele 211; reduction in head size. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 2144Insulin-like receptorPRO_0000016718
Signal peptidei1 – ?Sequence analysis
Chaini651 – 1081431Insulin-like receptor subunit alphaPRO_0000016715Add
BLAST
Chaini1086 – 21441059Insulin-like receptor subunit beta 1PRO_0000016716Add
BLAST
Chaini1086 – ?Insulin-like receptor subunit beta 2PRO_0000016717

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi74 – 741N-linked (GlcNAc...)Sequence analysis
Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence analysis
Glycosylationi265 – 2651N-linked (GlcNAc...)Sequence analysis
Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence analysis
Glycosylationi376 – 3761N-linked (GlcNAc...)Sequence analysis
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence analysis
Glycosylationi468 – 4681N-linked (GlcNAc...)Sequence analysis
Glycosylationi509 – 5091N-linked (GlcNAc...)Sequence analysis
Disulfide bondi531 ↔ 539By similarity
Disulfide bondi535 ↔ 545By similarity
Disulfide bondi546 ↔ 554By similarity
Disulfide bondi550 ↔ 564By similarity
Glycosylationi561 – 5611N-linked (GlcNAc...)Sequence analysis
Disulfide bondi567 ↔ 576By similarity
Glycosylationi569 – 5691N-linked (GlcNAc...)Sequence analysis
Disulfide bondi580 ↔ 591By similarity
Disulfide bondi597 ↔ 618By similarity
Disulfide bondi635 ↔ 638By similarity
Glycosylationi751 – 7511N-linked (GlcNAc...)Sequence analysis
Glycosylationi810 – 8101N-linked (GlcNAc...)Sequence analysis
Glycosylationi824 – 8241N-linked (GlcNAc...)1 Publication
Glycosylationi839 – 8391N-linked (GlcNAc...)1 Publication
Glycosylationi864 – 8641N-linked (GlcNAc...)1 Publication
Glycosylationi898 – 8981N-linked (GlcNAc...)1 Publication
Glycosylationi946 – 9461N-linked (GlcNAc...)Sequence analysis
Glycosylationi1053 – 10531N-linked (GlcNAc...)Sequence analysis
Glycosylationi1147 – 11471N-linked (GlcNAc...)1 Publication
Glycosylationi1218 – 12181N-linked (GlcNAc...)1 Publication
Glycosylationi1219 – 12191N-linked (GlcNAc...); atypical1 Publication
Glycosylationi1265 – 12651N-linked (GlcNAc...)Sequence analysis
Modified residuei1354 – 13541Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1545 – 15451Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1549 – 15491Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1550 – 15501Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1816 – 18161Phosphoserine1 Publication

Post-translational modificationi

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.1 Publication
Autophosphorylated on tyrosine residues in response to exogenous insulin.1 Publication
Phosphorylation of Tyr-1354 is required for Chico-binding.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP09208.

PTM databases

iPTMnetiP09208.

Expressioni

Tissue specificityi

Widely distributed throughout the embryo. Expressed at high levels in the embryonic nervous system. Larval expression is limited to the nervous system and all imaginal disks. Expressed at high levels in the adult nervous system and ovaries.2 Publications

Developmental stagei

Expressed throughout development. Embryonic expression is most prominent 8 to 12 hours after egg laying.2 Publications

Gene expression databases

BgeeiP09208.
ExpressionAtlasiP09208. differential.
GenevisibleiP09208. DM.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-92063,EBI-92063
chicoQ9XTN23EBI-92063,EBI-176370

GO - Molecular functioni

Protein-protein interaction databases

BioGridi67515. 12 interactions.
IntActiP09208. 5 interactions.
STRINGi7227.FBpp0288669.

Structurei

3D structure databases

ProteinModelPortaliP09208.
SMRiP09208. Positions 1361-1668.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini825 – 927103Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini928 – 102699Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini1210 – 130596Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini1371 – 1659289Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1351 – 13544Chico-bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi176 – 25277Gln-richAdd
BLAST
Compositional biasi177 – 19721His-richAdd
BLAST
Compositional biasi521 – 58060Cys-richAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation
Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3-binding, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4258. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118818.
InParanoidiP09208.
KOiK05087.
OMAiKDPRAFI.
OrthoDBiEOG7B31KZ.
PhylomeDBiP09208.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProiIPR003961. FN3_dom.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PfamiPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 3 hits.
SSF52058. SSF52058. 2 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS50853. FN3. 3 hits.
PS01352. HEMATOPO_REC_L_F1. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09208-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFNMPRGVTK SKSKRGKIKM ENDMAAAATT TACTLGHICV LCRQEMLLDT
60 70 80 90 100
CCCRQAVEAV DSPASSEEAY SSSNSSSCQA SSEISAEEVW FLSHDDIVLC
110 120 130 140 150
RRPKFDEVET TGKKRDVKCS GHQCSNECDD GSTKNNRQQR ENFNIFSNCH
160 170 180 190 200
NILRTLQSLL LLMFNCGIFN KRRRRQHQQQ HHHHYQHHHQ QHHQQHHQRQ
210 220 230 240 250
QANVSYTKFL LLLQTLAAAT TRLSLSPKNY KQQQQLQHNQ QLPRATPQQK
260 270 280 290 300
QQEKDRHKCF HYKHNYSYSP GISLLLFILL ANTLAIQAVV LPAHQQHLLH
310 320 330 340 350
NDIADGLDKT ALSVSGTQSR WTRSESNPTM RLSQNVKPCK SMDIRNMVSH
360 370 380 390 400
FNQLENCTVI EGFLLIDLIN DASPLNRSFP KLTEVTDYII IYRVTGLHSL
410 420 430 440 450
SKIFPNLSVI RGNKLFDGYA LVVYSNFDLM DLGLHKLRSI TRGGVRIEKN
460 470 480 490 500
HKLCYDRTID WLEILAENET QLVVLTENGK EKECRLSKCP GEIRIEEGHD
510 520 530 540 550
TTAIEGELNA SCQLHNNRRL CWNSKLCQTK CPEKCRNNCI DEHTCCSQDC
560 570 580 590 600
LGGCVIDKNG NESCISCRNV SFNNICMDSC PKGYYQFDSR CVTANECITL
610 620 630 640 650
TKFETNSVYS GIPYNGQCIT HCPTGYQKSE NKRMCEPCPG GKCDKECSSG
660 670 680 690 700
LIDSLERARE FHGCTIITGT EPLTISIKRE SGAHVMDELK YGLAAVHKIQ
710 720 730 740 750
SSLMVHLTYG LKSLKFFQSL TEISGDPPMD ADKYALYVLD NRDLDELWGP
760 770 780 790 800
NQTVFIRKGG VFFHFNPKLC VSTINQLLPM LASKPKFFEK SDVGADSNGN
810 820 830 840 850
RGSCGTAVLN VTLQSVGANS AMLNVTTKVE IGEPQKPSNA TIVFKDPRAF
860 870 880 890 900
IGFVFYHMID PYGNSTKSSD DPCDDRWKVS SPEKSGVMVL SNLIPYTNYS
910 920 930 940 950
YYVRTMAISS ELTNAESDVK NFRTNPGRPS KVTEVVATAI SDSKINVTWS
960 970 980 990 1000
YLDKPYGVLT RYFIKAKLIN RPTRNNNRDY CTEPLVKAME NDLPATTPTK
1010 1020 1030 1040 1050
KISDPLAGDC KCVEGSKKTS SQEYDDRKVQ AGMEFENALQ NFIFVPNIRK
1060 1070 1080 1090 1100
SKNGSSDKSD GAEGAALDSN AIPNGGATNP SRRRRDVALE PELDDVEGSV
1110 1120 1130 1140 1150
LLRHVRSITD DTDAFFEKDD ENTYKDEEDL SSNKQFYEVF AKELPPNQTH
1160 1170 1180 1190 1200
FVFEKLRHFT RYAIFVVACR EEIPSEKLRD TSFKKSLCSD YDTVFQTTKR
1210 1220 1230 1240 1250
KKFADIVMDL KVDLEHANNT ESPVRVRWTP PVDPNGEIVT YEVAYKLQKP
1260 1270 1280 1290 1300
DQVEEKKCIP AADFNQTAGY LIKLNEGLYS FRVRANSIAG YGDFTEVEHI
1310 1320 1330 1340 1350
KVEPPPSYAK VFFWLLGIGL AFLIVSLFGY VCYLHKRKVP SNDLHMNTEV
1360 1370 1380 1390 1400
NPFYASMQYI PDDWEVLREN IIQLAPLGQG SFGMVYEGIL KSFPPNGVDR
1410 1420 1430 1440 1450
ECAIKTVNEN ATDRERTNFL SEASVMKEFD TYHVVRLLGV CSRGQPALVV
1460 1470 1480 1490 1500
MELMKKGDLK SYLRAHRPEE RDEAMMTYLN RIGVTGNVQP PTYGRIYQMA
1510 1520 1530 1540 1550
IEIADGMAYL AAKKFVHRDL AARNCMVADD LTVKIGDFGM TRDIYETDYY
1560 1570 1580 1590 1600
RKGTKGLLPV RWMPPESLRD GVYSSASDVF SFGVVLWEMA TLAAQPYQGL
1610 1620 1630 1640 1650
SNEQVLRYVI DGGVMERPEN CPDFLHKLMQ RCWHHRSSAR PSFLDIIAYL
1660 1670 1680 1690 1700
EPQCPNSQFK EVSFYHSEAG LQHREKERKE RNQLDAFAAV PLDQDLQDRE
1710 1720 1730 1740 1750
QQEDATTPLR MGDYQQNSSL DQPPESPIAM VDDQGSHLPF SLPSGFIASS
1760 1770 1780 1790 1800
TPDGQTVMAT AFQNIPAAQG DISATYVVPD ADALDGDRGY EIYDPSPKCA
1810 1820 1830 1840 1850
ELPTSRSGST GGGKLSGEQH LLPRKGRQPT IMSSSMPDDV IGGSSLQPST
1860 1870 1880 1890 1900
ASAGSSNASS HTGRPSLKKT VADSVRNKAN FINRHLFNHK RTGSNASHKS
1910 1920 1930 1940 1950
NASNAPSTSS NTNLTSHPVA MGNLGTIESG GSGSAGSYTG TPRFYTPSAT
1960 1970 1980 1990 2000
PGGGSGMAIS DNPNYRLLDE SIASEQATIL TTSSPNPNYE MMHPPTSLVS
2010 2020 2030 2040 2050
TNPNYMPMNE TPVQMAGVTI SHNPNYQPMQ APLNARQSQS SSDEDNEQEE
2060 2070 2080 2090 2100
DDEDEDDDVD DEHVEHIKME RMPLSRPRQR ALPSKTQPPR SRSVSQTRKS
2110 2120 2130 2140
PTNPNSGIGA TGAGNRSNLL KENWLRPAST PRPPPPNGFI GREA
Length:2,144
Mass (Da):239,776
Last modified:March 29, 2005 - v3
Checksum:iC4A8ECB08C70523A
GO

Sequence cautioni

The sequence AAA28644.1 differs from that shown. Reason: Frameshift at position 1753. Curated
The sequence AAA68953.1 differs from that shown. Reason: Frameshift at positions 864, 877 and 2095. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291T → ATTAK in AAC47458 (PubMed:7876183).Curated
Sequence conflicti89 – 891V → D in AAA68953 (PubMed:7628438).Curated
Sequence conflicti157 – 1571Q → H in AAA68953 (PubMed:7628438).Curated
Sequence conflicti157 – 1571Q → H in AAC47458 (PubMed:7876183).Curated
Sequence conflicti164 – 1641F → C in AAA68953 (PubMed:7628438).Curated
Sequence conflicti197 – 1971H → L in AAA68953 (PubMed:7628438).Curated
Sequence conflicti197 – 1971H → L in AAC47458 (PubMed:7876183).Curated
Sequence conflicti319 – 3191S → T in AAA68953 (PubMed:7628438).Curated
Sequence conflicti319 – 3191S → T in AAC47458 (PubMed:7876183).Curated
Sequence conflicti322 – 3221T → P in AAA68953 (PubMed:7628438).Curated
Sequence conflicti322 – 3221T → P in AAC47458 (PubMed:7876183).Curated
Sequence conflicti470 – 4701T → S in AAA68953 (PubMed:7628438).Curated
Sequence conflicti485 – 4851R → S in AAA68953 (PubMed:7628438).Curated
Sequence conflicti501 – 5011T → N in AAA68953 (PubMed:7628438).Curated
Sequence conflicti501 – 5011T → N in AAC47458 (PubMed:7876183).Curated
Sequence conflicti653 – 6608DSLERARE → PPPPPPPL in AAA28644 (PubMed:3099787).Curated
Sequence conflicti679 – 6813RES → GER in AAA28644 (PubMed:3099787).Curated
Sequence conflicti723 – 7275ISGDP → LAAI in AAA28644 (PubMed:3099787).Curated
Sequence conflicti793 – 7931V → E in AAA68953 (PubMed:7628438).Curated
Sequence conflicti822 – 8221M → S in AAA68953 (PubMed:7628438).Curated
Sequence conflicti864 – 87714NSTKS…CDDRW → TQLKAVTIHAMIAG in AAA28644 (PubMed:3099787).CuratedAdd
BLAST
Sequence conflicti933 – 9353Missing in AAA68953 (PubMed:7628438).Curated
Sequence conflicti933 – 9353Missing in AAA28644 (PubMed:3099787).Curated
Sequence conflicti954 – 9585KPYGV → NLMA in AAA68953 (PubMed:7628438).Curated
Sequence conflicti954 – 9585KPYGV → NLMA in AAA28644 (PubMed:3099787).Curated
Sequence conflicti1161 – 11611Missing in AAA28644 (PubMed:3099787).Curated
Sequence conflicti1187 – 11926LCSDYD → SAAIIH in AAA28644 (PubMed:3099787).Curated
Sequence conflicti1224 – 12329VRVRWTPPV → ATFSLGRHQL in AAA68953 (PubMed:7628438).Curated
Sequence conflicti1224 – 12329VRVRWTPPV → ATFSLGRHQL in AAA28644 (PubMed:3099787).Curated
Sequence conflicti1263 – 128220DFNQT…LYSFR → RLQPDCRLFNKAQRGPLQLQ in AAA28644 (PubMed:3099787).CuratedAdd
BLAST
Sequence conflicti1300 – 13034IKVE → LIQQ in AAA28645 (PubMed:7876183).Curated
Sequence conflicti1457 – 14582GD → VE in AAA28644 (PubMed:3099787).Curated
Sequence conflicti1469 – 148416EERDE…NRIGV → RSGMRPDDVSLIAWM in AAA28644 (PubMed:3099787).CuratedAdd
BLAST
Sequence conflicti1473 – 14797EAMMTYL → DGHDDVS in AAA28645 (PubMed:7876183).Curated
Sequence conflicti1499 – 14991M → V in AAA28644 (PubMed:3099787).Curated
Sequence conflicti1519 – 15202DL → PF in AAA28645 (PubMed:7876183).Curated
Sequence conflicti1569 – 157810RDGVYSSASD → QAWCLLLVPVT in AAA28645 (PubMed:7876183).Curated
Sequence conflicti1591 – 15988TLAAQPYQ → ILSLWRSP in AAA28645 (PubMed:7876183).Curated
Sequence conflicti1682 – 16821N → H in AAC47458 (PubMed:7876183).Curated
Sequence conflicti1682 – 16821N → H in AAA28644 (PubMed:3099787).Curated
Sequence conflicti1706 – 17061T → S in AAA28644 (PubMed:3099787).Curated
Sequence conflicti1715 – 17151Q → E in AAC47458 (PubMed:7876183).Curated
Sequence conflicti1792 – 17998IYDPSPKC → STIPVRNG in AAA28644 (PubMed:3099787).Curated
Sequence conflicti1828 – 18281Q → K in AAA28644 (PubMed:3099787).Curated
Sequence conflicti1850 – 18512TA → GI in AAA28644 (PubMed:3099787).Curated
Sequence conflicti1852 – 18543SAG → FTT in AAA68953 (PubMed:7628438).Curated
Sequence conflicti1854 – 18541G → A in AAC47458 (PubMed:7876183).Curated
Sequence conflicti1887 – 18871F → Y in AAA68953 (PubMed:7628438).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28136 mRNA. Translation: AAA68953.1. Frameshift.
U18351 Genomic DNA. Translation: AAC47458.1.
AE014297 Genomic DNA. Translation: AAF55903.2.
AE014297 Genomic DNA. Translation: ACL83549.1.
AE014297 Genomic DNA. Translation: ACL83550.1.
AE014297 Genomic DNA. Translation: ACL83551.1.
M14778 mRNA. Translation: AAA28644.1. Frameshift.
M13568 Genomic DNA. Translation: AAA28645.1.
PIRiA56081.
S57245.
RefSeqiNP_001138093.1. NM_001144621.3.
NP_001138094.1. NM_001144622.2.
NP_001138095.1. NM_001144623.2.
NP_524436.2. NM_079712.6.
UniGeneiDm.1271.

Genome annotation databases

EnsemblMetazoaiFBtr0084121; FBpp0083519; FBgn0013984.
FBtr0290230; FBpp0288669; FBgn0013984.
FBtr0290231; FBpp0288670; FBgn0013984.
FBtr0290232; FBpp0288671; FBgn0013984.
GeneIDi42549.
KEGGidme:Dmel_CG18402.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28136 mRNA. Translation: AAA68953.1. Frameshift.
U18351 Genomic DNA. Translation: AAC47458.1.
AE014297 Genomic DNA. Translation: AAF55903.2.
AE014297 Genomic DNA. Translation: ACL83549.1.
AE014297 Genomic DNA. Translation: ACL83550.1.
AE014297 Genomic DNA. Translation: ACL83551.1.
M14778 mRNA. Translation: AAA28644.1. Frameshift.
M13568 Genomic DNA. Translation: AAA28645.1.
PIRiA56081.
S57245.
RefSeqiNP_001138093.1. NM_001144621.3.
NP_001138094.1. NM_001144622.2.
NP_001138095.1. NM_001144623.2.
NP_524436.2. NM_079712.6.
UniGeneiDm.1271.

3D structure databases

ProteinModelPortaliP09208.
SMRiP09208. Positions 1361-1668.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67515. 12 interactions.
IntActiP09208. 5 interactions.
STRINGi7227.FBpp0288669.

PTM databases

iPTMnetiP09208.

Proteomic databases

PaxDbiP09208.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0084121; FBpp0083519; FBgn0013984.
FBtr0290230; FBpp0288669; FBgn0013984.
FBtr0290231; FBpp0288670; FBgn0013984.
FBtr0290232; FBpp0288671; FBgn0013984.
GeneIDi42549.
KEGGidme:Dmel_CG18402.

Organism-specific databases

CTDi42549.
FlyBaseiFBgn0283499. InR.

Phylogenomic databases

eggNOGiKOG4258. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118818.
InParanoidiP09208.
KOiK05087.
OMAiKDPRAFI.
OrthoDBiEOG7B31KZ.
PhylomeDBiP09208.

Enzyme and pathway databases

BRENDAi2.7.10.1. 1994.
ReactomeiR-DME-77387. Insulin receptor recycling.
SignaLinkiP09208.

Miscellaneous databases

GenomeRNAii42549.
PROiP09208.

Gene expression databases

BgeeiP09208.
ExpressionAtlasiP09208. differential.
GenevisibleiP09208. DM.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
3.80.20.20. 2 hits.
InterProiIPR003961. FN3_dom.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR002011. Tyr_kinase_rcpt_2_CS.
[Graphical view]
PfamiPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00060. FN3. 3 hits.
SM00261. FU. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 3 hits.
SSF52058. SSF52058. 2 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS50853. FN3. 3 hits.
PS01352. HEMATOPO_REC_L_F1. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00239. RECEPTOR_TYR_KIN_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila insulin receptor homolog: a gene essential for embryonic development encodes two receptor isoforms with different signaling potential."
    Fernandez R., Tabarini D., Azpiazu N., Frasch M., Schlessinger J.
    EMBO J. 14:3373-3384(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, PROTEOLYTIC PROCESSING.
  2. "The Drosophila insulin receptor contains a novel carboxyl-terminal extension likely to play an important role in signal transduction."
    Ruan Y., Chen C., Cao Y., Garofalo R.S.
    J. Biol. Chem. 270:4236-4243(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. "Cloning of a Drosophila cDNA encoding a polypeptide similar to the human insulin receptor precursor."
    Nishida Y., Hata M., Nishizuka Y., Rutter W.J., Ebina Y.
    Biochem. Biophys. Res. Commun. 141:474-481(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 652-1851.
    Strain: Oregon-R.
    Tissue: Embryo.
  6. "Isolation of a Drosophila genomic sequence homologous to the kinase domain of the human insulin receptor and detection of the phosphorylated Drosophila receptor with an anti-peptide antibody."
    Petruzzelli L., Herrera R., Arenas-Garcia R., Fernandez R., Birnbaum M.J., Rosen O.M.
    Proc. Natl. Acad. Sci. U.S.A. 83:4710-4714(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1300-1598, DEVELOPMENTAL STAGE, AUTOPHOSPHORYLATION.
  7. "Tissue localization of Drosophila melanogaster insulin receptor transcripts during development."
    Garofalo R.S., Rosen O.M.
    Mol. Cell. Biol. 8:1638-1647(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  8. "The Drosophila insulin receptor is required for normal growth."
    Chen C., Jack J., Garofalo R.S.
    Endocrinology 137:846-856(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOPHOSPHORYLATION.
  9. "The carboxyl terminal extension of the Drosophila insulin receptor homologue binds IRS-1 and influences cell survival."
    Marin-Hincapie M., Garofalo R.S.
    J. Biol. Chem. 274:24987-24994(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHICO.
  10. "An evolutionarily conserved function of the Drosophila insulin receptor and insulin-like peptides in growth control."
    Brogiolo W., Stocker H., Ikeya T., Rintelen F., Fernandez R., Hafen E.
    Curr. Biol. 11:213-221(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-1467; GLY-1539 AND GLY-1599.
  11. "A mutant Drosophila insulin receptor homolog that extends life-span and impairs neuroendocrine function."
    Tatar M., Kopelman A., Epstein D., Tu M.P., Yin C.M., Garofalo R.S.
    Science 292:107-110(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Axons guided by insulin receptor in Drosophila visual system."
    Song J., Wu L., Chen Z., Kohanski R.A., Pick L.
    Science 300:502-505(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DOCK.
  13. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1816, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  14. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-824; ASN-839; ASN-864; ASN-898; ASN-1147; ASN-1218 AND ASN-1219, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiINSR_DROME
AccessioniPrimary (citable) accession number: P09208
Secondary accession number(s): B7Z0N6
, Q24023, Q24089, Q9VD94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 29, 2005
Last modified: June 8, 2016
This is version 193 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.