IRS1_DROME
ID IRS1_DROME Reviewed; 968 AA.
AC Q9XTN2; D0UY43; D0UY45; D0UY46; D0UY47; D0UY49; D0UY50; D0UY51; D0UY52;
AC D0UY54; D0UY55; D0UY61; D0UY62; D0UY64; D0UY65; D0UY66; D0UY67; D0UY68;
AC Q5U0V5; Q9U4G2;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Insulin receptor substrate 1;
DE Short=dIRS;
DE AltName: Full=Protein chico;
GN Name=chico; Synonyms=IRS; ORFNames=CG5686;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=10399915; DOI=10.1016/s0092-8674(00)80799-0;
RA Boehni R., Riesgo-Escovar J., Oldham S.M., Brogiolo W., Stocker H.,
RA Andruss B.F., Beckingham K., Hafen E.;
RT "Autonomous control of cell and organ size by CHICO, a Drosophila homolog
RT of vertebrate IRS1-4.";
RL Cell 97:865-875(1999).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=10801879; DOI=10.1074/jbc.m003579200;
RA Poltilove R.M.K., Jacobs A.R., Haft C.R., Xu P., Taylor S.I.;
RT "Characterization of Drosophila insulin receptor substrate.";
RL J. Biol. Chem. 275:23346-23354(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-29; THR-165; HIS-334
RP DEL; VAL-429; THR-452; ARG-664; SER-675; ILE-676; GLY-721; LEU-722;
RP SER-744; HIS-758 DEL; MET-808; VAL-851 AND THR-873.
RC STRAIN=FSP15, FSP16, FSP19, FSP2, FSP23, FSP25, FSP29, FSP3, RR11, RR17,
RC RR18, RR33, RR35, RR52, RR8, S103, S107, S108, S76, S97, SL5_131, SL5_29,
RC T15, T28, T39, T41, and T9;
RX PubMed=20074316; DOI=10.1111/j.1365-294x.2009.04508.x;
RA Paaby A.B., Blacket M.J., Hoffmann A.A., Schmidt P.S.;
RT "Identification of a candidate adaptive polymorphism for Drosophila life
RT history by parallel independent clines on two continents.";
RL Mol. Ecol. 19:760-774(2010).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 551-968.
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11292874; DOI=10.1126/science.1057991;
RA Clancy D.J., Gems D., Harshman L.G., Oldham S., Stocker H., Hafen E.,
RA Leevers S.J., Partridge L.;
RT "Extension of life-span by loss of CHICO, a Drosophila insulin receptor
RT substrate protein.";
RL Science 292:104-106(2001).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15890189; DOI=10.1016/j.jinsphys.2004.12.013;
RA Richard D.S., Rybczynski R., Wilson T.G., Wang Y., Wayne M.L., Zhou Y.,
RA Partridge L., Harshman L.G.;
RT "Insulin signaling is necessary for vitellogenesis in Drosophila
RT melanogaster independent of the roles of juvenile hormone and ecdysteroids:
RT female sterility of the chico1 insulin signaling mutation is autonomous to
RT the ovary.";
RL J. Insect Physiol. 51:455-464(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286; SER-287; SER-342;
RP SER-555; SER-932 AND SER-935, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Activates phosphatidylinositol 3-kinase when bound to the
CC regulatory p85 subunit (By similarity). May mediate the control of
CC various cellular processes by insulin-like peptides. When
CC phosphorylated by the insulin receptor binds specifically to various
CC cellular proteins containing SH2 domains. Involved in control of cell
CC proliferation, cell size, and body and organ growth throughout
CC development. Also has a role in a signaling pathway controlling the
CC physiological response required to endure periods of low nutrient
CC conditions. Insulin/insulin-like growth factor (IGF) signaling pathway
CC has a role in regulating aging and is necessary in the ovary for
CC vitellogenic maturation. {ECO:0000250, ECO:0000269|PubMed:10399915,
CC ECO:0000269|PubMed:10801879, ECO:0000269|PubMed:11292874,
CC ECO:0000269|PubMed:15890189}.
CC -!- SUBUNIT: Bindings to phosphatidylinositol 3-kinase and SHP2.
CC -!- INTERACTION:
CC Q9XTN2; P09208: InR; NbExp=3; IntAct=EBI-176370, EBI-92063;
CC -!- DEVELOPMENTAL STAGE: Expressed during G1, S and G2 phase of the cell
CC cycle. {ECO:0000269|PubMed:10399915}.
CC -!- DISRUPTION PHENOTYPE: Female sterile. Extends fruit fly median life-
CC span by up to 48% in homozygotes and 36% in heterozygotes.
CC {ECO:0000269|PubMed:11292874, ECO:0000269|PubMed:15890189}.
CC -!- MISCELLANEOUS: 'Chico' means 'small boy' in Spanish. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD55429.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF154826; AAD40880.1; -; mRNA.
DR EMBL; AF092046; AAD43005.1; -; mRNA.
DR EMBL; GQ927177; ACY01718.1; -; Genomic_DNA.
DR EMBL; GQ927178; ACY01719.1; -; Genomic_DNA.
DR EMBL; GQ927179; ACY01720.1; -; Genomic_DNA.
DR EMBL; GQ927180; ACY01721.1; -; Genomic_DNA.
DR EMBL; GQ927181; ACY01722.1; -; Genomic_DNA.
DR EMBL; GQ927182; ACY01723.1; -; Genomic_DNA.
DR EMBL; GQ927183; ACY01724.1; -; Genomic_DNA.
DR EMBL; GQ927184; ACY01725.1; -; Genomic_DNA.
DR EMBL; GQ927185; ACY01726.1; -; Genomic_DNA.
DR EMBL; GQ927186; ACY01727.1; -; Genomic_DNA.
DR EMBL; GQ927187; ACY01728.1; -; Genomic_DNA.
DR EMBL; GQ927188; ACY01729.1; -; Genomic_DNA.
DR EMBL; GQ927189; ACY01730.1; -; Genomic_DNA.
DR EMBL; GQ927190; ACY01731.1; -; Genomic_DNA.
DR EMBL; GQ927191; ACY01732.1; -; Genomic_DNA.
DR EMBL; GQ927192; ACY01733.1; -; Genomic_DNA.
DR EMBL; GQ927193; ACY01734.1; -; Genomic_DNA.
DR EMBL; GQ927194; ACY01735.1; -; Genomic_DNA.
DR EMBL; GQ927195; ACY01736.1; -; Genomic_DNA.
DR EMBL; GQ927196; ACY01737.1; -; Genomic_DNA.
DR EMBL; GQ927197; ACY01738.1; -; Genomic_DNA.
DR EMBL; GQ927198; ACY01739.1; -; Genomic_DNA.
DR EMBL; GQ927199; ACY01740.1; -; Genomic_DNA.
DR EMBL; GQ927200; ACY01741.1; -; Genomic_DNA.
DR EMBL; GQ927201; ACY01742.1; -; Genomic_DNA.
DR EMBL; GQ927202; ACY01743.1; -; Genomic_DNA.
DR EMBL; GQ927203; ACY01744.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52882.1; -; Genomic_DNA.
DR EMBL; BT016137; AAV37022.1; -; mRNA.
DR EMBL; AF181643; AAD55429.1; ALT_INIT; mRNA.
DR RefSeq; NP_001188772.1; NM_001201843.2.
DR RefSeq; NP_001260316.1; NM_001273387.1.
DR RefSeq; NP_723540.1; NM_164899.3.
DR AlphaFoldDB; Q9XTN2; -.
DR SMR; Q9XTN2; -.
DR BioGRID; 72865; 39.
DR DIP; DIP-23631N; -.
DR IntAct; Q9XTN2; 7.
DR STRING; 7227.FBpp0079677; -.
DR iPTMnet; Q9XTN2; -.
DR PaxDb; Q9XTN2; -.
DR PRIDE; Q9XTN2; -.
DR DNASU; 64880; -.
DR EnsemblMetazoa; FBtr0080088; FBpp0079677; FBgn0024248.
DR EnsemblMetazoa; FBtr0303904; FBpp0292907; FBgn0024248.
DR EnsemblMetazoa; FBtr0333412; FBpp0305604; FBgn0024248.
DR GeneID; 64880; -.
DR KEGG; dme:Dmel_CG5686; -.
DR UCSC; CG5686-RA; d. melanogaster.
DR CTD; 30067; -.
DR FlyBase; FBgn0024248; chico.
DR VEuPathDB; VectorBase:FBgn0024248; -.
DR eggNOG; ENOG502QUNU; Eukaryota.
DR GeneTree; ENSGT00940000170368; -.
DR HOGENOM; CLU_012544_0_0_1; -.
DR InParanoid; Q9XTN2; -.
DR OMA; HYRLNTR; -.
DR OrthoDB; 187805at2759; -.
DR PhylomeDB; Q9XTN2; -.
DR Reactome; R-DME-109704; PI3K Cascade.
DR Reactome; R-DME-110478; Insulin signaling pathway.
DR Reactome; R-DME-112399; IRS-mediated signalling.
DR Reactome; R-DME-112412; SOS-mediated signalling.
DR Reactome; R-DME-1257604; PIP3 activates AKT signaling.
DR Reactome; R-DME-198203; PI3K/AKT activation.
DR Reactome; R-DME-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DME-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-DME-74749; Signal attenuation.
DR Reactome; R-DME-9027276; Erythropoietin activates Phosphoinositide-3-kinase (PI3K).
DR Reactome; R-DME-9027284; Erythropoietin activates RAS.
DR SignaLink; Q9XTN2; -.
DR BioGRID-ORCS; 64880; 0 hits in 3 CRISPR screens.
DR ChiTaRS; chico; fly.
DR GenomeRNAi; 64880; -.
DR PRO; PR:Q9XTN2; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0024248; Expressed in capitellum (Drosophila) and 26 other tissues.
DR ExpressionAtlas; Q9XTN2; baseline and differential.
DR Genevisible; Q9XTN2; DM.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0005158; F:insulin receptor binding; IGI:FlyBase.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISS:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IMP:FlyBase.
DR GO; GO:0009267; P:cellular response to starvation; IMP:FlyBase.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IMP:FlyBase.
DR GO; GO:0042593; P:glucose homeostasis; IMP:FlyBase.
DR GO; GO:0007295; P:growth of a germarium-derived egg chamber; IMP:FlyBase.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IMP:FlyBase.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:FlyBase.
DR GO; GO:0048133; P:male germ-line stem cell asymmetric division; IMP:FlyBase.
DR GO; GO:0035264; P:multicellular organism growth; IMP:FlyBase.
DR GO; GO:0061964; P:negative regulation of entry into reproductive diapause; IMP:FlyBase.
DR GO; GO:0010897; P:negative regulation of triglyceride catabolic process; IMP:FlyBase.
DR GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IMP:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:FlyBase.
DR GO; GO:0045927; P:positive regulation of growth; IMP:FlyBase.
DR GO; GO:0050778; P:positive regulation of immune response; IMP:FlyBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:FlyBase.
DR GO; GO:0046622; P:positive regulation of organ growth; IMP:FlyBase.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:FlyBase.
DR GO; GO:0007285; P:primary spermatocyte growth; IMP:FlyBase.
DR GO; GO:0043491; P:protein kinase B signaling; IMP:FlyBase.
DR GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
DR GO; GO:0034059; P:response to anoxia; IDA:FlyBase.
DR GO; GO:0042594; P:response to starvation; IMP:FlyBase.
DR GO; GO:0007296; P:vitellogenesis; IMP:UniProtKB.
DR CDD; cd01204; PTB_IRS; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR039011; IRS.
DR InterPro; IPR002404; IRS_PTB.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10614; PTHR10614; 1.
DR Pfam; PF02174; IRS; 1.
DR PRINTS; PR00628; INSULINRSI.
DR SMART; SM00233; PH; 1.
DR SMART; SM00310; PTBI; 1.
DR PROSITE; PS51064; IRS_PTB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Differentiation; Growth regulation; Oogenesis; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..968
FT /note="Insulin receptor substrate 1"
FT /id="PRO_0000084235"
FT DOMAIN 8..109
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145,
FT ECO:0000305"
FT DOMAIN 122..236
FT /note="IRS-type PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT REGION 248..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 411..414
FT /note="YXXM motif 1"
FT MOTIF 641..644
FT /note="YXXM motif 2"
FT COMPBIAS 304..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 411
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 911
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 935
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 948
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT VARIANT 29
FT /note="Y -> C (in strain: S108)"
FT /evidence="ECO:0000269|PubMed:20074316"
FT VARIANT 165
FT /note="P -> T (in strain: FSP2, FSP15, FSP16, FSP19, FSP23,
FT FSP29, RR8, RR11, RR17, RR18, RR35, RR52, S76, SL5_131,
FT SL5_29, T28 and T39)"
FT /evidence="ECO:0000269|PubMed:20074316"
FT VARIANT 334
FT /note="Missing (in strain: S108)"
FT /evidence="ECO:0000269|PubMed:20074316"
FT VARIANT 429
FT /note="A -> V (in strain: FSP19, RR33 and S108)"
FT /evidence="ECO:0000269|PubMed:20074316"
FT VARIANT 452
FT /note="A -> T (in strain: RR33, S108, T28 and T39)"
FT /evidence="ECO:0000269|PubMed:20074316"
FT VARIANT 664
FT /note="K -> R (in strain: FSP2, FSP3, FSP15, FSP19, FSP23,
FT FSP25, FSP29, RR8, RR11, RR17, RR18, RR33, RR35, RR52, S76,
FT S107, S108, T9, T15, T28, T39 and T41)"
FT /evidence="ECO:0000269|PubMed:20074316"
FT VARIANT 675
FT /note="P -> S (in strain: S103)"
FT /evidence="ECO:0000269|PubMed:20074316"
FT VARIANT 676
FT /note="L -> I (in strain: FSP3, FSP15, FSP19, FSP23, FSP25,
FT RR8, RR11, RR17, RR33, RR35, RR52, S76, S97, S107, S108,
FT T9, T28, T39 and T41)"
FT /evidence="ECO:0000269|PubMed:20074316"
FT VARIANT 721
FT /note="S -> G (in strain: FSP2, FSP3, FSP15, FSP23, FSP25,
FT FSP29, RR8, RR11, RR17, RR18, RR33, RR35, RR52, S108, T9,
FT T15, T28, T39 and T41)"
FT /evidence="ECO:0000269|PubMed:20074316"
FT VARIANT 722
FT /note="S -> L (in strain: FSP2, FSP3, FSP15, FSP16, FSP19,
FT FSP23, FSP25, FSP29, RR8, RR11, RR17, RR18, RR33, RR35,
FT RR52, S76, S97, S103, S107, S108, SL5_131, SL5_29, T9, T15,
FT T28, T39 and T41)"
FT /evidence="ECO:0000269|PubMed:20074316"
FT VARIANT 744
FT /note="C -> S (in strain: FSP3, FSP15, FSP16, FSP23, FSP25,
FT FSP29, RR8, RR11, RR17, RR33, RR35, RR52, S108, T9, T15,
FT T28, T39 and T41)"
FT /evidence="ECO:0000269|PubMed:20074316"
FT VARIANT 758
FT /note="Missing (in strain: FSP2, FSP3, FSP15, FSP16, FSP23,
FT FSP25. FSP29, RR8, RR11, RR17, RR18, RR35, RR52, S97, S103,
FT S108, SL5_131, SL5_29, T9, T15 and T41)"
FT /evidence="ECO:0000269|PubMed:20074316"
FT VARIANT 808
FT /note="I -> M (in strain: RR8 and T41)"
FT /evidence="ECO:0000269|PubMed:20074316"
FT VARIANT 851
FT /note="A -> V (in strain: FSP19)"
FT /evidence="ECO:0000269|PubMed:20074316"
FT VARIANT 873
FT /note="A -> T (in strain: FSP16)"
FT /evidence="ECO:0000269|PubMed:20074316"
SQ SEQUENCE 968 AA; 107832 MW; 04E9856F37F7A4CF CRC64;
MASISDDGMA LSGYLKKLKT MKKKFFVLYE ETSTSAARLE YYDTEKKFLQ RAEPKRVIYL
KNCFNINRRL DTKHRFVIVL SSRDGGFGIV LENENDLRKW LDKLLVLQRN IANSNGTAHS
PYDHVWQVVI QKKGISEKVG ITGTYHCCLT SKSLTFVCIG PEKTPNGEDR VASIEILLTT
IRRCGHASPQ CIFYVELGRQ SVLGSGDLWM ETDNAAIATN MHNTILSAMS AKTESNTNLI
NVYQNRPDLS HEPMRKRSSS ANEASKPINV NVIQNSQNSL ELRSCSSPHN YGFGRERCDS
LPTRNGTLSE SSNQTYFGSN HGLRSNTISG IRPHSTNKHS NSPTFTMPLR CSESEESSIS
VDESDDNGSF SHYRLNTRSS ETAIPEENID DFASAELFSK VTEQNVSDEN YIPMNPVNPT
DAIHEKEKAD MQRLEDASLH FNFPEHASEK LAKDFDLDSD NQCCRPIRAY SIGNKVEHLK
FNKRLGHLND TGQNPNRVRA YSVGSKSKIP RCDLQRVVLV EDNKHEFTAN RSQSSITKEG
TSYGSSANRQ KKSTSAPLLS LKNQINSDRM SDLMEIDFSQ ATNLEKQKFI KNNEIPKYIE
NVFPKAPRTD SSSLTLHATS QKDIFNGTKL NNTAITSEDG YLEMKPVGNG YTPSSNCLPM
KVEKLKLSDY QTAPPLTATA APVHDLNKIS TYNISAEKWR EQPSRSEEKK SNSPLNDNTF
SSKPTNVEST SKSHDVHSAN QIDCEKVCAQ SSDKLNNHLA DKIVENNNLD IGGHEEKKLV
HSISSEDYTQ IKDKSNDFTK FNEAGYKILQ IKSDSSLISS KLYQKGIHKD NLERSQRLTE
SVNTIPDNAT ATAVSSSSLT KFNINSAKPA AAADSRSTGT DPSTPQNILQ IKDLNFPSRS
SSRISQPELH YASLDLPHCS GQNPAKYLKR GSRESPPVSA CPEDGNTYAK IDFDQSDSSS
SSSNIFNT
