IRS1_DROYA
ID IRS1_DROYA Reviewed; 949 AA.
AC B4NZ70;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Insulin receptor substrate 1 {ECO:0000250|UniProtKB:Q9XTN2};
DE AltName: Full=Protein chico {ECO:0000250|UniProtKB:Q9XTN2};
GN Name=chico {ECO:0000250|UniProtKB:Q9XTN2}; ORFNames=GE26285;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1] {ECO:0000312|EMBL:EDW88765.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01 {ECO:0000312|EMBL:EDW88765.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Activates phosphatidylinositol 3-kinase when bound to the
CC regulatory p85 subunit. May mediate the control of various cellular
CC processes by insulin-like peptides. When phosphorylated by the insulin
CC receptor binds specifically to various cellular proteins containing SH2
CC domains. Involved in control of cell proliferation, cell size, and body
CC and organ growth throughout development. Also has a role in a signaling
CC pathway controlling the physiological response required to endure
CC periods of low nutrient conditions. Insulin/insulin-like growth factor
CC (IGF) signaling pathway has a role in regulating aging and is necessary
CC in the ovary for vitellogenic maturation (By similarity).
CC {ECO:0000250|UniProtKB:P35570, ECO:0000250|UniProtKB:Q9XTN2}.
CC -!- SUBUNIT: Bindings to phosphatidylinositol 3-kinase and SHP2.
CC {ECO:0000250|UniProtKB:Q9XTN2}.
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DR EMBL; CM000157; EDW88765.1; -; Genomic_DNA.
DR RefSeq; XP_002089053.2; XM_002089017.2.
DR RefSeq; XP_015054493.1; XM_015199007.1.
DR RefSeq; XP_015054494.1; XM_015199008.1.
DR AlphaFoldDB; B4NZ70; -.
DR SMR; B4NZ70; -.
DR STRING; 7245.FBpp0271295; -.
DR EnsemblMetazoa; FBtr0401223; FBpp0360148; FBgn0243316.
DR EnsemblMetazoa; FBtr0402210; FBpp0361071; FBgn0243316.
DR GeneID; 6527986; -.
DR eggNOG; ENOG502QUNU; Eukaryota.
DR HOGENOM; CLU_012544_0_0_1; -.
DR OMA; HYRLNTR; -.
DR OrthoDB; 187805at2759; -.
DR PhylomeDB; B4NZ70; -.
DR ChiTaRS; chico; fly.
DR Proteomes; UP000002282; Chromosome 2L.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005158; F:insulin receptor binding; ISS:UniProtKB.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0007296; P:vitellogenesis; ISS: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 3: Inferred from homology;
KW Differentiation; Growth regulation; Oogenesis; Phosphoprotein; Repeat.
FT CHAIN 1..949
FT /note="Insulin receptor substrate 1"
FT /id="PRO_0000395322"
FT DOMAIN 8..109
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 122..236
FT /note="IRS-type PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT REGION 247..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 410..413
FT /note="YXXM motif 1"
FT /evidence="ECO:0000255"
FT MOTIF 640..643
FT /note="YXXM motif 2"
FT /evidence="ECO:0000255"
FT COMPBIAS 304..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9XTN2"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9XTN2"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9XTN2"
FT MOD_RES 410
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9XTN2"
FT MOD_RES 892
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT MOD_RES 913
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9XTN2"
FT MOD_RES 916
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9XTN2"
FT MOD_RES 929
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250|UniProtKB:P35570"
SQ SEQUENCE 949 AA; 106273 MW; 1C34A2E10E196EC4 CRC64;
MASISDDGMA LSGYLKKLKT MKKKFFVLYE ETSHSAARLE YYDSEKKFLQ RAEPKRVIYL
KNCFNINRRL DTKHRFVIVL SSRDGGFGIV LENENDLRKW LDKLLVLQRN IANSNGTAHS
PYDQVWQVVI QKKGISEKVG ITGTYHCCLT SKSLTFVCIG PEKTPNGEDR VASIEILLTT
IRRCGHASPQ CIFYVELGRQ SVLGSGDLWM ETDNAAVATN MHNTILSAMS AKTESNTNLI
NVYQNRPDLS HEPMRKRSSS ANEASKPINV NVIQNSQNSL EFRSCSSPHN YGFGRERCDS
LPTRNGTLSE SSNQTYFGSN HGLRSNTISG NRPHSTNKHS NSPTFTMPLR CSESEESSIS
VEESDDNGSY SHYRLNTRTS ETAIPEENID DFASAEFSKV TEPNESDENY IPMTPINPTD
AIHEKEKIDM QRLEDASLHF DFPEHASEKL AKDYDLDSDN QCVRPIRAYS IGNKVEHLKF
NKRLGHLNDT GQNPNRVRAY SVGSKSKIPR CDLQRVVLVE DNKHEFVANR SQSSITKEGS
GYGTSGNRQK KSTSAPLLSL KNQINSDRMS DLMEIDFSQA SNLEKQKFIK NNEIPKYIEN
VFPKTPRTDS SSLTLHATSQ KDIFNGTKLN NTANTSEDGY LEMKPVGNAY TPSSNCLPIK
VEKLKLSDYT APLTTAAPVH DLNKISTYNI SAEKWREQTT SEEKKSNSPL NEKPFSLKPT
NVENISHDVH STNNIDCEQV SVQSDKQNNL DDKIVENNNL DIGGHEEKKL VHSISSEDYT
QIKDKSNDFT KFNEAGYKIL QIKSDSSLIS SKLYQKGIHK DNLERSHRLT ESVNTIPDNA
TASSSVTKFN INAKAADSRS TDPSTPQNIL QIKDLNFPSR SSSRISQPEL HYASLDLPHC
SGQNPAKYLK RGSRESPPVS ACPEDGNTYA KIDFDQSDSS SSSSNIFNT
