IRS1_XENTR
ID IRS1_XENTR Reviewed; 654 AA.
AC Q6P4Y6;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Insulin receptor substrate 1;
DE Short=IRS-1;
GN Name=irs1 {ECO:0000250|UniProtKB:P35570};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAH63198.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH63198.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May mediate the control of various cellular processes by
CC insulin. When phosphorylated by the insulin receptor binds specifically
CC to various cellular proteins containing SH2 domains such as
CC phosphatidylinositol 3-kinase p85 subunit or grb2. Activates
CC phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the NPXY motif of tyrosine-phosphorylated igf1r
CC and insr via the PTB domain. Binds to phosphatidylinositol 3-kinase p85
CC subunit via the phosphorylated YXXM motifs (By similarity).
CC {ECO:0000250|UniProtKB:P35568, ECO:0000250|UniProtKB:Q91615}.
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DR EMBL; BC063198; AAH63198.1; -; mRNA.
DR AlphaFoldDB; Q6P4Y6; -.
DR SMR; Q6P4Y6; -.
DR STRING; 8364.ENSXETP00000057258; -.
DR PaxDb; Q6P4Y6; -.
DR PRIDE; Q6P4Y6; -.
DR eggNOG; ENOG502QUNU; Eukaryota.
DR InParanoid; Q6P4Y6; -.
DR Proteomes; UP000008143; Genome assembly.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
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:0043548; F:phosphatidylinositol 3-kinase binding; ISS:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; 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; 4.
DR Pfam; PF02174; IRS; 1.
DR Pfam; PF00169; PH; 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 2: Evidence at transcript level;
KW Phosphoprotein; Reference proteome; Repeat; Transducer.
FT CHAIN 1..654
FT /note="Insulin receptor substrate 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000223526"
FT DOMAIN 3..107
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 126..230
FT /note="IRS-type PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT REGION 228..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 345..348
FT /note="YXXM motif 1"
FT /evidence="ECO:0000255"
FT MOTIF 384..387
FT /note="YXXM motif 2"
FT /evidence="ECO:0000255"
FT MOTIF 398..401
FT /note="YXXM motif 3"
FT /evidence="ECO:0000255"
FT MOTIF 411..414
FT /note="YXXM motif 4"
FT /evidence="ECO:0000255"
FT MOTIF 430..433
FT /note="YXXM motif 5"
FT /evidence="ECO:0000255"
FT MOTIF 466..469
FT /note="YXXM motif 6"
FT /evidence="ECO:0000255"
FT COMPBIAS 232..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 36
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35568"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT MOD_RES 345
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 398
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 411
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 430
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35568"
FT MOD_RES 563
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
SQ SEQUENCE 654 AA; 71920 MW; 6A6368DDE23A6617 CRC64;
MEDIKKCGYL RKQKSMRKRY FVLRCPGTRG PARLEYYENE KKFRVAEGSG GPRGVLNLEE
AFGVNKRSDA KKRHLLVIYT RDGGLGVSAD GEEEQDEWYQ AILEVQAQAR ALSSSPDAPA
WPGPAFREVW QVSVRPRGLG QTRNLSGIYR LCLAERTLGL LRLRSENPSV TLQLMNVRRC
GHSDNYFFVE VGRSAVTGPG ELWMQVEDSV VAQNMHETIL EAMKSLSEEF RPRTKSQSLS
STPISVPSRR HHPNPPPPSQ VGISRRSRAE TPIENSPVPK PHSLSKDYSV QSPEEEEEEK
GARVETNESS ADYGSASSDE YGSSPGVLEA PVFLPPSPGP RETNYISMAL YGRRSLVMEP
ISTNANVPAE EGSRLTLFQE EDNYAMMGQR EPRQETGYMP MLPGSNRSQD YMPMTPTSIS
PPAPVEMAGY VMMSPLGSCS PEIERLSWPP SQEVSAGSSD SHASDYMNMW SLSRSASSTP
PPQEAFLSSP GGPCRVPASY RSLPRSYKME PQPSARASCS SSSDSLEEVN AGKNRRPLSI
SIDSWNTGTL SGNYRRPPSP GEYVSIHFRA PPEEDLREGS HRCPKRVRFH GGAALGDAQR
GLHGNGLCAS QNFTTSCKNE RGTGNERGKC LQTCGEITAG LGEDFLGEGL LGCR
