IRS1A_XENLA
ID IRS1A_XENLA Reviewed; 885 AA.
AC Q91615;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Insulin receptor substrate 1-A;
DE Short=IRS1-A;
DE Short=xIRS-1-A;
DE AltName: Full=XIRS-L;
GN Name=irs1-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAA73572.1}
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, PHOSPHORYLATION, AND
RP INTERACTION WITH PIK3R1.
RC TISSUE=Ovary {ECO:0000269|PubMed:7791763};
RX PubMed=7791763; DOI=10.1128/mcb.15.7.3563;
RA Liu X.J., Sorisky A., Zhu L., Pawson T.;
RT "Molecular cloning of an amphibian insulin receptor substrate 1-like cDNA
RT and involvement of phosphatidylinositol 3-kinase in insulin-induced Xenopus
RT oocyte maturation.";
RL Mol. Cell. Biol. 15:3563-3570(1995).
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 (By similarity). Binds to
CC phosphatidylinositol 3-kinase p85 subunit at a low level in vitro prior
CC to phosphorylation. Binding is greatly enhanced following tyrosine
CC phosphorylation by insr and probably occurs via the phosphorylated YXXM
CC motifs. {ECO:0000250|UniProtKB:P35568, ECO:0000269|PubMed:7791763}.
CC -!- DEVELOPMENTAL STAGE: Expressed in stage VI primed oocytes (at protein
CC level). {ECO:0000269|PubMed:7791763}.
CC -!- PTM: Phosphorylation of Tyr-582 is required for grb2-binding.
CC {ECO:0000250}.
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DR EMBL; U27842; AAA73572.1; -; mRNA.
DR RefSeq; NP_001084092.1; NM_001090623.1.
DR AlphaFoldDB; Q91615; -.
DR SMR; Q91615; -.
DR PRIDE; Q91615; -.
DR GeneID; 399299; -.
DR KEGG; xla:399299; -.
DR CTD; 399299; -.
DR Xenbase; XB-GENE-478676; irs1.L.
DR OrthoDB; 298675at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 399299; Expressed in muscle tissue and 19 other tissues.
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:0043548; F:phosphatidylinositol 3-kinase binding; IDA:UniProtKB.
DR GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR039011; IRS.
DR InterPro; IPR002404; IRS_PTB.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR10614; PTHR10614; 1.
DR Pfam; PF02174; IRS; 1.
DR PRINTS; PR00628; INSULINRSI.
DR SMART; SM00310; PTBI; 1.
DR PROSITE; PS51064; IRS_PTB; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Repeat; Transducer.
FT CHAIN 1..885
FT /note="Insulin receptor substrate 1-A"
FT /evidence="ECO:0000305"
FT /id="PRO_0000223524"
FT DOMAIN 1..56
FT /note="IRS-type PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT REGION 56..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..584
FT /note="GRB2-binding"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT REGION 637..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 257..260
FT /note="YXXM motif 1"
FT /evidence="ECO:0000255"
FT MOTIF 318..321
FT /note="YXXM motif 2"
FT /evidence="ECO:0000255"
FT MOTIF 364..367
FT /note="YXXM motif 3"
FT /evidence="ECO:0000255"
FT MOTIF 381..384
FT /note="YXXM motif 4"
FT /evidence="ECO:0000255"
FT MOTIF 409..412
FT /note="YXXM motif 5"
FT /evidence="ECO:0000255"
FT MOTIF 451..454
FT /note="YXXM motif 6"
FT /evidence="ECO:0000255"
FT MOTIF 620..623
FT /note="YXXM motif 7"
FT /evidence="ECO:0000255"
FT MOTIF 672..675
FT /note="YXXM motif 8"
FT /evidence="ECO:0000255"
FT MOTIF 706..709
FT /note="YXXM motif 9"
FT /evidence="ECO:0000255"
FT COMPBIAS 58..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT MOD_RES 257
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 364
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 381
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 409
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35568"
FT MOD_RES 582
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 620
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 672
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 834
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 866
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
SQ SEQUENCE 885 AA; 96146 MW; 9F1B96C64949CA7D CRC64;
MNIRRCGHSE NFFFIEVGRS AVTGAGEFWM QVDDSVVAQN MHETILEAMK ALSDEFRPRS
KSQSSSNCSN PISVPLRRHH LNHPPPSQVG LNRRARTESA TATSPAGGAA KHGSSSFRVR
ASSDGEGTMS RPASMEGSPV SPSASRTQSH RHRGSSRLHP PLNHSRSIPM PATRCSPSAT
SPVSLSSSST SGHGSTSDCM CPRRSSASIS GSPSDGGFIS SDEYGSSPCD FRSSFRSVTP
DSMGHTPPAR EEELNNYICM GKSSSHLQRG PQQRYQPSRG EELTDFDKVF RKRTHSSGTS
PPTVSHQKTP SQSSIEEYTE MMPTHPVRLT SFRHSAFVPT YSYPEECLDL HLEGSRANHK
DDGYMPMSPG VAPVSTKTND YMPMSPKSVS APQQIINPRW HSAVDSNGYM MMSPSGSCSP
DNTNYSKIWT NGTNPKLSID SIEGKLPCSD YINMSPASGS TTSTPPDSYL NSVEESTKPV
YSYFSLPRSF KHVHRKSEDG NLRISANSGH NLYTEDSSSS STSSDSLGGQ DPQQPRKGEG
CIQGKRLTRP TRLSLENSSK ASTLPRVREP ALPPEPKSPG EYVNIEFNDK VFSGGLVPSM
CSLPFVQSRV VPQRENLSEY MNMDLGVWRA KTSYASTSSY EPPNKPVNSV CPTETCSSSR
PPIRGKPISR DYMSMQLGSL CPDYSQVPPT RLSAKSITLS SSKSNYAEMS SGRVSDNIPA
IAPASNSSLS EASRSSLLGQ GSGPSAFTRV SLSPNRNPSA KVIRAGDPQG RRRHSSETFS
STPTTARVTT GPVSGEDVKR HSSASFENVW LRPGEIARRD SLQPSDHTHN GLNYIDLDLA
KDLSSLDHCN SHQSGVSHPS DDLSPYASIT FHKLEEHRSQ AETEE
