IRS1B_XENLA
ID IRS1B_XENLA Reviewed; 1088 AA.
AC P84770;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Insulin receptor substrate 1-B;
DE Short=IRS1-B;
DE Short=xIRS-1-B;
DE AltName: Full=XIRS-L';
GN Name=irs1-b;
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}
RP NUCLEOTIDE SEQUENCE [MRNA].
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. Binds to phosphatidylinositol 3-kinase p85
CC subunit at a low level in vitro prior to phosphorylation. Binding is
CC greatly enhanced following tyrosine phosphorylation by insr and
CC probably occurs via the phosphorylated YXXM motifs (By similarity).
CC {ECO:0000250|UniProtKB:P35568, ECO:0000250|UniProtKB:Q91615}.
CC -!- PTM: Phosphorylation of Tyr-785 is required for grb2-binding.
CC {ECO:0000250}.
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DR AlphaFoldDB; P84770; -.
DR SMR; P84770; -.
DR IntAct; P84770; 1.
DR Proteomes; UP000186698; Genome assembly.
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; ISS: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 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 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..1088
FT /note="Insulin receptor substrate 1-B"
FT /evidence="ECO:0000305"
FT /id="PRO_0000223525"
FT DOMAIN 15..117
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 155..259
FT /note="IRS-type PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT REGION 259..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..787
FT /note="GRB2-binding"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT REGION 840..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 460..463
FT /note="YXXM motif 1"
FT /evidence="ECO:0000255"
FT MOTIF 521..524
FT /note="YXXM motif 2"
FT /evidence="ECO:0000255"
FT MOTIF 567..570
FT /note="YXXM motif 3"
FT /evidence="ECO:0000255"
FT MOTIF 584..587
FT /note="YXXM motif 4"
FT /evidence="ECO:0000255"
FT MOTIF 612..615
FT /note="YXXM motif 5"
FT /evidence="ECO:0000255"
FT MOTIF 654..657
FT /note="YXXM motif 6"
FT /evidence="ECO:0000255"
FT MOTIF 823..826
FT /note="YXXM motif 7"
FT /evidence="ECO:0000255"
FT MOTIF 875..878
FT /note="YXXM motif 8"
FT /evidence="ECO:0000255"
FT MOTIF 909..912
FT /note="YXXM motif 9"
FT /evidence="ECO:0000255"
FT COMPBIAS 261..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35568"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35570"
FT MOD_RES 460
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 567
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 584
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 612
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35568"
FT MOD_RES 785
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 823
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 875
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 1037
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
FT MOD_RES 1069
FT /note="Phosphotyrosine; by INSR"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1088 AA; 119106 MW; 1D656F5849D39B34 CRC64;
MASPTDPQAQ ENFSDVRKVG YLRKPKSMHK RFFVLRAASE SSLARLEYYE NEKKWRHKSG
APKRSIPLES CFNINKRADS KNKHLVALYT KDECFAIAAE CEQEQEGWYQ ALVDLHNRGK
THHQHHNHDG AVNGVHDGLN GDEVYGEVTP PGLAFKEVWQ VIMKPKGLGQ LKNLVGIYRL
CLTNRTISLV KLNSDAAAVV LQLMNIRRCG HSENFFFIEV GRSAVTGAGE FWMQVDDSVV
AQNMHETILE AMKALSDEFR PRSKSQSSSN CSNPISVPLR RHHLNHPPPS QVGLNRRART
ESATATSPAG GAAKHGSSSF RVRASSDGEG TMSRPASMEG SPVSPSASRT QSHRHRGSSR
LHPPLNHSRS IPMPATRCSP SATSPVSLSS SSTSGHGSTS DCMCPRRSSA SISGSPSDGG
FISSDEYGSS PCDFRSSFRS VTPDSMGHTP PAREEELNNY ICMGKSSSHL QRGPQQRYQP
SRGEELTDFD KVFRKRTHSS GTSPPTVSHQ KTPSQSSIEE YTEMMPTHPV RLTSFRHSAF
VPTYSYPEEC LDLHLEGSRA NHKDDGYMPM SPGVAPVSTK TNDYMPMSPK SVSAPQQIIN
PRWHSAVDSN GYMMMSPSGS CSPDNTNYSK IWTNGTNPKL SIDSIEGKLP CSDYINMSPA
SGSTTSTPPD SYLNSVEEST KPVYSYFSLP RSFKHVHRKS EDGNLRISAN SGHNLYTEDS
SSSSTSSDSL GGQDPQQPRK GEGCIQGKRL TRPTRLSLEN SSKASTLPRV REPALPPEPK
SPGEYVNIEF NDKVFSGGLV PSMCSLPFVQ SRVVPQRENL SEYMNMDLGV WRAKTSYAST
SSYEPPNKPV NSVCPTETCS SSRPPIRGKP ISRDYMSMQL GSLCPDYSQV PPTRLSAKSI
TLSSSKSNYA EMSSGRVSDN IPAIAPASNS SLSEASRSSL LGQGSGPSAF TRVSLSPNRN
PSAKVIRAGD PQGRRRHSSE TFSSTPTTAR VTTGPVSGED VKRHSSASFE NVWLRPGEIA
RRDSLQPSDH THNGLNYIDL DLAKDLSSLD HCNSHQSGVS HPSDDLSPYA SITFHKLEEH
RSQAETEE
