FRS3_MOUSE
ID FRS3_MOUSE Reviewed; 492 AA.
AC Q91WJ0;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Fibroblast growth factor receptor substrate 3;
DE Short=FGFR substrate 3;
DE AltName: Full=FRS2-beta;
GN Name=Frs3; Synonyms=Frs2b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=12688531; DOI=10.1023/a:1022231426309;
RA Zhou L., McDougall K., Kubu C.J., Verdi J.M., Meakin S.O.;
RT "Genomic organization and comparative sequence analysis of the mouse and
RT human FRS2, FRS3 genes.";
RL Mol. Biol. Rep. 30:15-25(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH FGFR1 AND NTRK1.
RX PubMed=10629055; DOI=10.1128/mcb.20.3.979-989.2000;
RA Ong S.-H., Guy G.R., Hadari Y.R., Laks S., Gotoh N., Schlessinger J.,
RA Lax I.;
RT "FRS2 proteins recruit intracellular signaling pathways by binding to
RT diverse targets on fibroblast growth factor and nerve growth factor
RT receptors.";
RL Mol. Cell. Biol. 20:979-989(2000).
RN [4]
RP PHOSPHORYLATION BY ULK2.
RX PubMed=16887332; DOI=10.1016/j.cellsig.2006.06.003;
RA Avery A.W., Figueroa C., Vojtek A.B.;
RT "UNC-51-like kinase regulation of fibroblast growth factor receptor
RT substrate 2/3.";
RL Cell. Signal. 19:177-184(2007).
CC -!- FUNCTION: Adapter protein that links FGF and NGF receptors to
CC downstream signaling pathways. Involved in the activation of MAP
CC kinases. Down-regulates ERK2 signaling by interfering with the
CC phosphorylation and nuclear translocation of ERK2.
CC -!- SUBUNIT: Binds NGFR, GRB2, PTPN11 and ERK2 (By similarity). Binds FGFR1
CC and NTRK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
CC -!- PTM: Phosphorylated on tyrosine residues upon stimulation by BFGF or
CC NGFB. Phosphorylated by ULK2 in vitro. {ECO:0000269|PubMed:16887332}.
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DR EMBL; AF456480; AAO15529.1; -; Genomic_DNA.
DR EMBL; BC014819; AAH14819.1; -; mRNA.
DR CCDS; CCDS28854.1; -.
DR RefSeq; NP_659188.1; NM_144939.2.
DR RefSeq; XP_006523531.1; XM_006523468.1.
DR RefSeq; XP_006523532.1; XM_006523469.3.
DR AlphaFoldDB; Q91WJ0; -.
DR SMR; Q91WJ0; -.
DR BioGRID; 223728; 1.
DR IntAct; Q91WJ0; 1.
DR STRING; 10090.ENSMUSP00000108921; -.
DR iPTMnet; Q91WJ0; -.
DR PhosphoSitePlus; Q91WJ0; -.
DR MaxQB; Q91WJ0; -.
DR PaxDb; Q91WJ0; -.
DR PeptideAtlas; Q91WJ0; -.
DR PRIDE; Q91WJ0; -.
DR ProteomicsDB; 271607; -.
DR Antibodypedia; 30086; 218 antibodies from 27 providers.
DR DNASU; 107971; -.
DR Ensembl; ENSMUST00000113296; ENSMUSP00000108921; ENSMUSG00000023266.
DR GeneID; 107971; -.
DR KEGG; mmu:107971; -.
DR UCSC; uc008cvz.1; mouse.
DR CTD; 10817; -.
DR MGI; MGI:2135965; Frs3.
DR VEuPathDB; HostDB:ENSMUSG00000023266; -.
DR eggNOG; KOG4047; Eukaryota.
DR GeneTree; ENSGT00940000159495; -.
DR HOGENOM; CLU_022374_0_0_1; -.
DR InParanoid; Q91WJ0; -.
DR OMA; CQPDRGG; -.
DR OrthoDB; 473504at2759; -.
DR PhylomeDB; Q91WJ0; -.
DR TreeFam; TF324994; -.
DR Reactome; R-MMU-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-MMU-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-MMU-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-MMU-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR BioGRID-ORCS; 107971; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Frs3; mouse.
DR PRO; PR:Q91WJ0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q91WJ0; protein.
DR Bgee; ENSMUSG00000023266; Expressed in retinal neural layer and 154 other tissues.
DR ExpressionAtlas; Q91WJ0; baseline and differential.
DR Genevisible; Q91WJ0; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005104; F:fibroblast growth factor receptor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IBA:GO_Central.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd01202; PTB_FRS2; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR038742; FRS2_PTB.
DR InterPro; IPR002404; IRS_PTB.
DR InterPro; IPR011993; PH-like_dom_sf.
DR Pfam; PF02174; IRS; 1.
DR SMART; SM00310; PTBI; 1.
DR PROSITE; PS51064; IRS_PTB; 1.
PE 1: Evidence at protein level;
KW Lipoprotein; Membrane; Myristate; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..492
FT /note="Fibroblast growth factor receptor substrate 3"
FT /id="PRO_0000087347"
FT DOMAIN 13..115
FT /note="IRS-type PTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT REGION 122..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 492 AA; 53976 MW; C0A895B9173394E6 CRC64;
MGSCWSCLDR DSVPHNHPTK FKVTNVDDEG VELGSGVMEL TQSELVLHLH QREAVRWPYL
CLRRYGYDSN LFSFESGRRC QTGQGIFAFK CSRAEDIFNL LQDLMQCNSI NVTEEPVIIT
RSSHPPELDL PRGPPQPAGY TVSGFSNGFP GCPGEGPRFS SAPRRPSTSS LRHPSPGEES
THTLIASEEQ SHTYVNTPTG DEDGRSRHCL QPLPEGRVPL PAQTQGSDQR DPQVLLQPGQ
VKFVLGPTPA RRQVMKCQSL CPGMQDPPHH NNNEGPSECP AQPKCTYENV SGGLQQGAGW
RLSPEERGWS GLAHRRAALL HYENLPPLPP VWESQGQQPG GEAGDDGDSR DGLTPSSNGF
PDGEEDETPL QKPTSTRASA RSHSGFPVPL TRRRGSPRVF NFDFRRQGPE PPRQLNYIQV
ELKGWGTARP KGPQNPSVSG APGPTPHPVR SSDSYAVIDL KKTAAMSDLQ RALPRDDGAV
RKTRHNSTDL PL
