ID   FRS3_RAT                Reviewed;         492 AA.
AC   Q52RG8;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Fibroblast growth factor receptor substrate 3;
DE            Short=FGFR substrate 3;
DE   AltName: Full=FGFR-signaling adaptor SNT2;
DE   AltName: Full=Suc1-associated neurotrophic factor target 2;
DE            Short=SNT-2;
GN   Name=Frs3; Synonyms=Snt2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Testis;
RA   Cotton L.M., Gibbs G.M., Morrison J.R., de Kretser D.M., O'Bryan M.K.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Binds NTRK1, FGFR1, NGFR, GRB2, PTPN11 and ERK2.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated on tyrosine residues upon stimulation by BFGF or
CC       NGFB. {ECO:0000250}.
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DR   EMBL; AY972083; AAX84972.1; -; mRNA.
DR   RefSeq; NP_001017382.1; NM_001017382.1.
DR   AlphaFoldDB; Q52RG8; -.
DR   SMR; Q52RG8; -.
DR   STRING; 10116.ENSRNOP00000019404; -.
DR   PaxDb; Q52RG8; -.
DR   GeneID; 316213; -.
DR   KEGG; rno:316213; -.
DR   UCSC; RGD:1310226; rat.
DR   CTD; 10817; -.
DR   RGD; 1310226; Frs3.
DR   eggNOG; KOG4047; Eukaryota.
DR   InParanoid; Q52RG8; -.
DR   PhylomeDB; Q52RG8; -.
DR   Reactome; R-RNO-5654693; FRS-mediated FGFR1 signaling.
DR   Reactome; R-RNO-5654700; FRS-mediated FGFR2 signaling.
DR   Reactome; R-RNO-5654706; FRS-mediated FGFR3 signaling.
DR   Reactome; R-RNO-5654712; FRS-mediated FGFR4 signaling.
DR   Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-RNO-9696270; RND2 GTPase cycle.
DR   Reactome; R-RNO-9696273; RND1 GTPase cycle.
DR   PRO; PR:Q52RG8; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005104; F:fibroblast growth factor receptor binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
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:RGD.
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   2: Evidence at transcript 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_0000087348"
FT   DOMAIN          13..115
FT                   /note="IRS-type PTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00389"
FT   REGION          125..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          425..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..386
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;  54347 MW;  0B93FCF5D4C9485B CRC64;
     MGSCCSCLDR DSVPHNHPTK FKVTNVDDEG VELGSGVMEL TQSELVLHLH QQEAVRWPYL
     CLRRYGYDSN LFSFESGRRC QTGQGIFAFK CSRAEEIFNL LQDLMQCNSI NVTEEPVIIT
     RNSHPQELDL PRGSSQPTGY TVSSFSNGFP GCPGEGPRFS SAPRRPSTSS LRHPSPGEES
     TQTLIASDEQ SHTYVNTPTG EEDRRSRHCL QPLPEGRVPF PPQTQVSDQR DPQVFLQPGQ
     VKFVLGPTPA RRQVMKCQSL CPSMQDPPLH NNNEGPSECP AQPKCTYENV SGGLQQGAGW
     RLSPEERGWS GLAHRRAALL HYENLPPLPP VWESQVQQLR GEAGDDGDSK DGLTPSSNGF
     PDGEEDETPL QKPTSTRASA RSHSSFPVPL TRRRGSPRVF NFDFRRPGPE PPRQLNYIQV
     ELKGWGTAHP KGPQNPSVSG APGPTPHPAR SSDSYAVIDL KKTVAMSNLQ RALPRDDGTV
     RKTRHNSTDL PL