FGFR2_MOUSE
ID FGFR2_MOUSE Reviewed; 821 AA.
AC P21803; O55141; Q00389; Q61342;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 4.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Fibroblast growth factor receptor 2;
DE Short=FGFR-2;
DE EC=2.7.10.1;
DE AltName: Full=Keratinocyte growth factor receptor;
DE Short=KGFR;
DE AltName: CD_antigen=CD332;
DE Flags: Precursor;
GN Name=Fgfr2; Synonyms=Bek, Ect1;
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 [MRNA] (ISOFORM LONG).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=1711190;
RA Raz V., Kelman Z., Avivi A., Neufeld G., Givol D., Yarden Y.;
RT "PCR-based identification of new receptors: molecular cloning of a receptor
RT for fibroblast growth factors.";
RL Oncogene 6:753-760(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX PubMed=1846048; DOI=10.1126/science.1846048;
RA Miki T., Fleming T.P., Bottaro D.P., Rubin J.S., Ron D., Aaronson S.A.;
RT "Expression cDNA cloning of the KGF receptor by creation of a transforming
RT autocrine loop.";
RL Science 251:72-75(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=Brain, and Liver;
RX PubMed=1373495; DOI=10.1073/pnas.89.8.3305;
RA Mansukhani A., Dell'Era P., Moscatelli D., Kornbluth S., Hanafusa H.,
RA Basilico C.;
RT "Characterization of the murine BEK fibroblast growth factor (FGF)
RT receptor: activation by three members of the FGF family and requirement for
RT heparin.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:3305-3309(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
RX PubMed=9499422; DOI=10.1093/hmg/7.4.685;
RA Twigg S.R.F., Burns H.D., Oldridge M., Heath J.K., Wilkie A.O.M.;
RT "Conserved use of a non-canonical 5' splice site (/GA) in alternative
RT splicing by fibroblast growth factor receptors 1, 2 and 3.";
RL Hum. Mol. Genet. 7:685-691(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 477-821.
RC TISSUE=Liver;
RX PubMed=2468999; DOI=10.1128/mcb.8.12.5541-5544.1988;
RA Kornbluth S., Paulson K.E., Hanafusa H.;
RT "Novel tyrosine kinase identified by phosphotyrosine antibody screening of
RT cDNA libraries.";
RL Mol. Cell. Biol. 8:5541-5544(1988).
RN [6]
RP FUNCTION.
RX PubMed=8393815; DOI=10.1006/dbio.1993.1205;
RA Orr-Urtreger A., Bedford M.T., Burakova T., Arman E., Zimmer Y., Yayon A.,
RA Givol D., Lonai P.;
RT "Developmental localization of the splicing alternatives of fibroblast
RT growth factor receptor-2 (FGFR2).";
RL Dev. Biol. 158:475-486(1993).
RN [7]
RP INTERACTION WITH FGF1; FGF2; FGF3; FGF4; FGF6; FGF7 AND FGF9, AND FUNCTION
RP IN CELL PROLIFERATION.
RX PubMed=8663044; DOI=10.1074/jbc.271.25.15292;
RA Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A., Coulier F.,
RA Gao G., Goldfarb M.;
RT "Receptor specificity of the fibroblast growth factor family.";
RL J. Biol. Chem. 271:15292-15297(1996).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=9435295; DOI=10.1242/dev.125.4.753;
RA Xu X., Weinstein M., Li C., Naski M., Cohen R.I., Ornitz D.M., Leder P.,
RA Deng C.;
RT "Fibroblast growth factor receptor 2 (FGFR2)-mediated reciprocal regulation
RT loop between FGF8 and FGF10 is essential for limb induction.";
RL Development 125:753-765(1998).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=9560232; DOI=10.1073/pnas.95.9.5082;
RA Arman E., Haffner-Krausz R., Chen Y., Heath J.K., Lonai P.;
RT "Targeted disruption of fibroblast growth factor (FGF) receptor 2 suggests
RT a role for FGF signaling in pregastrulation mammalian development.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:5082-5087(1998).
RN [10]
RP DISRUPTION PHENOTYPE.
RX PubMed=10518547; DOI=10.1073/pnas.96.21.11895;
RA Arman E., Haffner-Krausz R., Gorivodsky M., Lonai P.;
RT "Fgfr2 is required for limb outgrowth and lung-branching morphogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11895-11899(1999).
RN [11]
RP FUNCTION.
RX PubMed=10851026; DOI=10.1083/jcb.149.6.1297;
RA Mansukhani A., Bellosta P., Sahni M., Basilico C.;
RT "Signaling by fibroblast growth factors (FGF) and fibroblast growth factor
RT receptor 2 (FGFR2)-activating mutations blocks mineralization and induces
RT apoptosis in osteoblasts.";
RL J. Cell Biol. 149:1297-1308(2000).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=12135917; DOI=10.1242/dev.129.16.3783;
RA Eswarakumar V.P., Monsonego-Ornan E., Pines M., Antonopoulou I.,
RA Morriss-Kay G.M., Lonai P.;
RT "The IIIc alternative of Fgfr2 is a positive regulator of bone formation.";
RL Development 129:3783-3793(2002).
RN [13]
RP FUNCTION IN CELL PROLIFERATION AND ACTIVATION OF SIGNALING PATHWAYS,
RP MUTAGENESIS OF TYR-769, PHOSPHORYLATION AT TYR-769, AND INTERACTION WITH
RP PLCG1.
RX PubMed=15629145; DOI=10.1016/j.bbrc.2004.12.031;
RA Ceridono M., Belleudi F., Ceccarelli S., Torrisi M.R.;
RT "Tyrosine 769 of the keratinocyte growth factor receptor is required for
RT receptor signaling but not endocytosis.";
RL Biochem. Biophys. Res. Commun. 327:523-532(2005).
RN [14]
RP INTERACTION WITH FLRT2.
RX PubMed=21765038; DOI=10.1177/0022034511415272;
RA Wei K., Xu Y., Tse H., Manolson M.F., Gong S.G.;
RT "Mouse FLRT2 interacts with the extracellular and intracellular regions of
RT FGFR2.";
RL J. Dent. Res. 90:1234-1239(2011).
CC -!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor
CC for fibroblast growth factors and plays an essential role in the
CC regulation of cell proliferation, differentiation, migration and
CC apoptosis, and in the regulation of embryonic development. Required for
CC normal embryonic patterning, trophoblast function, limb bud
CC development, lung morphogenesis, osteogenesis and skin development.
CC Plays an essential role in the regulation of osteoblast
CC differentiation, proliferation and apoptosis, and is required for
CC normal skeleton development. Promotes cell proliferation in
CC keratinocytes and immature osteoblasts, but promotes apoptosis in
CC differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand
CC binding leads to the activation of several signaling cascades.
CC Activation of PLCG1 leads to the production of the cellular signaling
CC molecules diacylglycerol and inositol 1,4,5-trisphosphate.
CC Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and
CC SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the
CC MAP kinase signaling pathway, as well as of the AKT1 signaling pathway.
CC FGFR2 signaling is down-regulated by ubiquitination, internalization
CC and degradation. Mutations that lead to constitutive kinase activation
CC or impair normal FGFR2 maturation, internalization and degradation lead
CC to aberrant signaling. Over-expressed FGFR2 promotes activation of
CC STAT1. {ECO:0000269|PubMed:10851026, ECO:0000269|PubMed:15629145,
CC ECO:0000269|PubMed:8393815, ECO:0000269|PubMed:8663044}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence
CC of bound ligand. Ligand binding leads to dimerization and activation by
CC autophosphorylation on tyrosine residues (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Homodimer after ligand binding. Interacts
CC predominantly with FGF1 and FGF2, but can also interact with FGF3,
CC FGF4, FGF6, FGF7, FGF8, FGF9, FGF10, FGF17, FGF18 and FGF22 (in vitro)
CC (PubMed:8663044). Ligand specificity is determined by tissue-specific
CC expression of isoforms, and differences in the third Ig-like domain are
CC crucial for ligand specificity. Affinity for fibroblast growth factors
CC (FGFs) is increased by heparan sulfate glycosaminoglycans that function
CC as coreceptors. Likewise, KLB increases the affinity for FGF19 and
CC FGF21. Interacts with PLCG1 (PubMed:15629145). Interacts with GRB2 and
CC PAK4 (By similarity). Interacts with FLRT2 (PubMed:21765038).
CC {ECO:0000250|UniProtKB:P21802, ECO:0000269|PubMed:15629145,
CC ECO:0000269|PubMed:21765038, ECO:0000269|PubMed:8663044}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle
CC {ECO:0000250}. Note=Detected on osteoblast plasma membrane lipid rafts.
CC After ligand binding, the activated receptor is rapidly internalized
CC and degraded (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P21803-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P21803-2; Sequence=VSP_002985, VSP_002986, VSP_002987;
CC -!- DOMAIN: The second and third Ig-like domains directly interact with
CC fibroblast growth factors (FGF) and heparan sulfate proteoglycans.
CC Alternative splicing events affecting the third Ig-like domain are
CC crucial for ligand selectivity (By similarity). {ECO:0000250}.
CC -!- PTM: Autophosphorylated. Binding of FGF family members together with
CC heparan sulfate proteoglycan or heparin promotes receptor dimerization
CC and autophosphorylation on tyrosine residues. Autophosphorylation
CC occurs in trans between the two FGFR molecules present in the dimer (By
CC similarity). {ECO:0000250}.
CC -!- PTM: N-glycosylated in the endoplasmic reticulum. The N-glycan chains
CC undergo further maturation to an Endo H-resistant form in the Golgi
CC apparatus (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated. FGFR2 is rapidly ubiquitinated after
CC autophosphorylation, leading to internalization and degradation.
CC Subject to degradation both in lysosomes and by the proteasome (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality shortly after implantation,
CC due to trophoblast defects, absence of a functional placenta, failure
CC of limb bud formation, plus defects in lung branching and heart
CC development. {ECO:0000269|PubMed:10518547, ECO:0000269|PubMed:12135917,
CC ECO:0000269|PubMed:9435295, ECO:0000269|PubMed:9560232}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fibroblast growth factor receptor subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X55441; CAA39083.1; -; mRNA.
DR EMBL; M63503; AAA39377.1; -; mRNA.
DR EMBL; M86441; AAA37286.1; -; mRNA.
DR EMBL; Y16152; CAA76098.1; -; Genomic_DNA.
DR EMBL; Y16167; CAA76099.1; -; Genomic_DNA.
DR EMBL; M23362; AAA37285.1; -; mRNA.
DR PIR; A38429; A38429.
DR PIR; A44142; TVMSBK.
DR PIR; S17295; S17295.
DR RefSeq; NP_034337.2; NM_010207.2.
DR RefSeq; NP_963895.2; NM_201601.2.
DR PDB; 4HWU; X-ray; 2.90 A; A/B=45-127.
DR PDBsum; 4HWU; -.
DR AlphaFoldDB; P21803; -.
DR SMR; P21803; -.
DR BioGRID; 199657; 20.
DR DIP; DIP-6038N; -.
DR IntAct; P21803; 2.
DR STRING; 10090.ENSMUSP00000112430; -.
DR ChEMBL; CHEMBL2111391; -.
DR GlyGen; P21803; 9 sites.
DR iPTMnet; P21803; -.
DR PhosphoSitePlus; P21803; -.
DR CPTAC; non-CPTAC-3806; -.
DR jPOST; P21803; -.
DR MaxQB; P21803; -.
DR PaxDb; P21803; -.
DR PRIDE; P21803; -.
DR ProteomicsDB; 271890; -. [P21803-1]
DR ProteomicsDB; 271891; -. [P21803-2]
DR ABCD; P21803; 1 sequenced antibody.
DR DNASU; 14183; -.
DR GeneID; 14183; -.
DR KEGG; mmu:14183; -.
DR CTD; 2263; -.
DR MGI; MGI:95523; Fgfr2.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; P21803; -.
DR OrthoDB; 220433at2759; -.
DR PhylomeDB; P21803; -.
DR BRENDA; 2.7.10.1; 3474.
DR Reactome; R-MMU-109704; PI3K Cascade.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-190375; FGFR2c ligand binding and activation.
DR Reactome; R-MMU-190377; FGFR2b ligand binding and activation.
DR Reactome; R-MMU-5654221; Phospholipase C-mediated cascade, FGFR2.
DR Reactome; R-MMU-5654695; PI-3K cascade:FGFR2.
DR Reactome; R-MMU-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-MMU-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-MMU-5654727; Negative regulation of FGFR2 signaling.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR BioGRID-ORCS; 14183; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Fgfr2; mouse.
DR PRO; PR:P21803; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P21803; protein.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0060076; C:excitatory synapse; IMP:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017134; F:fibroblast growth factor binding; IDA:MGI.
DR GO; GO:0005007; F:fibroblast growth factor receptor activity; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IGI:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR GO; GO:0060348; P:bone development; IMP:MGI.
DR GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR GO; GO:0060349; P:bone morphogenesis; IMP:MGI.
DR GO; GO:0060667; P:branch elongation involved in salivary gland morphogenesis; IMP:MGI.
DR GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IMP:MGI.
DR GO; GO:0060442; P:branching involved in prostate gland morphogenesis; IMP:MGI.
DR GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IMP:MGI.
DR GO; GO:0048755; P:branching morphogenesis of a nerve; IMP:MGI.
DR GO; GO:0060449; P:bud elongation involved in lung branching; IMP:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IGI:MGI.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IGI:MGI.
DR GO; GO:0051301; P:cell division; IMP:MGI.
DR GO; GO:0045165; P:cell fate commitment; IDA:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0007267; P:cell-cell signaling; IMP:MGI.
DR GO; GO:0060365; P:coronal suture morphogenesis; IMP:MGI.
DR GO; GO:0048565; P:digestive tract development; IMP:MGI.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISO:MGI.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:MGI.
DR GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR GO; GO:0048562; P:embryonic organ morphogenesis; IMP:MGI.
DR GO; GO:0009880; P:embryonic pattern specification; IMP:MGI.
DR GO; GO:0061031; P:endodermal digestive tract morphogenesis; IMP:MGI.
DR GO; GO:0048730; P:epidermis morphogenesis; IMP:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0060664; P:epithelial cell proliferation involved in salivary gland morphogenesis; IMP:MGI.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IMP:MGI.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IGI:MGI.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0035603; P:fibroblast growth factor receptor signaling pathway involved in hemopoiesis; IMP:UniProtKB.
DR GO; GO:0060595; P:fibroblast growth factor receptor signaling pathway involved in mammary gland specification; IMP:MGI.
DR GO; GO:0035602; P:fibroblast growth factor receptor signaling pathway involved in negative regulation of apoptotic process in bone marrow cell; IMP:UniProtKB.
DR GO; GO:0035607; P:fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development; IMP:UniProtKB.
DR GO; GO:0035604; P:fibroblast growth factor receptor signaling pathway involved in positive regulation of cell proliferation in bone marrow; IMP:UniProtKB.
DR GO; GO:0022612; P:gland morphogenesis; IMP:MGI.
DR GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0032808; P:lacrimal gland development; IMP:MGI.
DR GO; GO:0060601; P:lateral sprouting from an epithelium; IMP:MGI.
DR GO; GO:0070307; P:lens fiber cell development; IMP:MGI.
DR GO; GO:0060174; P:limb bud formation; IMP:MGI.
DR GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0060463; P:lung lobe morphogenesis; IMP:MGI.
DR GO; GO:0060484; P:lung-associated mesenchyme development; IMP:MGI.
DR GO; GO:0060615; P:mammary gland bud formation; IMP:MGI.
DR GO; GO:0003149; P:membranous septum morphogenesis; IMP:MGI.
DR GO; GO:0048762; P:mesenchymal cell differentiation; IGI:MGI.
DR GO; GO:0060915; P:mesenchymal cell differentiation involved in lung development; IGI:MGI.
DR GO; GO:0010463; P:mesenchymal cell proliferation; IGI:MGI.
DR GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; IMP:MGI.
DR GO; GO:0030901; P:midbrain development; IGI:MGI.
DR GO; GO:0140014; P:mitotic nuclear division; IGI:MGI.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IGI:MGI.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISO:MGI.
DR GO; GO:0045839; P:negative regulation of mitotic nuclear division; IGI:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR GO; GO:0042476; P:odontogenesis; IMP:MGI.
DR GO; GO:0021769; P:orbitofrontal cortex development; IMP:UniProtKB.
DR GO; GO:0035265; P:organ growth; IMP:MGI.
DR GO; GO:0030916; P:otic vesicle formation; IMP:MGI.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; IMP:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IGI:MGI.
DR GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0060501; P:positive regulation of epithelial cell proliferation involved in lung morphogenesis; IMP:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IGI:MGI.
DR GO; GO:0010518; P:positive regulation of phospholipase activity; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:1904677; P:positive regulation of somatic stem cell division; IMP:MGI.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0050677; P:positive regulation of urothelial cell proliferation; IMP:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0060527; P:prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis; IMP:MGI.
DR GO; GO:0060523; P:prostate epithelial cord elongation; IMP:MGI.
DR GO; GO:0060512; P:prostate gland morphogenesis; IMP:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0021860; P:pyramidal neuron development; IMP:UniProtKB.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IMP:MGI.
DR GO; GO:0060688; P:regulation of morphogenesis of a branching structure; IMP:MGI.
DR GO; GO:0033688; P:regulation of osteoblast proliferation; IMP:MGI.
DR GO; GO:0051150; P:regulation of smooth muscle cell differentiation; IMP:MGI.
DR GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP:MGI.
DR GO; GO:0048608; P:reproductive structure development; IMP:MGI.
DR GO; GO:0048103; P:somatic stem cell division; IMP:MGI.
DR GO; GO:0060529; P:squamous basal epithelial stem cell differentiation involved in prostate gland acinus development; IMP:MGI.
DR GO; GO:0048863; P:stem cell differentiation; IGI:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0001657; P:ureteric bud development; IGI:MGI.
DR GO; GO:0050674; P:urothelial cell proliferation; IMP:MGI.
DR GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; TAS:DFLAT.
DR GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:MGI.
DR GO; GO:0021847; P:ventricular zone neuroblast division; IMP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR016248; FGF_rcpt_fam.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000628; FGFR; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; ATP-binding; Cell membrane;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Heparin-binding; Immunoglobulin domain; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Proto-oncogene; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..21
FT CHAIN 22..821
FT /note="Fibroblast growth factor receptor 2"
FT /id="PRO_0000016784"
FT TOPO_DOM 22..377
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..821
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..125
FT /note="Ig-like C2-type 1"
FT DOMAIN 154..247
FT /note="Ig-like C2-type 2"
FT DOMAIN 256..358
FT /note="Ig-like C2-type 3"
FT DOMAIN 481..770
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 129..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..178
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT ACT_SITE 626
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 487..495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 565..567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 571
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 466
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P21802"
FT MOD_RES 586
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P21802"
FT MOD_RES 588
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P21802"
FT MOD_RES 656
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P21802"
FT MOD_RES 657
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P21802"
FT MOD_RES 769
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P21802"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P21802"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 179..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 278..342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 37
FT /note="E -> G (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:1846048"
FT /id="VSP_002985"
FT VAR_SEQ 38..152
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:1846048"
FT /id="VSP_002986"
FT VAR_SEQ 314..361
FT /note="AAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLP ->
FT HSGINSSNAEVLALFNVTEMDAGEYICKVSNYIGQANQSAWLTVLPKQQ (in
FT isoform Short)"
FT /evidence="ECO:0000303|PubMed:1846048"
FT /id="VSP_002987"
FT MUTAGEN 769
FT /note="Y->F: Abolishes phosphorylation of FRS2 and
FT activation of MAP kinases."
FT /evidence="ECO:0000269|PubMed:15629145"
FT CONFLICT 53
FT /note="A -> V (in Ref. 1; CAA39083)"
FT /evidence="ECO:0000305"
FT CONFLICT 55..56
FT /note="GE -> RG (in Ref. 1; CAA39083)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="E -> R (in Ref. 1; CAA39083)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="I -> Y (in Ref. 1; CAA39083)"
FT /evidence="ECO:0000305"
FT CONFLICT 142..143
FT /note="DV -> R (in Ref. 1; CAA39083)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="C -> V (in Ref. 1; CAA39083 and 2; AAA39377)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="S -> P (in Ref. 1; CAA39083 and 2; AAA39377)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="W -> R (in Ref. 1; CAA39083)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="Y -> I (in Ref. 1; CAA39083)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="E -> R (in Ref. 1; CAA39083)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="N -> Y (in Ref. 1; CAA39083 and 2; AAA39377)"
FT /evidence="ECO:0000305"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:4HWU"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:4HWU"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:4HWU"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:4HWU"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:4HWU"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:4HWU"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:4HWU"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:4HWU"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:4HWU"
SQ SEQUENCE 821 AA; 91984 MW; FCDB28ADD61F4414 CRC64;
MVSWGRFICL VLVTMATLSL ARPSFSLVED TTLEPEEPPT KYQISQPEAY VVAPGESLEL
QCMLKDAAVI SWTKDGVHLG PNNRTVLIGE YLQIKGATPR DSGLYACTAA RTVDSETWIF
MVNVTDAISS GDDEDDTDSS EDVVSENRSN QRAPYWTNTE KMEKRLHACP AANTVKFRCP
AGGNPTSTMR WLKNGKEFKQ EHRIGGYKVR NQHWSLIMES VVPSDKGNYT CLVENEYGSI
NHTYHLDVVE RSPHRPILQA GLPANASTVV GGDVEFVCKV YSDAQPHIQW IKHVEKNGSK
NGPDGLPYLK VLKAAGVNTT DKEIEVLYIR NVTFEDAGEY TCLAGNSIGI SFHSAWLTVL
PAPVREKEIT ASPDYLEIAI YCIGVFLIAC MVVTVIFCRM KTTTKKPDFS SQPAVHKLTK
RIPLRRQVTV SAESSSSMNS NTPLVRITTR LSSTADTPML AGVSEYELPE DPKWEFPRDK
LTLGKPLGEG CFGQVVMAEA VGIDKDKPKE AVTVAVKMLK DDATEKDLSD LVSEMEMMKM
IGKHKNIINL LGACTQDGPL YVIVEYASKG NLREYLRARR PPGMEYSYDI NRVPEEQMTF
KDLVSCTYQL ARGMEYLASQ KCIHRDLAAR NVLVTENNVM KIADFGLARD INNIDYYKKT
TNGRLPVKWM APEALFDRVY THQSDVWSFG VLMWEIFTLG GSPYPGIPVE ELFKLLKEGH
RMDKPTNCTN ELYMMMRDCW HAVPSQRPTF KQLVEDLDRI LTLTTNEEYL DLTQPLEQYS
PSYPDTSSSC SSGDDSVFSP DPMPYEPCLP QYPHINGSVK T
