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Fibroblast growth factor receptor 2 (FGFR-2) (EC 2.7.10.1) (Keratinocyte growth factor receptor) (KGFR) (CD antigen CD332)

 FGFR2_MOUSE             Reviewed;         821 AA.
P21803; O55141; Q00389; Q61342;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 4.
25-OCT-2017, entry version 173.
RecName: Full=Fibroblast growth factor receptor 2;
Short=FGFR-2;
EC=2.7.10.1;
AltName: Full=Keratinocyte growth factor receptor;
Short=KGFR;
AltName: CD_antigen=CD332;
Flags: Precursor;
Name=Fgfr2; Synonyms=Bek, Ect1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=1711190;
Raz V., Kelman Z., Avivi A., Neufeld G., Givol D., Yarden Y.;
"PCR-based identification of new receptors: molecular cloning of a
receptor for fibroblast growth factors.";
Oncogene 6:753-760(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
PubMed=1846048; DOI=10.1126/science.1846048;
Miki T., Fleming T.P., Bottaro D.P., Rubin J.S., Ron D.,
Aaronson S.A.;
"Expression cDNA cloning of the KGF receptor by creation of a
transforming autocrine loop.";
Science 251:72-75(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Brain, and Liver;
PubMed=1373495; DOI=10.1073/pnas.89.8.3305;
Mansukhani A., Dell'Era P., Moscatelli D., Kornbluth S., Hanafusa H.,
Basilico C.;
"Characterization of the murine BEK fibroblast growth factor (FGF)
receptor: activation by three members of the FGF family and
requirement for heparin.";
Proc. Natl. Acad. Sci. U.S.A. 89:3305-3309(1992).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
PubMed=9499422; DOI=10.1093/hmg/7.4.685;
Twigg S.R.F., Burns H.D., Oldridge M., Heath J.K., Wilkie A.O.M.;
"Conserved use of a non-canonical 5' splice site (/GA) in alternative
splicing by fibroblast growth factor receptors 1, 2 and 3.";
Hum. Mol. Genet. 7:685-691(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 477-821.
TISSUE=Liver;
PubMed=2468999; DOI=10.1128/MCB.8.12.5541;
Kornbluth S., Paulson K.E., Hanafusa H.;
"Novel tyrosine kinase identified by phosphotyrosine antibody
screening of cDNA libraries.";
Mol. Cell. Biol. 8:5541-5544(1988).
[6]
FUNCTION.
PubMed=8393815; DOI=10.1006/dbio.1993.1205;
Orr-Urtreger A., Bedford M.T., Burakova T., Arman E., Zimmer Y.,
Yayon A., Givol D., Lonai P.;
"Developmental localization of the splicing alternatives of fibroblast
growth factor receptor-2 (FGFR2).";
Dev. Biol. 158:475-486(1993).
[7]
INTERACTION WITH FGF1; FGF2; FGF3; FGF4; FGF6; FGF7 AND FGF9, AND
FUNCTION IN CELL PROLIFERATION.
PubMed=8663044; DOI=10.1074/jbc.271.25.15292;
Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A.,
Coulier F., Gao G., Goldfarb M.;
"Receptor specificity of the fibroblast growth factor family.";
J. Biol. Chem. 271:15292-15297(1996).
[8]
DISRUPTION PHENOTYPE.
PubMed=9435295;
Xu X., Weinstein M., Li C., Naski M., Cohen R.I., Ornitz D.M.,
Leder P., Deng C.;
"Fibroblast growth factor receptor 2 (FGFR2)-mediated reciprocal
regulation loop between FGF8 and FGF10 is essential for limb
induction.";
Development 125:753-765(1998).
[9]
DISRUPTION PHENOTYPE.
PubMed=9560232; DOI=10.1073/pnas.95.9.5082;
Arman E., Haffner-Krausz R., Chen Y., Heath J.K., Lonai P.;
"Targeted disruption of fibroblast growth factor (FGF) receptor 2
suggests a role for FGF signaling in pregastrulation mammalian
development.";
Proc. Natl. Acad. Sci. U.S.A. 95:5082-5087(1998).
[10]
DISRUPTION PHENOTYPE.
PubMed=10518547; DOI=10.1073/pnas.96.21.11895;
Arman E., Haffner-Krausz R., Gorivodsky M., Lonai P.;
"Fgfr2 is required for limb outgrowth and lung-branching
morphogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 96:11895-11899(1999).
[11]
FUNCTION.
PubMed=10851026; DOI=10.1083/jcb.149.6.1297;
Mansukhani A., Bellosta P., Sahni M., Basilico C.;
"Signaling by fibroblast growth factors (FGF) and fibroblast growth
factor receptor 2 (FGFR2)-activating mutations blocks mineralization
and induces apoptosis in osteoblasts.";
J. Cell Biol. 149:1297-1308(2000).
[12]
DISRUPTION PHENOTYPE.
PubMed=12135917;
Eswarakumar V.P., Monsonego-Ornan E., Pines M., Antonopoulou I.,
Morriss-Kay G.M., Lonai P.;
"The IIIc alternative of Fgfr2 is a positive regulator of bone
formation.";
Development 129:3783-3793(2002).
[13]
FUNCTION IN CELL PROLIFERATION AND ACTIVATION OF SIGNALING PATHWAYS,
MUTAGENESIS OF TYR-769, PHOSPHORYLATION AT TYR-769, AND INTERACTION
WITH PLCG1.
PubMed=15629145; DOI=10.1016/j.bbrc.2004.12.031;
Ceridono M., Belleudi F., Ceccarelli S., Torrisi M.R.;
"Tyrosine 769 of the keratinocyte growth factor receptor is required
for receptor signaling but not endocytosis.";
Biochem. Biophys. Res. Commun. 327:523-532(2005).
[14]
INTERACTION WITH FLRT2.
PubMed=21765038; DOI=10.1177/0022034511415272;
Wei K., Xu Y., Tse H., Manolson M.F., Gong S.G.;
"Mouse FLRT2 interacts with the extracellular and intracellular
regions of FGFR2.";
J. Dent. Res. 90:1234-1239(2011).
-!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface
receptor for fibroblast growth factors and plays an essential role
in the regulation of cell proliferation, differentiation,
migration and apoptosis, and in the regulation of embryonic
development. Required for normal embryonic patterning, trophoblast
function, limb bud development, lung morphogenesis, osteogenesis
and skin development. Plays an essential role in the regulation of
osteoblast differentiation, proliferation and apoptosis, and is
required for normal skeleton development. Promotes cell
proliferation in keratinocytes and immature osteoblasts, but
promotes apoptosis in differentiated osteoblasts. Phosphorylates
PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of
several signaling cascades. Activation of PLCG1 leads to the
production of the cellular signaling molecules diacylglycerol and
inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers
recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates
activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase
signaling pathway, as well as of the AKT1 signaling pathway. FGFR2
signaling is down-regulated by ubiquitination, internalization and
degradation. Mutations that lead to constitutive kinase activation
or impair normal FGFR2 maturation, internalization and degradation
lead to aberrant signaling. Over-expressed FGFR2 promotes
activation of STAT1. {ECO:0000269|PubMed:10851026,
ECO:0000269|PubMed:15629145, ECO:0000269|PubMed:8393815,
ECO:0000269|PubMed:8663044}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Present in an inactive conformation in the
absence of bound ligand. Ligand binding leads to dimerization and
activation by autophosphorylation on tyrosine residues (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Monomer. Homodimer after ligand binding. Interacts
predominantly with FGF1 and FGF2, but can also interact with FGF3,
FGF4, FGF6, FGF7, FGF8, FGF9, FGF10, FGF17, FGF18 and FGF22 (in
vitro) (PubMed:8663044). Ligand specificity is determined by
tissue-specific expression of isoforms, and differences in the
third Ig-like domain are crucial for ligand specificity. Affinity
for fibroblast growth factors (FGFs) is increased by heparan
sulfate glycosaminoglycans that function as coreceptors. Likewise,
KLB increases the affinity for FGF19 and FGF21. Interacts with
PLCG1 (PubMed:15629145). Interacts with GRB2 and PAK4 (By
similarity). Interacts with FLRT2 (PubMed:21765038).
{ECO:0000250|UniProtKB:P21802, ECO:0000269|PubMed:15629145,
ECO:0000269|PubMed:21765038, ECO:0000269|PubMed:8663044}.
-!- INTERACTION:
P13595:Ncam1; NbExp=2; IntAct=EBI-6286942, EBI-774943;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle
{ECO:0000250}. Note=Detected on osteoblast plasma membrane lipid
rafts. After ligand binding, the activated receptor is rapidly
internalized and degraded (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P21803-1; Sequence=Displayed;
Name=Short;
IsoId=P21803-2; Sequence=VSP_002985, VSP_002986, VSP_002987;
-!- DOMAIN: The second and third Ig-like domains directly interact
with fibroblast growth factors (FGF) and heparan sulfate
proteoglycans. Alternative splicing events affecting the third Ig-
like domain are crucial for ligand selectivity (By similarity).
{ECO:0000250}.
-!- PTM: Autophosphorylated. Binding of FGF family members together
with heparan sulfate proteoglycan or heparin promotes receptor
dimerization and autophosphorylation on tyrosine residues.
Autophosphorylation occurs in trans between the two FGFR molecules
present in the dimer (By similarity). {ECO:0000250}.
-!- PTM: N-glycosylated in the endoplasmic reticulum. The N-glycan
chains undergo further maturation to an Endo H-resistant form in
the Golgi apparatus (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated. FGFR2 is rapidly ubiquitinated after
autophosphorylation, leading to internalization and degradation.
Subject to degradation both in lysosomes and by the proteasome (By
similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality shortly after
implantation, due to trophoblast defects, absence of a functional
placenta, failure of limb bud formation, plus defects in lung
branching and heart development. {ECO:0000269|PubMed:10518547,
ECO:0000269|PubMed:12135917, ECO:0000269|PubMed:9435295,
ECO:0000269|PubMed:9560232}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Fibroblast growth factor receptor subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
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EMBL; X55441; CAA39083.1; -; mRNA.
EMBL; M63503; AAA39377.1; -; mRNA.
EMBL; M86441; AAA37286.1; -; mRNA.
EMBL; Y16152; CAA76098.1; -; Genomic_DNA.
EMBL; Y16167; CAA76099.1; -; Genomic_DNA.
EMBL; M23362; AAA37285.1; -; mRNA.
PIR; A38429; A38429.
PIR; A44142; TVMSBK.
PIR; S17295; S17295.
RefSeq; NP_034337.2; NM_010207.2.
RefSeq; NP_963895.2; NM_201601.2.
UniGene; Mm.16340; -.
PDB; 4HWU; X-ray; 2.90 A; A/B=45-127.
PDBsum; 4HWU; -.
ProteinModelPortal; P21803; -.
SMR; P21803; -.
BioGrid; 199657; 2.
DIP; DIP-6038N; -.
IntAct; P21803; 2.
STRING; 10090.ENSMUSP00000112430; -.
ChEMBL; CHEMBL2111391; -.
iPTMnet; P21803; -.
PhosphoSitePlus; P21803; -.
MaxQB; P21803; -.
PaxDb; P21803; -.
PRIDE; P21803; -.
GeneID; 14183; -.
KEGG; mmu:14183; -.
CTD; 2263; -.
MGI; MGI:95523; Fgfr2.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
HOGENOM; HOG000263410; -.
HOVERGEN; HBG000345; -.
InParanoid; P21803; -.
KO; K05093; -.
PhylomeDB; P21803; -.
BRENDA; 2.7.10.1; 3474.
ChiTaRS; Fgfr2; mouse.
PRO; PR:P21803; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_FGFR2; -.
GO; GO:0005938; C:cell cortex; ISO:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0060076; C:excitatory synapse; IMP:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:MGI.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0017134; F:fibroblast growth factor binding; IDA:MGI.
GO; GO:0005007; F:fibroblast growth factor-activated receptor activity; ISO:MGI.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0001525; P:angiogenesis; IGI:MGI.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007409; P:axonogenesis; IMP:MGI.
GO; GO:0060348; P:bone development; IMP:MGI.
GO; GO:0030282; P:bone mineralization; IMP:MGI.
GO; GO:0060349; P:bone morphogenesis; IMP:MGI.
GO; GO:0060667; P:branch elongation involved in salivary gland morphogenesis; IMP:MGI.
GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IMP:MGI.
GO; GO:0060442; P:branching involved in prostate gland morphogenesis; IMP:MGI.
GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IMP:MGI.
GO; GO:0048755; P:branching morphogenesis of a nerve; IMP:MGI.
GO; GO:0060449; P:bud elongation involved in lung branching; IMP:MGI.
GO; GO:0045165; P:cell fate commitment; IDA:MGI.
GO; GO:0007267; P:cell-cell signaling; IMP:MGI.
GO; GO:0060365; P:coronal suture morphogenesis; IMP:MGI.
GO; GO:0048565; P:digestive tract development; IMP:MGI.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISO:MGI.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:MGI.
GO; GO:0048568; P:embryonic organ development; IMP:MGI.
GO; GO:0048562; P:embryonic organ morphogenesis; IMP:MGI.
GO; GO:0009880; P:embryonic pattern specification; IMP:MGI.
GO; GO:0061031; P:endodermal digestive tract morphogenesis; IMP:MGI.
GO; GO:0048730; P:epidermis morphogenesis; IMP:MGI.
GO; GO:0030855; P:epithelial cell differentiation; IMP:MGI.
GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
GO; GO:0060664; P:epithelial cell proliferation involved in salivary gland morphogenesis; IMP:MGI.
GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IMP:MGI.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:MGI.
GO; GO:0035603; P:fibroblast growth factor receptor signaling pathway involved in hemopoiesis; IMP:UniProtKB.
GO; GO:0060595; P:fibroblast growth factor receptor signaling pathway involved in mammary gland specification; IMP:MGI.
GO; GO:0035602; P:fibroblast growth factor receptor signaling pathway involved in negative regulation of apoptotic process in bone marrow; IMP:UniProtKB.
GO; GO:0035607; P:fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development; IMP:UniProtKB.
GO; GO:0035604; P:fibroblast growth factor receptor signaling pathway involved in positive regulation of cell proliferation in bone marrow; IMP:UniProtKB.
GO; GO:0022612; P:gland morphogenesis; IMP:MGI.
GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
GO; GO:0032808; P:lacrimal gland development; IMP:MGI.
GO; GO:0060601; P:lateral sprouting from an epithelium; IMP:MGI.
GO; GO:0070307; P:lens fiber cell development; IMP:MGI.
GO; GO:0060174; P:limb bud formation; IMP:MGI.
GO; GO:0048286; P:lung alveolus development; IMP:MGI.
GO; GO:0030324; P:lung development; IMP:MGI.
GO; GO:0060463; P:lung lobe morphogenesis; IMP:MGI.
GO; GO:0060484; P:lung-associated mesenchyme development; IMP:MGI.
GO; GO:0060615; P:mammary gland bud formation; IMP:MGI.
GO; GO:0003149; P:membranous septum morphogenesis; IMP:MGI.
GO; GO:0048762; P:mesenchymal cell differentiation; IGI:MGI.
GO; GO:0060915; P:mesenchymal cell differentiation involved in lung development; IGI:MGI.
GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; IMP:MGI.
GO; GO:0030901; P:midbrain development; IGI:MGI.
GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IGI:MGI.
GO; GO:0045839; P:negative regulation of mitotic nuclear division; IGI:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
GO; GO:0042476; P:odontogenesis; IMP:MGI.
GO; GO:0021769; P:orbitofrontal cortex development; IMP:UniProtKB.
GO; GO:0035265; P:organ growth; IMP:MGI.
GO; GO:0030916; P:otic vesicle formation; IMP:MGI.
GO; GO:0003148; P:outflow tract septum morphogenesis; IMP:MGI.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:MGI.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IGI:MGI.
GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB.
GO; GO:0051781; P:positive regulation of cell division; IMP:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IGI:MGI.
GO; GO:0060501; P:positive regulation of epithelial cell proliferation involved in lung morphogenesis; IMP:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IGI:MGI.
GO; GO:0010518; P:positive regulation of phospholipase activity; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:MGI.
GO; GO:0009791; P:post-embryonic development; IMP:MGI.
GO; GO:0060527; P:prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis; IMP:MGI.
GO; GO:0060523; P:prostate epithelial cord elongation; IMP:MGI.
GO; GO:0060512; P:prostate gland morphogenesis; IMP:MGI.
GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
GO; GO:0021860; P:pyramidal neuron development; IMP:UniProtKB.
GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; IMP:MGI.
GO; GO:0010453; P:regulation of cell fate commitment; IMP:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:MGI.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IMP:MGI.
GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; IMP:MGI.
GO; GO:0060688; P:regulation of morphogenesis of a branching structure; IMP:MGI.
GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
GO; GO:0051150; P:regulation of smooth muscle cell differentiation; IMP:MGI.
GO; GO:0008589; P:regulation of smoothened signaling pathway; IMP:MGI.
GO; GO:0048608; P:reproductive structure development; IMP:MGI.
GO; GO:0060529; P:squamous basal epithelial stem cell differentiation involved in prostate gland acinus development; IMP:MGI.
GO; GO:0048489; P:synaptic vesicle transport; IMP:MGI.
GO; GO:0001657; P:ureteric bud development; IGI:MGI.
GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; TAS:DFLAT.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:MGI.
GO; GO:0021847; P:ventricular zone neuroblast division; IMP:UniProtKB.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR016248; FGF_rcpt_fam.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07679; I-set; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF000628; FGFR; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 3.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 3.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50835; IG_LIKE; 3.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; ATP-binding;
Cell membrane; Complete proteome; Cytoplasmic vesicle; Disulfide bond;
Glycoprotein; Golgi apparatus; Heparin-binding; Immunoglobulin domain;
Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Proto-oncogene;
Receptor; Reference proteome; Repeat; Signal; Transferase;
Transmembrane; Transmembrane helix; Tyrosine-protein kinase;
Ubl conjugation.
SIGNAL 1 21
CHAIN 22 821 Fibroblast growth factor receptor 2.
/FTId=PRO_0000016784.
TOPO_DOM 22 377 Extracellular. {ECO:0000255}.
TRANSMEM 378 398 Helical. {ECO:0000255}.
TOPO_DOM 399 821 Cytoplasmic. {ECO:0000255}.
DOMAIN 25 125 Ig-like C2-type 1.
DOMAIN 154 247 Ig-like C2-type 2.
DOMAIN 256 358 Ig-like C2-type 3.
DOMAIN 481 770 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 487 495 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 565 567 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 161 178 Heparin-binding. {ECO:0000250}.
ACT_SITE 626 626 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 517 517 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 571 571 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 466 466 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P21802}.
MOD_RES 586 586 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P21802}.
MOD_RES 588 588 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P21802}.
MOD_RES 656 656 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P21802}.
MOD_RES 657 657 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P21802}.
MOD_RES 769 769 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P21802}.
MOD_RES 780 780 Phosphoserine.
{ECO:0000250|UniProtKB:P21802}.
CARBOHYD 83 83 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 147 147 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 228 228 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 265 265 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 297 297 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 318 318 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 331 331 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 62 107 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 179 231 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 278 342 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 37 37 E -> G (in isoform Short).
{ECO:0000303|PubMed:1846048}.
/FTId=VSP_002985.
VAR_SEQ 38 152 Missing (in isoform Short).
{ECO:0000303|PubMed:1846048}.
/FTId=VSP_002986.
VAR_SEQ 314 361 AAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHS
AWLTVLP -> HSGINSSNAEVLALFNVTEMDAGEYICKVS
NYIGQANQSAWLTVLPKQQ (in isoform Short).
{ECO:0000303|PubMed:1846048}.
/FTId=VSP_002987.
MUTAGEN 769 769 Y->F: Abolishes phosphorylation of FRS2
and activation of MAP kinases.
{ECO:0000269|PubMed:15629145}.
CONFLICT 53 53 A -> V (in Ref. 1; CAA39083).
{ECO:0000305}.
CONFLICT 55 56 GE -> RG (in Ref. 1; CAA39083).
{ECO:0000305}.
CONFLICT 90 90 E -> R (in Ref. 1; CAA39083).
{ECO:0000305}.
CONFLICT 119 119 I -> Y (in Ref. 1; CAA39083).
{ECO:0000305}.
CONFLICT 142 143 DV -> R (in Ref. 1; CAA39083).
{ECO:0000305}.
CONFLICT 169 169 C -> V (in Ref. 1; CAA39083 and 2;
AAA39377). {ECO:0000305}.
CONFLICT 187 187 S -> P (in Ref. 1; CAA39083 and 2;
AAA39377). {ECO:0000305}.
CONFLICT 214 214 W -> R (in Ref. 1; CAA39083).
{ECO:0000305}.
CONFLICT 229 229 Y -> I (in Ref. 1; CAA39083).
{ECO:0000305}.
CONFLICT 275 275 E -> R (in Ref. 1; CAA39083).
{ECO:0000305}.
CONFLICT 301 301 N -> Y (in Ref. 1; CAA39083 and 2;
AAA39377). {ECO:0000305}.
STRAND 48 52 {ECO:0000244|PDB:4HWU}.
STRAND 58 61 {ECO:0000244|PDB:4HWU}.
STRAND 69 74 {ECO:0000244|PDB:4HWU}.
STRAND 77 79 {ECO:0000244|PDB:4HWU}.
STRAND 83 88 {ECO:0000244|PDB:4HWU}.
STRAND 91 94 {ECO:0000244|PDB:4HWU}.
HELIX 99 101 {ECO:0000244|PDB:4HWU}.
STRAND 103 110 {ECO:0000244|PDB:4HWU}.
STRAND 115 124 {ECO:0000244|PDB:4HWU}.
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


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