FGFR3_MOUSE
ID FGFR3_MOUSE Reviewed; 801 AA.
AC Q61851; Q61564; Q63834;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Fibroblast growth factor receptor 3;
DE Short=FGFR-3;
DE EC=2.7.10.1;
DE AltName: Full=Heparin-binding growth factor receptor;
DE AltName: CD_antigen=CD333;
DE Flags: Precursor;
GN Name=Fgfr3; Synonyms=Mfr3, Sam3;
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 1).
RX PubMed=1379594; DOI=10.1016/s0021-9258(18)42001-7;
RA Ornitz D.M., Leder P.;
RT "Ligand specificity and heparin dependence of fibroblast growth factor
RT receptors 1 and 3.";
RL J. Biol. Chem. 267:16305-16311(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8382556;
RA Katoh O., Hattori Y., Sasaki H., Sakamoto H., Fujimoto K., Fujii T.,
RA Sugimura T., Terada M.;
RT "Isolation of the complementary DNA encoding a mouse heparin-binding growth
RT factor receptor with the use of a unique kinase insert sequence.";
RL Cancer Res. 53:1136-1141(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 242-364 (ISOFORM 2).
RX PubMed=7512569; DOI=10.1016/s0021-9258(19)78170-8;
RA Chellaiah A.T., McEwen D.G., Werner S., Xu J., Ornitz D.M.;
RT "Fibroblast growth factor receptor (FGFR) 3. Alternative splicing in
RT immunoglobulin-like domain III creates a receptor highly specific for
RT acidic FGF/FGF-1.";
RL J. Biol. Chem. 269:11620-11627(1994).
RN [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=8601314; DOI=10.1016/s0092-8674(00)81069-7;
RA Deng C., Wynshaw-Boris A., Zhou F., Kuo A., Leder P.;
RT "Fibroblast growth factor receptor 3 is a negative regulator of bone
RT growth.";
RL Cell 84:911-921(1996).
RN [5]
RP INTERACTION WITH FGF1; FGF2; FGF4; FGF8 AND FGF9, AND FUNCTION IN CELL
RP 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 [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=8630492; DOI=10.1038/ng0496-390;
RA Colvin J.S., Bohne B.A., Harding G.W., McEwen D.G., Ornitz D.M.;
RT "Skeletal overgrowth and deafness in mice lacking fibroblast growth factor
RT receptor 3.";
RL Nat. Genet. 12:390-397(1996).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=9716527; DOI=10.1242/dev.125.18.3615;
RA Weinstein M., Xu X., Ohyama K., Deng C.X.;
RT "FGFR-3 and FGFR-4 function cooperatively to direct alveogenesis in the
RT murine lung.";
RL Development 125:3615-3623(1998).
RN [8]
RP FUNCTION AS FGF2 RECEPTOR AND IN PHOSPHORYLATION OF CBL, UBIQUITINATION,
RP PHOSPHORYLATION, ACTIVITY REGULATION, AND MUTAGENESIS OF 644.
RX PubMed=14699054; DOI=10.1073/pnas.2237184100;
RA Cho J.Y., Guo C., Torello M., Lunstrum G.P., Iwata T., Deng C.,
RA Horton W.A.;
RT "Defective lysosomal targeting of activated fibroblast growth factor
RT receptor 3 in achondroplasia.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:609-614(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438 AND SER-439, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN VITAMIN D METABOLISM.
RX PubMed=21561999; DOI=10.1152/ajprenal.00740.2010;
RA Gattineni J., Twombley K., Goetz R., Mohammadi M., Baum M.;
RT "Regulation of serum 1,25(OH)2Vitamin D3 levels by fibroblast growth factor
RT 23 is mediated by FGF receptors 3 and 4.";
RL Am. J. Physiol. 301:F371-F377(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 and apoptosis. Plays
CC an essential role in the regulation of chondrocyte differentiation,
CC proliferation and apoptosis, and is required for normal skeleton
CC development. Regulates both osteogenesis and postnatal bone
CC mineralization by osteoblasts. Promotes apoptosis in chondrocytes, but
CC can also promote cancer cell proliferation. Required for normal
CC development of the inner ear. Phosphorylates PLCG1, CBL and FRS2.
CC Ligand 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 Plays a role in the regulation of vitamin D metabolism. Mutations that
CC lead to constitutive kinase activation or impair normal FGFR3
CC maturation, internalization and degradation lead to aberrant signaling.
CC Over-expressed or constitutively activated FGFR3 promotes activation of
CC STAT1, STAT5A and STAT5B. Plays a role in postnatal lung development.
CC {ECO:0000269|PubMed:14699054, ECO:0000269|PubMed:21561999,
CC ECO:0000269|PubMed:8601314, ECO:0000269|PubMed:8630492,
CC ECO:0000269|PubMed:8663044, ECO:0000269|PubMed:9716527}.
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 with FGF1,
CC FGF2, FGF4, FGF6; FGF8, FGF9, FGF10, FGF17, FGF18, FGF19, FGF20 and
CC FGF23 (in vitro). Interacts with KLB. Affinity for fibroblast growth
CC factors (FGFs) is increased by heparan sulfate glycosaminoglycans that
CC function as coreceptors. Likewise, KLB increases the affinity for FGF19
CC and FGF21. Interacts with PIK3R1, PLCG1, SOCS1 and SOCS3 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q61851; Q9JID9: Sh2b2; NbExp=3; IntAct=EBI-6287052, EBI-8100899;
CC Q61851-1; O35082: Kl; NbExp=2; IntAct=EBI-15820536, EBI-1570828;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cytoplasmic vesicle {ECO:0000250}. Endoplasmic reticulum
CC {ECO:0000250}. Note=The activated receptor is rapidly internalized and
CC degraded. Detected in intracellular vesicles after internalization of
CC the autophosphorylated receptor (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=IIIc;
CC IsoId=Q61851-1; Sequence=Displayed;
CC Name=2; Synonyms=IIIb;
CC IsoId=Q61851-2; Sequence=VSP_002990;
CC -!- TISSUE SPECIFICITY: In embryo, expressed in heart, lung, kidney, skin,
CC head and liver but not in muscle. In adult, highest levels in brain.
CC Also expressed in liver, lung, kidney, testis, ovary and uterus. Very
CC low levels in heart, thymus, spleen and muscle.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos from mid-gestation and in
CC adult.
CC -!- DOMAIN: The second and third Ig-like domains directly interact with
CC fibroblast growth factors (FGF) and heparan sulfate proteoglycans.
CC {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.
CC Phosphorylation at Tyr-719 is essential for stimulation of cell
CC proliferation and activation of PIK3R1, STAT1 and MAP kinase signaling.
CC Phosphorylation at Tyr-755 is required for interaction with PIK3R1 and
CC PLCG1 (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Is rapidly ubiquitinated after ligand binding and
CC autophosphorylation, leading to receptor internalization and
CC degradation. Subject to both proteasomal and lysosomal degradation (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 -!- DISRUPTION PHENOTYPE: Mice exhibit defects in their skeleton, including
CC kyphosis, scoliosis, crooked tails and curvature and overgrowth of long
CC bones and vertebrae. This bone dysplasia is due to defects in the
CC regulation of chondrocyte proliferation and differentiation in the
CC cartilaginous growth plate. Mice also display inner ear defects
CC including failure of pillar cell differentiation and tunnel of Corti
CC formation, resulting in profound deafness. Mice lacking both FGFR3 and
CC FGFR4 display pronounced dwarfism, and while their lungs appear normal
CC at birth, they are completely blocked in alveogenesis and do not form
CC secondary septae to delimit alveoli. These mice also show elevated
CC serum levels of 1,25-dihydroxyvitamin D3 and reduced serum phosphorus
CC levels. {ECO:0000269|PubMed:21561999, ECO:0000269|PubMed:8601314,
CC ECO:0000269|PubMed:8630492, ECO:0000269|PubMed:9716527}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Fibroblast growth factor receptor subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M81342; AAA39535.1; -; mRNA.
DR EMBL; S56291; AAB25535.1; -; mRNA.
DR EMBL; L26492; AAA21490.2; -; Genomic_DNA.
DR PIR; A48991; A48991.
DR PIR; I55363; I55363.
DR AlphaFoldDB; Q61851; -.
DR SMR; Q61851; -.
DR DIP; DIP-6031N; -.
DR IntAct; Q61851; 4.
DR MINT; Q61851; -.
DR STRING; 10090.ENSMUSP00000085122; -.
DR BindingDB; Q61851; -.
DR ChEMBL; CHEMBL4066; -.
DR GlyConnect; 2313; 2 N-Linked glycans (1 site).
DR GlyGen; Q61851; 6 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q61851; -.
DR PhosphoSitePlus; Q61851; -.
DR jPOST; Q61851; -.
DR MaxQB; Q61851; -.
DR PaxDb; Q61851; -.
DR PRIDE; Q61851; -.
DR ProteomicsDB; 271583; -. [Q61851-1]
DR ProteomicsDB; 271584; -. [Q61851-2]
DR MGI; MGI:95524; Fgfr3.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; Q61851; -.
DR PhylomeDB; Q61851; -.
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-190371; FGFR3b ligand binding and activation.
DR Reactome; R-MMU-190372; FGFR3c ligand binding and activation.
DR Reactome; R-MMU-5654227; Phospholipase C-mediated cascade, FGFR3.
DR Reactome; R-MMU-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-MMU-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-MMU-5654710; PI-3K cascade:FGFR3.
DR Reactome; R-MMU-5654732; Negative regulation of FGFR3 signaling.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR ChiTaRS; Fgfr3; mouse.
DR PRO; PR:Q61851; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61851; protein.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0030133; C:transport vesicle; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISS:UniProtKB.
DR GO; GO:0005007; F:fibroblast growth factor receptor activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0035198; F:miRNA binding; IDA:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0061144; P:alveolar secondary septum development; IGI:MGI.
DR GO; GO:0048708; P:astrocyte differentiation; IMP:MGI.
DR GO; GO:0060385; P:axonogenesis involved in innervation; IMP:MGI.
DR GO; GO:0060348; P:bone development; IMP:MGI.
DR GO; GO:0070977; P:bone maturation; IMP:BHF-UCL.
DR GO; GO:0030282; P:bone mineralization; IMP:BHF-UCL.
DR GO; GO:0060349; P:bone morphogenesis; IMP:BHF-UCL.
DR GO; GO:0061430; P:bone trabecula morphogenesis; IMP:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; IGI:MGI.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0007267; P:cell-cell signaling; ISO:MGI.
DR GO; GO:0022010; P:central nervous system myelination; IMP:MGI.
DR GO; GO:0090102; P:cochlea development; IMP:MGI.
DR GO; GO:0048546; P:digestive tract morphogenesis; IMP:MGI.
DR GO; GO:0001935; P:endothelial cell proliferation; IMP:MGI.
DR GO; GO:0072148; P:epithelial cell fate commitment; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:MGI.
DR GO; GO:1902178; P:fibroblast growth factor receptor apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; IMP:MGI.
DR GO; GO:0048839; P:inner ear development; IMP:MGI.
DR GO; GO:0070307; P:lens fiber cell development; IGI:MGI.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0140014; P:mitotic nuclear division; IGI:MGI.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:MGI.
DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0048640; P:negative regulation of developmental growth; IMP:BHF-UCL.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR GO; GO:0045608; P:negative regulation of inner ear auditory receptor cell differentiation; IMP:MGI.
DR GO; GO:0045839; P:negative regulation of mitotic nuclear division; IGI:MGI.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0060563; P:neuroepithelial cell differentiation; IMP:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR GO; GO:0014003; P:oligodendrocyte development; IMP:MGI.
DR GO; GO:0038066; P:p38MAPK cascade; IMP:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; TAS:ParkinsonsUK-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; IMP:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
DR GO; GO:0090080; P:positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway; IGI:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
DR GO; GO:0010518; P:positive regulation of phospholipase activity; ISS:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISS:UniProtKB.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IMP:BHF-UCL.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
DR GO; GO:0046850; P:regulation of bone remodeling; IMP:MGI.
DR GO; GO:0010712; P:regulation of collagen metabolic process; IMP:MGI.
DR GO; GO:0030278; P:regulation of ossification; IMP:MGI.
DR GO; GO:0045670; P:regulation of osteoclast differentiation; IMP:MGI.
DR GO; GO:0048678; P:response to axon injury; IMP:MGI.
DR GO; GO:1904383; P:response to sodium phosphate; IDA:MGI.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR GO; GO:0021762; P:substantia nigra development; IMP:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
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; 1.
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 Alternative splicing; Apoptosis; ATP-binding; Cell membrane;
KW Cytoplasmic vesicle; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase;
KW Ubl conjugation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..801
FT /note="Fibroblast growth factor receptor 3"
FT /id="PRO_0000016786"
FT TOPO_DOM 21..369
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..801
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..124
FT /note="Ig-like C2-type 1"
FT DOMAIN 145..238
FT /note="Ig-like C2-type 2"
FT DOMAIN 247..349
FT /note="Ig-like C2-type 3"
FT DOMAIN 466..756
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 125..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 611
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 472..480
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 502
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 641
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P22607"
FT MOD_RES 642
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P22607"
FT MOD_RES 719
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P22607"
FT MOD_RES 755
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P22607"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 59..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 170..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 269..333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 305..352
FT /note="TAGANTTDKELEVLSLHNVTFEDAGEYTCLAGNSIGFSHHSAWLVVLP ->
FT SWISENVEADARLRLANVSERDGGEYLCRATNFIGVAEKAFWLRVHGPQA (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_002990"
FT MUTAGEN 644
FT /note="K->E: Constitutively activated kinase."
FT /evidence="ECO:0000269|PubMed:14699054"
FT CONFLICT 684
FT /note="P -> L (in Ref. 2; AAB25535)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="Missing (in Ref. 2; AAB25535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 801 AA; 87758 MW; 68BC110212691705 CRC64;
MVVPACVLVF CVAVVAGATS EPPGPEQRVV RRAAEVPGPE PSQQEQVAFG SGDTVELSCH
PPGGAPTGPT VWAKDGTGLV ASHRILVGPQ RLQVLNASHE DAGVYSCQHR LTRRVLCHFS
VRVTDAPSSG DDEDGEDVAE DTGAPYWTRP ERMDKKLLAV PAANTVRFRC PAAGNPTPSI
SWLKNGKEFR GEHRIGGIKL RHQQWSLVME SVVPSDRGNY TCVVENKFGS IRQTYTLDVL
ERSPHRPILQ AGLPANQTAI LGSDVEFHCK VYSDAQPHIQ WLKHVEVNGS KVGPDGTPYV
TVLKTAGANT TDKELEVLSL HNVTFEDAGE YTCLAGNSIG FSHHSAWLVV LPAEEELMET
DEAGSVYAGV LSYGVVFFLF ILVVAAVILC RLRSPPKKGL GSPTVHKVSR FPLKRQVSLE
SNSSMNSNTP LVRIARLSSG EGPVLANVSE LELPADPKWE LSRTRLTLGK PLGEGCFGQV
VMAEAIGIDK DRTAKPVTVA VKMLKDDATD KDLSDLVSEM EMMKMIGKHK NIINLLGACT
QGGPLYVLVE YAAKGNLREF LRARRPPGMD YSFDACRLPE EQLTCKDLVS CAYQVARGME
YLASQKCIHR DLAARNVLVT EDNVMKIADF GLARDVHNLD YYKKTTNGRL PVKWMAPEAL
FDRVYTHQSD VWSFGVLLWE IFTPGGPSPY PGIPVEELFK LLKEGHRMDK PASCTHDLYM
IMRECWHAVP SQRPTFKQLV EDLDRILTVT STDEYLDLSV PFEQYSPGGQ DTPSSSSSGD
DSVFTHDLLP PGPPSNGGPR T
