ID   FGFR1_RAT               Reviewed;         822 AA.
AC   Q04589;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=Fibroblast growth factor receptor 1;
DE            Short=FGFR-1;
DE            Short=bFGF-R-1;
DE            EC=2.7.10.1 {ECO:0000250|UniProtKB:P11362};
DE   AltName: Full=Basic fibroblast growth factor receptor 1;
DE   AltName: Full=MFR;
DE   AltName: Full=Proto-oncogene c-Fgr;
DE   AltName: CD_antigen=CD331;
DE   Flags: Precursor;
GN   Name=Fgfr1; Synonyms=Flg;
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].
RX   PubMed=8382532; DOI=10.1016/0167-4781(93)90266-g;
RA   Yazaki N., Hiroko F., Mitsuhiro O., Toshisuke K., Nobuyuki I.;
RT   "The structure and expression of the FGF receptor-1 mRNA isoforms in rat
RT   tissues.";
RL   Biochim. Biophys. Acta 1172:37-42(1993).
RN   [2]
RP   INTERACTION WITH RPS6KA1, AND SUBCELLULAR LOCATION.
RX   PubMed=15117958; DOI=10.1074/jbc.m311144200;
RA   Hu Y., Fang X., Dunham S.M., Prada C., Stachowiak E.K., Stachowiak M.K.;
RT   "90-kDa ribosomal S6 kinase is a direct target for the nuclear fibroblast
RT   growth factor receptor 1 (FGFR1): role in FGFR1 signaling.";
RL   J. Biol. Chem. 279:29325-29335(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=17992255; DOI=10.1172/jci32409;
RA   Ben-Dov I.Z., Galitzer H., Lavi-Moshayoff V., Goetz R., Kuro-o M.,
RA   Mohammadi M., Sirkis R., Naveh-Many T., Silver J.;
RT   "The parathyroid is a target organ for FGF23 in rats.";
RL   J. Clin. Invest. 117:4003-4008(2007).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor
CC       for fibroblast growth factors and plays an essential role in the
CC       regulation of embryonic development, cell proliferation,
CC       differentiation and migration. Required for normal mesoderm patterning
CC       and correct axial organization during embryonic development, normal
CC       skeletogenesis and normal development of the gonadotropin-releasing
CC       hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and
CC       SHB. Ligand binding leads to the activation of several signaling
CC       cascades. Activation of PLCG1 leads to the production of the cellular
CC       signaling 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       Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the
CC       nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the
CC       regulation of transcription. FGFR1 signaling is down-regulated by
CC       IL17RD/SEF, and by FGFR1 ubiquitination, internalization and
CC       degradation (By similarity). {ECO:0000250|UniProtKB:P11362,
CC       ECO:0000250|UniProtKB:P16092}.
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:0000250|UniProtKB:P11362, ECO:0000255|PROSITE-
CC         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       sequential autophosphorylation on tyrosine residues (By similarity).
CC       {ECO:0000250|UniProtKB:P11362}.
CC   -!- SUBUNIT: Monomer. Homodimer after ligand binding. Interacts
CC       predominantly with FGF1 and FGF2, but can also interact with FGF3,
CC       FGF4, FGF5, FGF6, FGF8, FGF10, FGF19, FGF21, FGF22 and FGF23 (in
CC       vitro). Ligand specificity is determined by tissue-specific expression
CC       of isoforms, and differences in the third Ig-like domain are crucial
CC       for ligand specificity. Affinity for fibroblast growth factors (FGFs)
CC       is increased by heparan sulfate glycosaminoglycans that function as
CC       coreceptors. Likewise, KLB increases the affinity for FGF19, FGF21 and
CC       FGF23. Interacts (phosphorylated on Tyr-766) with PLCG1 (via SH2
CC       domains). Interacts with FRS2. Interacts (via C-terminus) with NEDD4
CC       (via WW3 domain). Interacts with RPS6KA1 (PubMed:15117958). Interacts
CC       with KL (By similarity). Interacts with SHB (via SH2 domain) and GRB10.
CC       Interacts with ANOS1; this interaction does not interfere with FGF2-
CC       binding to FGFR1, but prevents binding of heparin-bound FGF2. Interacts
CC       with SOX2 and SOX3 (By similarity). Interacts with FLRT1, FLRT2 and
CC       FLRT3. Found in a ternary complex with FGF1 and ITGAV:ITGB3 (By
CC       similarity). {ECO:0000250|UniProtKB:P11362,
CC       ECO:0000250|UniProtKB:P16092, ECO:0000269|PubMed:15117958}.
CC   -!- INTERACTION:
CC       Q04589; P19327: Htr1a; NbExp=5; IntAct=EBI-2480918, EBI-6570156;
CC       Q04589; P10686: Plcg1; NbExp=2; IntAct=EBI-2480918, EBI-520788;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15117958};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:15117958}.
CC       Nucleus {ECO:0000269|PubMed:15117958}. Cytoplasm, cytosol
CC       {ECO:0000269|PubMed:15117958}. Cytoplasmic vesicle {ECO:0000250}.
CC       Note=After ligand binding, both receptor and ligand are rapidly
CC       internalized. Can translocate to the nucleus after internalization, or
CC       by translocation from the endoplasmic reticulum or Golgi apparatus to
CC       the cytosol, and from there to the nucleus (By similarity).
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in the parathyroid.
CC       {ECO:0000269|PubMed:17992255}.
CC   -!- DOMAIN: The second and third Ig-like domains directly interact with
CC       fibroblast growth factors (FGF) and heparan sulfate proteoglycans.
CC       Isoforms lacking the first Ig-like domain have higher affinity for
CC       fibroblast growth factors (FGF) and heparan sulfate proteoglycans than
CC       isoforms with all three Ig-like domains (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 and
CC       proceeds in a highly ordered manner. Initial autophosphorylation at
CC       Tyr-653 increases the kinase activity by a factor of 50 to 100. After
CC       this, Tyr-583 becomes phosphorylated, followed by phosphorylation of
CC       Tyr-463, Tyr-766, Tyr-583 and Tyr-585. In a third stage, Tyr-654 is
CC       autophosphorylated, resulting in a further tenfold increase of kinase
CC       activity. Phosphotyrosine residues provide docking sites for
CC       interacting proteins and so are crucial for FGFR1 function and its
CC       regulation (By similarity). {ECO:0000250|UniProtKB:P11362}.
CC   -!- PTM: Ubiquitinated. FGFR1 is rapidly ubiquitinated by NEDD4 after
CC       autophosphorylation, leading to internalization and lysosomal
CC       degradation. CBL is recruited to activated FGFR1 via FRS2 and GRB2, and
CC       mediates ubiquitination and subsequent degradation of FGFR1 (By
CC       similarity). {ECO:0000250|UniProtKB:P11362}.
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|UniProtKB:P11362}.
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; D12498; BAA02059.1; -; mRNA.
DR   PIR; S29840; S29840.
DR   RefSeq; NP_077060.1; NM_024146.1.
DR   AlphaFoldDB; Q04589; -.
DR   BMRB; Q04589; -.
DR   SMR; Q04589; -.
DR   BioGRID; 249399; 4.
DR   CORUM; Q04589; -.
DR   IntAct; Q04589; 3.
DR   MINT; Q04589; -.
DR   STRING; 10116.ENSRNOP00000043459; -.
DR   ChEMBL; CHEMBL4523276; -.
DR   GlyCosmos; Q04589; 8 sites, No reported glycans.
DR   GlyGen; Q04589; 8 sites.
DR   iPTMnet; Q04589; -.
DR   jPOST; Q04589; -.
DR   PaxDb; 10116-ENSRNOP00000036885; -.
DR   GeneID; 79114; -.
DR   KEGG; rno:79114; -.
DR   UCSC; RGD:620713; rat.
DR   AGR; RGD:620713; -.
DR   CTD; 2260; -.
DR   RGD; 620713; Fgfr1.
DR   eggNOG; KOG0200; Eukaryota.
DR   InParanoid; Q04589; -.
DR   OrthoDB; 1614410at2759; -.
DR   PhylomeDB; Q04589; -.
DR   BRENDA; 2.7.10.1; 5301.
DR   Reactome; R-RNO-109704; PI3K Cascade.
DR   Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-RNO-190370; FGFR1b ligand binding and activation.
DR   Reactome; R-RNO-190373; FGFR1c ligand binding and activation.
DR   Reactome; R-RNO-190374; FGFR1c and Klotho ligand binding and activation.
DR   Reactome; R-RNO-445144; Signal transduction by L1.
DR   Reactome; R-RNO-5654219; Phospholipase C-mediated cascade: FGFR1.
DR   Reactome; R-RNO-5654687; Downstream signaling of activated FGFR1.
DR   Reactome; R-RNO-5654688; SHC-mediated cascade:FGFR1.
DR   Reactome; R-RNO-5654689; PI-3K cascade:FGFR1.
DR   Reactome; R-RNO-5654693; FRS-mediated FGFR1 signaling.
DR   Reactome; R-RNO-5654726; Negative regulation of FGFR1 signaling.
DR   Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   PRO; PR:Q04589; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0043235; C:receptor complex; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
DR   GO; GO:0017134; F:fibroblast growth factor binding; ISS:UniProtKB.
DR   GO; GO:0005007; F:fibroblast growth factor receptor activity; ISS:UniProtKB.
DR   GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0090722; F:receptor-receptor interaction; ISO:RGD.
DR   GO; GO:0042169; F:SH2 domain binding; ISO:RGD.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR   GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR   GO; GO:0060117; P:auditory receptor cell development; ISO:RGD.
DR   GO; GO:0048514; P:blood vessel morphogenesis; ISO:RGD.
DR   GO; GO:0007420; P:brain development; ISO:RGD.
DR   GO; GO:0060445; P:branching involved in salivary gland morphogenesis; ISO:RGD.
DR   GO; GO:0055074; P:calcium ion homeostasis; ISO:RGD.
DR   GO; GO:0060038; P:cardiac muscle cell proliferation; ISO:RGD.
DR   GO; GO:0048469; P:cell maturation; ISO:RGD.
DR   GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR   GO; GO:0030031; P:cell projection assembly; ISO:RGD.
DR   GO; GO:0071420; P:cellular response to histamine; IEP:RGD.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR   GO; GO:0071529; P:cementum mineralization; ISO:RGD.
DR   GO; GO:0021954; P:central nervous system neuron development; IMP:RGD.
DR   GO; GO:0002062; P:chondrocyte differentiation; ISO:RGD.
DR   GO; GO:0071344; P:diphosphate metabolic process; ISO:RGD.
DR   GO; GO:0043583; P:ear development; ISO:RGD.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; ISO:RGD.
DR   GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:RGD.
DR   GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0035607; P:fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development; ISO:RGD.
DR   GO; GO:0010467; P:gene expression; ISO:RGD.
DR   GO; GO:0048699; P:generation of neurons; ISO:RGD.
DR   GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR   GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
DR   GO; GO:0030324; P:lung development; ISO:RGD.
DR   GO; GO:0060484; P:lung-associated mesenchyme development; ISO:RGD.
DR   GO; GO:0048762; P:mesenchymal cell differentiation; ISO:RGD.
DR   GO; GO:0010463; P:mesenchymal cell proliferation; ISO:RGD.
DR   GO; GO:0030901; P:midbrain development; ISO:RGD.
DR   GO; GO:0042474; P:middle ear morphogenesis; ISO:RGD.
DR   GO; GO:0021837; P:motogenic signaling involved in postnatal olfactory bulb interneuron migration; IMP:RGD.
DR   GO; GO:0090272; P:negative regulation of fibroblast growth factor production; ISO:RGD.
DR   GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0031175; P:neuron projection development; IDA:RGD.
DR   GO; GO:0021769; P:orbitofrontal cortex development; ISO:RGD.
DR   GO; GO:0001759; P:organ induction; ISO:RGD.
DR   GO; GO:0042473; P:outer ear morphogenesis; ISO:RGD.
DR   GO; GO:0048339; P:paraxial mesoderm development; ISO:RGD.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR   GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:RGD.
DR   GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:RGD.
DR   GO; GO:0045787; P:positive regulation of cell cycle; ISO:RGD.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IBA:GO_Central.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:2000546; P:positive regulation of endothelial cell chemotaxis to fibroblast growth factor; ISO:RGD.
DR   GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:RGD.
DR   GO; GO:2000491; P:positive regulation of hepatic stellate cell activation; IMP:RGD.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR   GO; GO:0090080; P:positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway; ISO:RGD.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:RGD.
DR   GO; GO:1903465; P:positive regulation of mitotic cell cycle DNA replication; ISO:RGD.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IDA:RGD.
DR   GO; GO:2000830; P:positive regulation of parathyroid hormone secretion; ISO:RGD.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:RGD.
DR   GO; GO:0010863; P:positive regulation of phospholipase C activity; ISS:UniProtKB.
DR   GO; GO:2000648; P:positive regulation of stem cell proliferation; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:1905564; P:positive regulation of vascular endothelial cell proliferation; ISO:RGD.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0060665; P:regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling; ISO:RGD.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IDA:RGD.
DR   GO; GO:0050678; P:regulation of epithelial cell proliferation; ISO:RGD.
DR   GO; GO:2001239; P:regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR   GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR   GO; GO:0048378; P:regulation of lateral mesodermal cell fate specification; ISO:RGD.
DR   GO; GO:0010966; P:regulation of phosphate transport; ISO:RGD.
DR   GO; GO:0051174; P:regulation of phosphorus metabolic process; ISO:RGD.
DR   GO; GO:0072091; P:regulation of stem cell proliferation; IMP:RGD.
DR   GO; GO:0002931; P:response to ischemia; IEP:RGD.
DR   GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR   GO; GO:1904383; P:response to sodium phosphate; ISO:RGD.
DR   GO; GO:0007435; P:salivary gland morphogenesis; ISO:RGD.
DR   GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR   GO; GO:0048863; P:stem cell differentiation; ISO:RGD.
DR   GO; GO:0019827; P:stem cell population maintenance; IMP:RGD.
DR   GO; GO:0072089; P:stem cell proliferation; ISO:RGD.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   GO; GO:0001657; P:ureteric bud development; ISO:RGD.
DR   GO; GO:0021847; P:ventricular zone neuroblast division; ISO:RGD.
DR   GO; GO:0070640; P:vitamin D3 metabolic process; ISO:RGD.
DR   CDD; cd04973; IgI_1_FGFR; 1.
DR   CDD; cd05857; IgI_2_FGFR; 1.
DR   CDD; cd05098; PTKc_FGFR1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR028174; FGF_rcpt_1.
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; IPR013151; Immunoglobulin.
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   PANTHER; PTHR24416:SF131; FIBROBLAST GROWTH FACTOR RECEPTOR 1; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF00047; ig; 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; Immunoglobulin; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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   ATP-binding; Cell membrane; Cytoplasm; Cytoplasmic vesicle; Disulfide bond;
KW   Glycoprotein; Heparin-binding; Immunoglobulin domain; Kinase; Membrane;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Signal; Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase; Ubl conjugation.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..822
FT                   /note="Fibroblast growth factor receptor 1"
FT                   /id="PRO_0000016782"
FT   TOPO_DOM        22..376
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        377..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        398..822
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          25..119
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          158..246
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          255..357
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          478..767
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          120..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..177
FT                   /note="Heparin-binding"
FT   REGION          770..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..137
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..794
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        623
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         484..490
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         514
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         562..564
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         568
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         641
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   SITE            766
FT                   /note="Mediates interaction with PLCG1 and SHB"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         463
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P11362"
FT   MOD_RES         583
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P11362"
FT   MOD_RES         585
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P11362"
FT   MOD_RES         653
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P11362"
FT   MOD_RES         654
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P11362"
FT   MOD_RES         730
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P11362"
FT   MOD_RES         766
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P11362"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        240
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        264
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        296
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        55..101
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        178..230
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        277..341
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   822 AA;  91825 MW;  E59D924D0A1DE5C5 CRC64;
     MWGWRGLLFW AVLVTATLCT ARPAPTLPEQ AQPWGVPVEV ESLLVHPGDL LQLRCRLRDD
     VQSINWLRDG VQLAESNRTR ITGEEVEVRD SIPADSGLYA CVTNSPSGSD TTYFSVNVSD
     ALPSSEDDDD DDDSSSEEKE TDNTKPNRRP VAPYWTSPEK MEKKLHAVPA AKTVKFKCPS
     SGTPSPTLRW LKNGKEFKPD HRIGGYKVRY ATWSIIMDSV VPSDKGNYTC IVENEYGSIN
     HTYQLDVVER SPHRPILQAG LPANKTVALG SNVEFMCKVY SDPQPHIQWL KHIEVNGSKI
     GPDNLPYDQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT CLAGNSIGLS HHSAWLTVLE
     ALEERPAVMT SPLYLEIIIY CTGAFLISCM VGSVIIYKMK SGTKKSDFHS QMAVHKLAKS
     IPLRRQVTVS ADSSASMNSG VLLVRPSRLS SSGTPMLAGV SEYELPEDPR WELPRDRLVL
     GKPLGEGCFG QVVLAEAIGL DKDKPNRVTK VAVKMLKSDA TEKDLSDLIS EMEMMKMIGK
     HKNIINLLGA CTQDGPLYVI VEYASKGNLR EYLQARRPPG LEYCYNPSHN PEEQLSSKDL
     VSCAYQVARG MEYLASKKCI HRDLAARNVL VTEDNVMKIA DFGLARDIHH IDYYKKTTNG
     RLPVKWMAPE ALFDRIYTHQ SDVWSFGVLL WEIFTLGGSP NPGVPVEELF KLLKEGHRMD
     KPSNCTNELY MMMRDCWNAV PSQRPTFKQL VEDLDRIVAL TSNQEYLDLS MPLDQDSPSF
     PDTRSSTCSS GEDSVFSHEP FPEEPCLPRH PTQLANGGLN RR
//