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Fibroblast growth factor receptor 1 (FGFR-1) (bFGF-R-1) (EC 2.7.10.1) (Basic fibroblast growth factor receptor 1) (MFR) (Proto-oncogene c-Fgr) (CD antigen CD331)

 FGFR1_MOUSE             Reviewed;         822 AA.
P16092; E9Q2P4; Q01736; Q60830; Q61562; Q80T10; Q8CFK8; Q9QZM7;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 2.
22-NOV-2017, entry version 196.
RecName: Full=Fibroblast growth factor receptor 1;
Short=FGFR-1;
Short=bFGF-R-1;
EC=2.7.10.1 {ECO:0000250|UniProtKB:P11362};
AltName: Full=Basic fibroblast growth factor receptor 1;
AltName: Full=MFR;
AltName: Full=Proto-oncogene c-Fgr;
AltName: CD_antigen=CD331;
Flags: Precursor;
Name=Fgfr1; Synonyms=Flg;
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 1).
TISSUE=Brain;
PubMed=1689490; DOI=10.1073/pnas.87.4.1596;
Reid H.H., Wilks A.F., Bernard O.;
"Two forms of the basic fibroblast growth factor receptor-like mRNA
are expressed in the developing mouse brain.";
Proc. Natl. Acad. Sci. U.S.A. 87:1596-1600(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=2161096;
Safran A., Avivi A., Orr-Urtereger A., Neufeld G., Lonai P., Givol D.,
Yarden Y.;
"The murine flg gene encodes a receptor for fibroblast growth
factor.";
Oncogene 5:635-643(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING.
PubMed=1708247; DOI=10.1016/0006-291X(91)90885-B;
Kouhara H., Kasayama S., Saito H., Matsumoto K., Sato B.;
"Expression cDNA cloning of fibroblast growth factor (FGF) receptor in
mouse breast cancer cells: a variant form in FGF-responsive
transformed cells.";
Biochem. Biophys. Res. Commun. 176:31-37(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=2161540; DOI=10.1073/pnas.87.11.4378;
Mansukhani A., Moscatelli D., Talarico D., Levytska V., Basilico C.;
"A murine fibroblast growth factor (FGF) receptor expressed in CHO
cells is activated by basic FGF and Kaposi FGF.";
Proc. Natl. Acad. Sci. U.S.A. 87:4378-4382(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
STRAIN=Swiss Webster; TISSUE=Embryonic heart;
PubMed=7897669; DOI=10.1006/jmcc.1994.1164;
Jin Y., Pasumarthi K.B., Bock M.E., Lytras A., Kardami E.,
Cattini P.A.;
"Cloning and expression of fibroblast growth factor receptor-1
isoforms in the mouse heart: evidence for isoform switching during
heart development.";
J. Mol. Cell. Cardiol. 26:1449-1459(1994).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), SUBCELLULAR LOCATION, FUNCTION
AS FGF7 RECEPTOR AND IN ACTIVATION OF SIGNALING PATHWAYS, INTERACTION
WITH FGF1; FGF2; FGF7 AND FGF10, GLYCOSYLATION, TISSUE SPECIFICITY,
AND ALTERNATIVE SPLICING.
STRAIN=BALB/cJ;
PubMed=10821861; DOI=10.1074/jbc.275.21.16091;
Beer H.-D., Vindevoghel L., Gait M.J., Revest J.-M., Duan D.R.,
Mason I., Dickson C., Werner S.;
"Fibroblast growth factor (FGF) receptor 1-IIIb is a naturally
occurring functional receptor for FGFs that is preferentially
expressed in the skin and the brain.";
J. Biol. Chem. 275:16091-16097(2000).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-15, AND ALTERNATIVE SPLICING.
PubMed=7802632; DOI=10.1006/bbrc.1994.2773;
Harada T., Saito H., Kouhara H., Kurebayashi S., Kasayama S.,
Terakawa N., Kishimoto T., Sato B.;
"Murine fibroblast growth factor receptor 1 gene generates multiple
messenger RNAs containing two open reading frames via alternative
splicing.";
Biochem. Biophys. Res. Commun. 205:1057-1063(1994).
[11]
INTERACTION WITH FGF1; FGF2; FGF4; FGF5; FGF6, AND FUNCTION IN CELL
PROLIFERATION.
PubMed=1309590; DOI=10.1128/MCB.12.1.240;
Ornitz D.M., Yayon A., Flanagan J.G., Svahn C.M., Levi E., Leder P.;
"Heparin is required for cell-free binding of basic fibroblast growth
factor to a soluble receptor and for mitogenesis in whole cells.";
Mol. Cell. Biol. 12:240-247(1992).
[12]
DISRUPTION PHENOTYPE, AND FUNCTION DURING EMBRYONIC DEVELOPMENT.
PubMed=8001822; DOI=10.1101/gad.8.24.3032;
Yamaguchi T.P., Harpal K., Henkemeyer M., Rossant J.;
"fgfr-1 is required for embryonic growth and mesodermal patterning
during mouse gastrulation.";
Genes Dev. 8:3032-3044(1994).
[13]
DISRUPTION PHENOTYPE, AND FUNCTION DURING EMBRYONIC DEVELOPMENT.
PubMed=8001823; DOI=10.1101/gad.8.24.3045;
Deng C.X., Wynshaw-Boris A., Shen M.M., Daugherty C., Ornitz D.M.,
Leder P.;
"Murine FGFR-1 is required for early postimplantation growth and axial
organization.";
Genes Dev. 8:3045-3057(1994).
[14]
SUBUNIT, AND LIGAND SPECIFICITY.
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).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10896947; DOI=10.1074/jbc.M910132199;
Chikazu D., Hakeda Y., Ogata N., Nemoto K., Itabashi A., Takato T.,
Kumegawa M., Nakamura K., Kawaguchi H.;
"Fibroblast growth factor (FGF)-2 directly stimulates mature
osteoclast function through activation of FGF receptor 1 and p42/p44
MAP kinase.";
J. Biol. Chem. 275:31444-31450(2000).
[16]
INTERACTION WITH SHB.
PubMed=12181353; DOI=10.1091/mbc.E02-02-0103;
Cross M.J., Lu L., Magnusson P., Nyqvist D., Holmqvist K., Welsh M.,
Claesson-Welsh L.;
"The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and
regulates the Ras/MEK/MAPK pathway via FRS2 phosphorylation in
endothelial cells.";
Mol. Biol. Cell 13:2881-2893(2002).
[17]
SUBCELLULAR LOCATION.
PubMed=15383174; DOI=10.1089/dna.2004.23.538;
Reilly J.F., Mizukoshi E., Maher P.A.;
"Ligand dependent and independent internalization and nuclear
translocation of fibroblast growth factor (FGF) receptor 1.";
DNA Cell Biol. 23:538-548(2004).
[18]
INTERACTION WITH FLRT1; FLRT2 AND FLRT3.
PubMed=16872596; DOI=10.1016/j.ydbio.2006.04.004;
Haines B.P., Wheldon L.M., Summerbell D., Heath J.K., Rigby P.W.J.;
"Regulated expression of FLRT genes implies a functional role in the
regulation of FGF signalling during mouse development.";
Dev. Biol. 297:14-25(2006).
[19]
FUNCTION, AND INTERACTION WITH KL AND FGF23.
PubMed=17086194; DOI=10.1038/nature05315;
Urakawa I., Yamazaki Y., Shimada T., Iijima K., Hasegawa H., Okawa K.,
Fujita T., Fukumoto S., Yamashita T.;
"Klotho converts canonical FGF receptor into a specific receptor for
FGF23.";
Nature 444:770-774(2006).
[20]
INTERACTION WITH SOX2 AND SOX3.
PubMed=17728342; DOI=10.1242/dev.007906;
Rizzoti K., Lovell-Badge R.;
"SOX3 activity during pharyngeal segmentation is required for
craniofacial morphogenesis.";
Development 134:3437-3448(2007).
[21]
INTERACTION WITH KLB.
PubMed=17452648; DOI=10.1073/pnas.0701600104;
Ogawa Y., Kurosu H., Yamamoto M., Nandi A., Rosenblatt K.P., Goetz R.,
Eliseenkova A.V., Mohammadi M., Kuro-o M.;
"BetaKlotho is required for metabolic activity of fibroblast growth
factor 21.";
Proc. Natl. Acad. Sci. U.S.A. 104:7432-7437(2007).
[22]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-317.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[24]
STRUCTURE BY NMR OF 25-119.
PubMed=16731982; DOI=10.1110/ps.062207906;
Kiselyov V.V., Bock E., Berezin V., Poulsen F.M.;
"NMR structure of the first Ig module of mouse FGFR1.";
Protein Sci. 15:1512-1515(2006).
-!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface
receptor for fibroblast growth factors and plays an essential role
in the regulation of embryonic development, cell proliferation,
differentiation and migration. Required for normal mesoderm
patterning and correct axial organization during embryonic
development, normal skeletogenesis and normal development of the
gonadotropin-releasing hormone (GnRH) neuronal system.
Phosphorylates PLCG1, FRS2, GAB1 and SHB. 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. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2.
In the nucleus, enhances RPS6KA1 and CREB1 activity and
contributes to the regulation of transcription. FGFR1 signaling is
down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination,
internalization and degradation (By similarity).
{ECO:0000250|UniProtKB:P11362, ECO:0000269|PubMed:10821861,
ECO:0000269|PubMed:10896947, ECO:0000269|PubMed:1309590,
ECO:0000269|PubMed:17086194, ECO:0000269|PubMed:8001822,
ECO:0000269|PubMed:8001823}.
-!- 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 sequential 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, FGF5, FGF6, FGF8, FGF10, FGF19, FGF21, FGF22 and FGF23 (in
vitro) (PubMed:10821861, PubMed:1309590, PubMed:17086194). 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, FGF21 and FGF23. Interacts (phosphorylated on Tyr-766) with
PLCG1 (via SH2 domains). Interacts with FRS2. Interacts with
RPS6KA1. Interacts (via C-terminus) with NEDD4 (via WW3 domain).
Interacts with KL (PubMed:17086194). Interacts with SHB (via SH2
domain) (PubMed:12181353). Interacts with GRB10 (By similarity).
Interacts with ANOS1; this interaction does not interfere with
FGF2-binding to FGFR1, but prevents binding of heparin-bound FGF2
(By similarity). Interacts with SOX2 and SOX3 (PubMed:17728342).
Interacts with FLRT1, FLRT2 and FLRT3 (PubMed:16872596). Found in
a ternary complex with FGF1 and ITGAV:ITGB3 (By similarity).
{ECO:0000250|UniProtKB:P11362, ECO:0000269|PubMed:10821861,
ECO:0000269|PubMed:12181353, ECO:0000269|PubMed:1309590,
ECO:0000269|PubMed:16872596, ECO:0000269|PubMed:17086194,
ECO:0000269|PubMed:17452648, ECO:0000269|PubMed:17728342,
ECO:0000269|PubMed:8663044}.
-!- INTERACTION:
O35082:Kl; NbExp=2; IntAct=EBI-7953898, EBI-1570828;
Q99N32:Klb; NbExp=3; IntAct=EBI-7953898, EBI-15633521;
P13596:Ncam1 (xeno); NbExp=2; IntAct=EBI-7953898, EBI-916499;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Nucleus. Cytoplasm, cytosol. Cytoplasmic vesicle.
Note=After ligand binding, both receptor and ligand are rapidly
internalized. Can translocate to the nucleus after
internalization, or by translocation from the endoplasmic
reticulum or Golgi apparatus to the cytosol, and from there to the
nucleus.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein.
-!- SUBCELLULAR LOCATION: Isoform 5: Cell membrane; Single-pass type I
membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=FGFR1-IIIc, Long;
IsoId=P16092-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=P16092-2; Sequence=VSP_002962;
Name=3; Synonyms=Variant;
IsoId=P16092-3; Sequence=VSP_002961, VSP_002963;
Name=4;
IsoId=P16092-4; Sequence=VSP_002962, VSP_002963;
Name=5; Synonyms=FGFR1-IIIb;
IsoId=P16092-5; Sequence=VSP_002962, VSP_002963, VSP_041919,
VSP_041920, VSP_041921, VSP_041922;
Name=6;
IsoId=P16092-6; Sequence=VSP_002963;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:10821861}.
-!- DOMAIN: The second and third Ig-like domains directly interact
with fibroblast growth factors (FGF) and heparan sulfate
proteoglycans. Isoforms lacking the first Ig-like domain have
higher affinity for fibroblast growth factors (FGF) and heparan
sulfate proteoglycans than isoforms with all three Ig-like domains
(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 and proceeds in a highly ordered manner.
Initial autophosphorylation at Tyr-653 increases the kinase
activity by a factor of 50 to 100. After this, Tyr-583 becomes
phosphorylated, followed by phosphorylation of Tyr-463, Tyr-766,
Tyr-583 and Tyr-585. In a third stage, Tyr-654 is
autophosphorylated, resulting in a further tenfold increase of
kinase activity. Phosphotyrosine residues provide docking sites
for interacting proteins and so are crucial for FGFR1 function and
its regulation (By similarity). {ECO:0000250|UniProtKB:P11362}.
-!- PTM: Ubiquitinated. FGFR1 is rapidly ubiquitinated by NEDD4 after
autophosphorylation, leading to internalization and lysosomal
degradation. CBL is recruited to activated FGFR1 via FRS2 and
GRB2, and mediates ubiquitination and subsequent degradation of
FGFR1 (By similarity). {ECO:0000250|UniProtKB:P11362}.
-!- PTM: N-glycosylated in the endoplasmic reticulum. The N-glycan
chains undergo further maturation to an Endo H-resistant form in
the Golgi apparatus. {ECO:0000269|PubMed:10821861,
ECO:0000269|PubMed:19349973}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality around gastrulation, due
to growth defects during early embryonic development and aberrant
mesoderm patterning. {ECO:0000269|PubMed:8001822,
ECO:0000269|PubMed:8001823}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Fibroblast growth factor receptor subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAB32845.1; Type=Miscellaneous discrepancy; Note=Proposes two coding sequences for the same mRNA.; Evidence={ECO:0000305};
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EMBL; M28998; AAA37290.1; -; mRNA.
EMBL; X51893; CAA36175.1; -; mRNA.
EMBL; M65053; AAA37620.1; -; mRNA.
EMBL; M33760; AAA37622.1; -; mRNA.
EMBL; U23445; AAC52183.1; -; mRNA.
EMBL; AF176552; AAF05312.1; -; mRNA.
EMBL; AK028354; BAC25899.1; -; mRNA.
EMBL; S74765; AAB32845.1; ALT_SEQ; mRNA.
EMBL; AC160526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC033447; AAH33447.1; -; mRNA.
CCDS; CCDS40304.1; -. [P16092-2]
CCDS; CCDS52526.1; -. [P16092-1]
CCDS; CCDS57614.1; -. [P16092-6]
PIR; A34849; TVMSFG.
PIR; B42057; B42057.
PIR; I49293; I49293.
PIR; JH0393; JH0393.
RefSeq; NP_001073377.1; NM_001079908.2. [P16092-6]
RefSeq; NP_001073378.1; NM_001079909.2. [P16092-2]
RefSeq; NP_034336.2; NM_010206.3. [P16092-1]
RefSeq; XP_006509073.1; XM_006509010.2. [P16092-1]
RefSeq; XP_006509075.1; XM_006509012.1. [P16092-1]
RefSeq; XP_011240423.1; XM_011242121.1. [P16092-4]
UniGene; Mm.265716; -.
PDB; 2CKN; NMR; -; A=25-119.
PDBsum; 2CKN; -.
ProteinModelPortal; P16092; -.
SMR; P16092; -.
BioGrid; 199656; 10.
DIP; DIP-6033N; -.
IntAct; P16092; 10.
MINT; MINT-2635590; -.
STRING; 10090.ENSMUSP00000081041; -.
BindingDB; P16092; -.
ChEMBL; CHEMBL3960; -.
iPTMnet; P16092; -.
PhosphoSitePlus; P16092; -.
MaxQB; P16092; -.
PaxDb; P16092; -.
PeptideAtlas; P16092; -.
PRIDE; P16092; -.
Ensembl; ENSMUST00000084027; ENSMUSP00000081041; ENSMUSG00000031565. [P16092-1]
Ensembl; ENSMUST00000117179; ENSMUSP00000113909; ENSMUSG00000031565. [P16092-6]
Ensembl; ENSMUST00000119398; ENSMUSP00000113855; ENSMUSG00000031565. [P16092-2]
Ensembl; ENSMUST00000167764; ENSMUSP00000131343; ENSMUSG00000031565. [P16092-5]
Ensembl; ENSMUST00000178276; ENSMUSP00000137515; ENSMUSG00000031565. [P16092-5]
GeneID; 14182; -.
KEGG; mmu:14182; -.
UCSC; uc009lfy.2; mouse. [P16092-1]
UCSC; uc009lga.2; mouse. [P16092-2]
UCSC; uc033jet.1; mouse. [P16092-4]
CTD; 2260; -.
MGI; MGI:95522; Fgfr1.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOGENOM; HOG000263410; -.
HOVERGEN; HBG000345; -.
InParanoid; P16092; -.
KO; K04362; -.
PhylomeDB; P16092; -.
TreeFam; TF316307; -.
BRENDA; 2.7.10.1; 3474.
Reactome; R-MMU-109704; PI3K Cascade.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-190370; FGFR1b ligand binding and activation.
Reactome; R-MMU-190373; FGFR1c ligand binding and activation.
Reactome; R-MMU-190374; FGFR1c and Klotho ligand binding and activation.
Reactome; R-MMU-445144; Signal transduction by L1.
Reactome; R-MMU-5654219; Phospholipase C-mediated cascade: FGFR1.
Reactome; R-MMU-5654687; Downstream signaling of activated FGFR1.
Reactome; R-MMU-5654688; SHC-mediated cascade:FGFR1.
Reactome; R-MMU-5654689; PI-3K cascade:FGFR1.
Reactome; R-MMU-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-MMU-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-MMU-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-MMU-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-MMU-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
ChiTaRS; Fgfr1; mouse.
EvolutionaryTrace; P16092; -.
PRO; PR:P16092; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031565; -.
CleanEx; MM_FGFR1; -.
CleanEx; MM_FLG; -.
ExpressionAtlas; P16092; baseline and differential.
Genevisible; P16092; MM.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IPI:MGI.
GO; GO:0043235; C:receptor complex; ISO: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; IDA:MGI.
GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
GO; GO:0090722; F:receptor-receptor interaction; ISO:MGI.
GO; GO:0001525; P:angiogenesis; IGI:MGI.
GO; GO:0060117; P:auditory receptor cell development; IMP:MGI.
GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
GO; GO:0007420; P:brain development; IMP:MGI.
GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IMP:MGI.
GO; GO:0048469; P:cell maturation; IMP:MGI.
GO; GO:0002062; P:chondrocyte differentiation; IGI:MGI.
GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IGI:MGI.
GO; GO:0035607; P:fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development; IMP:UniProtKB.
GO; GO:0048699; P:generation of neurons; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
GO; GO:0030324; P:lung development; IMP:MGI.
GO; GO:0060484; P:lung-associated mesenchyme development; IGI:MGI.
GO; GO:0048762; P:mesenchymal cell differentiation; IGI:MGI.
GO; GO:0030901; P:midbrain development; IMP:MGI.
GO; GO:0042474; P:middle ear morphogenesis; IMP:MGI.
GO; GO:0090272; P:negative regulation of fibroblast growth factor production; IGI:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0021769; P:orbitofrontal cortex development; IMP:UniProtKB.
GO; GO:0001759; P:organ induction; IMP:MGI.
GO; GO:0042473; P:outer ear morphogenesis; IMP:MGI.
GO; GO:0048339; P:paraxial mesoderm development; IGI:MGI.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
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:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:2000546; P:positive regulation of endothelial cell chemotaxis to fibroblast growth factor; ISO:MGI.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
GO; GO:0090080; P:positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway; IGI:MGI.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI.
GO; GO:1903465; P:positive regulation of mitotic cell cycle DNA replication; IDA:MGI.
GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; IGI:MGI.
GO; GO:2000830; P:positive regulation of parathyroid hormone secretion; IGI:MGI.
GO; GO:0010863; P:positive regulation of phospholipase C activity; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
GO; GO:0060665; P:regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling; IDA:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:2001239; P:regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0048378; P:regulation of lateral mesodermal cell fate specification; IGI:MGI.
GO; GO:0051174; P:regulation of phosphorus metabolic process; IGI:MGI.
GO; GO:0007435; P:salivary gland morphogenesis; IMP:MGI.
GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
GO; GO:0001657; P:ureteric bud development; IGI:MGI.
GO; GO:0007037; P:vacuolar phosphate transport; IGI:MGI.
GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; TAS:DFLAT.
GO; GO:0021847; P:ventricular zone neuroblast division; IMP:UniProtKB.
GO; GO:0070640; P:vitamin D3 metabolic process; IGI:MGI.
CDD; cd05098; PTKc_FGFR1; 1.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR028174; FGF_rcpt_1.
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; IPR013151; Immunoglobulin.
InterPro; IPR011009; Kinase-like_dom_sf.
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; PF00047; ig; 1.
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; ATP-binding; Cell membrane;
Complete proteome; Cytoplasm; Cytoplasmic vesicle; Disulfide bond;
Glycoprotein; Heparin-binding; Immunoglobulin domain; Kinase;
Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 822 Fibroblast growth factor receptor 1.
/FTId=PRO_0000016781.
TOPO_DOM 22 376 Extracellular. {ECO:0000255}.
TRANSMEM 377 397 Helical. {ECO:0000255}.
TOPO_DOM 398 822 Cytoplasmic. {ECO:0000255}.
DOMAIN 25 119 Ig-like C2-type 1.
DOMAIN 158 246 Ig-like C2-type 2.
DOMAIN 255 357 Ig-like C2-type 3.
DOMAIN 478 767 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 484 490 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 562 564 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 160 177 Heparin-binding.
ACT_SITE 623 623 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 514 514 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 568 568 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 627 627 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 641 641 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 766 766 Mediates interaction with PLCG1 and SHB.
{ECO:0000250}.
MOD_RES 463 463 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P11362}.
MOD_RES 583 583 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P11362}.
MOD_RES 585 585 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P11362}.
MOD_RES 653 653 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P11362}.
MOD_RES 654 654 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P11362}.
MOD_RES 730 730 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P11362}.
MOD_RES 766 766 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P11362}.
CARBOHYD 77 77 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 117 117 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 227 227 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 317 317 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 55 101 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 178 230 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 277 341 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 30 30 Q -> QGSSSWPLWVAAA (in isoform 3).
{ECO:0000303|PubMed:1708247}.
/FTId=VSP_002961.
VAR_SEQ 31 119 Missing (in isoform 2, isoform 4 and
isoform 5). {ECO:0000303|PubMed:10821861,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:2161540,
ECO:0000303|PubMed:7897669}.
/FTId=VSP_002962.
VAR_SEQ 148 149 Missing (in isoform 3, isoform 4, isoform
5 and isoform 6).
{ECO:0000303|PubMed:10821861,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1708247,
ECO:0000303|PubMed:2161096}.
/FTId=VSP_002963.
VAR_SEQ 313 323 TAGVNTTDKEM -> HSGINSSDA (in isoform 5).
{ECO:0000303|PubMed:10821861}.
/FTId=VSP_041919.
VAR_SEQ 327 336 HLRNVSFEDA -> TLFNVTEAQS (in isoform 5).
{ECO:0000303|PubMed:10821861}.
/FTId=VSP_041920.
VAR_SEQ 340 352 TCLAGNSIGLSHH -> VCKVSNYIGEANQ (in
isoform 5).
{ECO:0000303|PubMed:10821861}.
/FTId=VSP_041921.
VAR_SEQ 359 360 LE -> TRPVAK (in isoform 5).
{ECO:0000303|PubMed:10821861}.
/FTId=VSP_041922.
CONFLICT 229 229 T -> S (in Ref. 4; AAA37622).
{ECO:0000305}.
CONFLICT 256 258 ILQ -> HPS (in Ref. 1; AAA37290 and 3;
AAA37620). {ECO:0000305}.
CONFLICT 265 265 K -> E (in Ref. 5; AAC52183).
{ECO:0000305}.
CONFLICT 270 270 G -> A (in Ref. 4; AAA37622).
{ECO:0000305}.
CONFLICT 387 387 I -> M (in Ref. 3; AAA37620).
{ECO:0000305}.
CONFLICT 440 440 G -> A (in Ref. 2; CAA36175).
{ECO:0000305}.
CONFLICT 457 457 L -> P (in Ref. 5; AAC52183).
{ECO:0000305}.
CONFLICT 508 508 V -> L (in Ref. 3; AAA37620).
{ECO:0000305}.
CONFLICT 544 544 I -> M (in Ref. 4; AAA37622).
{ECO:0000305}.
CONFLICT 549 549 G -> E (in Ref. 6; AAF05312).
{ECO:0000305}.
CONFLICT 753 753 D -> V (in Ref. 6; AAF05312).
{ECO:0000305}.
CONFLICT 756 756 R -> H (in Ref. 1; AAA37290).
{ECO:0000305}.
CONFLICT 763 763 N -> S (in Ref. 5; AAC52183).
{ECO:0000305}.
CONFLICT 765 765 E -> D (in Ref. 4; AAA37622).
{ECO:0000305}.
STRAND 43 45 {ECO:0000244|PDB:2CKN}.
STRAND 51 54 {ECO:0000244|PDB:2CKN}.
STRAND 57 60 {ECO:0000244|PDB:2CKN}.
STRAND 63 68 {ECO:0000244|PDB:2CKN}.
STRAND 77 81 {ECO:0000244|PDB:2CKN}.
STRAND 83 90 {ECO:0000244|PDB:2CKN}.
HELIX 93 95 {ECO:0000244|PDB:2CKN}.
STRAND 96 105 {ECO:0000244|PDB:2CKN}.
STRAND 108 118 {ECO:0000244|PDB:2CKN}.
SEQUENCE 822 AA; 91981 MW; D5A4695FA680926B CRC64;
MWGWKCLLFW AVLVTATLCT ARPAPTLPEQ AQPWGVPVEV ESLLVHPGDL LQLRCRLRDD
VQSINWLRDG VQLVESNRTR ITGEEVEVRD SIPADSGLYA CVTSSPSGSD TTYFSVNVSD
ALPSSEDDDD DDDSSSEEKE TDNTKPNRRP VAPYWTSPEK MEKKLHAVPA AKTVKFKCPS
SGTPNPTLRW LKNGKEFKPD HRIGGYKVRY ATWSIIMDSV VPSDKGNYTC IVENEYGSIN
HTYQLDVVER SPHRPILQAG LPANKTVALG SNVEFMCKVY SDPQPHIQWL KHIEVNGSKI
GPDNLPYVQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT CLAGNSIGLS HHSAWLTVLE
ALEERPAVMT SPLYLEIIIY CTGAFLISCM LGSVIIYKMK 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 YPGVPVEELF KLLKEGHRMD
KPSNCTNELY MMMRDCWHAV PSQRPTFKQL VEDLDRIVAL TSNQEYLDLS IPLDQYSPSF
PDTRSSTCSS GEDSVFSHEP LPEEPCLPRH PTQLANSGLK RR


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