ID   E9QNJ9_MOUSE            Unreviewed;       802 AA.
AC   E9QNJ9;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Fibroblast growth factor receptor {ECO:0000256|PIRNR:PIRNR000628};
DE            EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR000628};
GN   Name=Fgfr3 {ECO:0000313|Ensembl:ENSMUSP00000110053.3,
GN   ECO:0000313|MGI:MGI:95524};
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 {ECO:0000313|Ensembl:ENSMUSP00000110053.3, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000110053.3, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000110053.3,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [3] {ECO:0000313|Ensembl:ENSMUSP00000110053.3}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000110053.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001171,
CC         ECO:0000256|PIRNR:PIRNR000628};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Fibroblast growth factor receptor subfamily.
CC       {ECO:0000256|PIRNR:PIRNR000628}.
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DR   RefSeq; NP_001156689.1; NM_001163217.2.
DR   RefSeq; XP_006503791.1; XM_006503728.1.
DR   ProteomicsDB; 340689; -.
DR   Antibodypedia; 3787; 844 antibodies from 45 providers.
DR   DNASU; 14184; -.
DR   Ensembl; ENSMUST00000114411.9; ENSMUSP00000110053.3; ENSMUSG00000054252.19.
DR   Ensembl; ENSMUST00000171509.9; ENSMUSP00000131845.3; ENSMUSG00000054252.19.
DR   GeneID; 14184; -.
DR   UCSC; uc012dut.2; mouse.
DR   AGR; MGI:95524; -.
DR   CTD; 2261; -.
DR   MGI; MGI:95524; Fgfr3.
DR   VEuPathDB; HostDB:ENSMUSG00000054252; -.
DR   GeneTree; ENSGT00940000159880; -.
DR   OMA; RPANCTH; -.
DR   OrthoDB; 1614410at2759; -.
DR   TreeFam; TF316307; -.
DR   BioGRID-ORCS; 14184; 0 hits in 77 CRISPR screens.
DR   ChiTaRS; Fgfr3; mouse.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000054252; Expressed in ventricular zone and 261 other cell types or tissues.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030133; C:transport vesicle; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017134; F:fibroblast growth factor binding; IEA:Ensembl.
DR   GO; GO:0005007; F:fibroblast growth factor receptor activity; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR   GO; GO:0007267; P:cell-cell signaling; IEA:Ensembl.
DR   GO; GO:1902178; P:fibroblast growth factor receptor apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR   CDD; cd05857; IgI_2_FGFR; 1.
DR   CDD; cd04974; IgI_3_FGFR; 1.
DR   CDD; cd05100; PTKc_FGFR3; 1.
DR   Gene3D; 6.10.250.1740; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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:SF505; FIBROBLAST GROWTH FACTOR RECEPTOR 3; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF21165; FGFR3_TM; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000628};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR000628-3};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000628};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000628};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000628, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteomics identification {ECO:0007829|MaxQB:E9QNJ9,
KW   ECO:0007829|ProteomicsDB:E9QNJ9};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000628};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000628};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW   ECO:0000256|PIRNR:PIRNR000628}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..802
FT                   /note="Fibroblast growth factor receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015090380"
FT   TRANSMEM        368..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          39..108
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          145..238
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          247..336
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          468..757
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          125..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          763..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..784
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        613
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-1"
FT   BINDING         474..480
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         504
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         552..554
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         558
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         617
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         631
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   DISULFID        59..107
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT   DISULFID        170..222
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT   DISULFID        269..332
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
SQ   SEQUENCE   802 AA;  88165 MW;  6DADCB5A2F20731F 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
     TVLKSWISEN VEADARLRLA NVSERDGGEY LCRATNFIGV AEKAFWLRVH GPQAAEEELM
     ETDEAGSVYA GVLSYGVVFF LFILVVAAVI LCRLRSPPKK GLGSPTVHKV SRFPLKRQVS
     LESNSSMNSN TPLVRIARLS SGEGPVLANV SELELPADPK WELSRTRLTL GKPLGEGCFG
     QVVMAEAIGI DKDRTAKPVT VAVKMLKDDA TDKDLSDLVS EMEMMKMIGK HKNIINLLGA
     CTQGGPLYVL VEYAAKGNLR EFLRARRPPG MDYSFDACRL PEEQLTCKDL VSCAYQVARG
     MEYLASQKCI HRDLAARNVL VTEDNVMKIA DFGLARDVHN LDYYKKTTNG RLPVKWMAPE
     ALFDRVYTHQ SDVWSFGVLL WEIFTLGGSP YPGIPVEELF KLLKEGHRMD KPASCTHDLY
     MIMRECWHAV PSQRPTFKQL VEDLDRILTV TSTDEYLDLS VPFEQYSPGG QDTPSSSSSG
     DDSVFTHDLL PPGPPSNGGP RT
//