ID   D3Z5M8_MOUSE            Unreviewed;       709 AA.
AC   D3Z5M8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Fibroblast growth factor receptor 2 {ECO:0000256|ARBA:ARBA00039656};
DE            EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
DE   Flags: Fragment;
GN   Name=Fgfr2 {ECO:0000313|Ensembl:ENSMUSP00000113474.2,
GN   ECO:0000313|MGI:MGI:95523};
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:ENSMUSP00000113474.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000113474.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000113474.2,
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:0000313|Ensembl:ENSMUSP00000113474.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000113474.2};
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC       Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}.
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DR   AlphaFoldDB; D3Z5M8; -.
DR   SMR; D3Z5M8; -.
DR   jPOST; D3Z5M8; -.
DR   MaxQB; D3Z5M8; -.
DR   ProteomicsDB; 307895; -.
DR   Antibodypedia; 4393; 1532 antibodies from 47 providers.
DR   Ensembl; ENSMUST00000120715.8; ENSMUSP00000113474.2; ENSMUSG00000030849.19.
DR   AGR; MGI:95523; -.
DR   MGI; MGI:95523; Fgfr2.
DR   VEuPathDB; HostDB:ENSMUSG00000030849; -.
DR   GeneTree; ENSGT00940000155447; -.
DR   HOGENOM; CLU_000288_74_3_1; -.
DR   ChiTaRS; Fgfr2; mouse.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000030849; Expressed in metanephric cortical collecting duct and 391 other cell types or tissues.
DR   ExpressionAtlas; D3Z5M8; baseline and differential.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005007; F:fibroblast growth factor receptor activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:InterPro.
DR   CDD; cd05857; IgI_2_FGFR; 1.
DR   CDD; cd05101; PTKc_FGFR2; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
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; 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:SF130; FIBROBLAST GROWTH FACTOR RECEPTOR 2; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF000628; FGFR; 2.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
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|PIRSR:PIRSR000628-
KW   2}; 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   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Kinase {ECO:0000256|ARBA:ARBA00023137};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteomics identification {ECO:0007829|MaxQB:D3Z5M8,
KW   ECO:0007829|ProteomicsDB:D3Z5M8}; Receptor {ECO:0000256|ARBA:ARBA00023170};
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|ARBA:ARBA00023137};
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}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..709
FT                   /note="Fibroblast growth factor receptor 2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003052432"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          39..125
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          154..247
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          369..658
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          129..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        514
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-1"
FT   BINDING         375..381
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         405
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         453..455
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         459
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         518
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         532
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   DISULFID        62..107
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT   DISULFID        179..231
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|Ensembl:ENSMUSP00000113474.2"
SQ   SEQUENCE   709 AA;  79966 MW;  225BB8CB6E1BF612 CRC64;
     MVSWGRFICL VLVTMATLSL ARPSFSLVED TTLEPEEPPT KYQISQPEAY VVAPGESLEL
     QCMLKDAAVI SWTKDGVHLG PNNRTVLIGE YLQIKGATPR DSGLYACTAA RTVDSETWYF
     MVNVTDAISS GDDEDDTDSS EDVVSENRSN QRAPYWTNTE KMEKRLHAVP AANTVKFRCP
     AGGNPTPTMR WLKNGKEFKQ EHRIGGYKVR NQHWSLIMES VVPSDKGNYT CLVENEYGSI
     NHTYHLDVVA PVREKEITAS PDYLEIAIYC IGVFLIACMV VTVIFCRMKT TTKKPDFSSQ
     PAVHKLTKRI PLRRQVTVSA ESSSSMNSNT PLVRITTRLS STADTPMLAG VSEYELPEDP
     KWEFPRDKLT LGKPLGEGCF GQVVMAEAVG IDKDKPKEAV TVAVKMLKDD ATEKDLSDLV
     SEMEMMKMIG KHKNIINLLG ACTQDGPLYV IVEYASKGNL REYLRARRPP GMEYSYDINR
     VPEEQMTFKD LVSCTYQLAR GMEYLASQKC IHRDLAARNV LVTENNVMKI ADFGLARDIN
     NIDYYKKTTN GRLPVKWMAP EALFDRVYTH QSDVWSFGVL MWEIFTLGGS PYPGIPVEEL
     FKLLKEGHRM DKPTNCTNEL YMMMRDCWHA VPSQRPTFKQ LVEDLDRILT LTTNEEYLDL
     TQPLEQYSPS YPDTRSSCSS GDDSVFSPDP MPYEPCLPQY PHINGSVKT
//