ID   E9PVU6_MOUSE            Unreviewed;       820 AA.
AC   E9PVU6;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 99.
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:ENSMUSP00000112992.2,
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:ENSMUSP00000112992.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000112992.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000112992.2,
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:ENSMUSP00000112992.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000112992.2};
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; E9PVU6; -.
DR   SMR; E9PVU6; -.
DR   jPOST; E9PVU6; -.
DR   MaxQB; E9PVU6; -.
DR   ProteomicsDB; 304198; -.
DR   Antibodypedia; 4393; 1532 antibodies from 47 providers.
DR   Ensembl; ENSMUST00000117089.8; ENSMUSP00000112992.2; ENSMUSG00000030849.19.
DR   UCSC; uc009jzr.1; mouse.
DR   AGR; MGI:95523; -.
DR   MGI; MGI:95523; Fgfr2.
DR   VEuPathDB; HostDB:ENSMUSG00000030849; -.
DR   GeneTree; ENSGT00940000155447; -.
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; E9PVU6; 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; 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; 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; 2.
DR   Pfam; PF13927; Ig_3; 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|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, ECO:0000256|PIRSR:PIRSR000628-
KW   4}; 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:E9PVU6,
KW   ECO:0007829|ProteomicsDB:E9PVU6}; 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..820
FT                   /note="Fibroblast growth factor receptor 2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003242986"
FT   TRANSMEM        379..399
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          256..356
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          480..769
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        625
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-1"
FT   BINDING         486..492
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         516
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         564..566
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         570
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         629
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         643
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-4"
FT   CARBOHYD        123
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-4"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-4"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-4"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-4"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-4"
FT   CARBOHYD        318
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-4"
FT   CARBOHYD        329
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-4"
FT   DISULFID        62..107
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT   DISULFID        179..231
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT   DISULFID        278..340
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|Ensembl:ENSMUSP00000112992.2"
SQ   SEQUENCE   820 AA;  92111 MW;  E0E9125022406DE2 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
     NHTYHLDVVE RSPHRPILQA GLPANASTVV GGDVEFVCKV YSDAQPHIQW IKHVEKNGSK
     YGPDGLPYLK VLKHSGINSS NAEVLALFNV TEMDAGEYIC KVSNYIGQAN QSAWLTVLPK
     QQAPVREKEI TASPDYLEIA IYCIGVFLIA CMVVTVIFCR MKTTTKKPDF SSQPAVHKLT
     KRIPLRRQVS AESSSSMNSN TPLVRITTRL SSTADTPMLA GVSEYELPED PKWEFPRDKL
     TLGKPLGEGC FGQVVMAEAV GIDKDKPKEA VTVAVKMLKD DATEKDLSDL VSEMEMMKMI
     GKHKNIINLL GACTQDGPLY VIVEYASKGN LREYLRARRP PGMEYSYDIN RVPEEQMTFK
     DLVSCTYQLA RGMEYLASQK CIHRDLAARN VLVTENNVMK IADFGLARDI NNIDYYKKTT
     NGRLPVKWMA PEALFDRVYT HQSDVWSFGV LMWEIFTLGG SPYPGIPVEE LFKLLKEGHR
     MDKPTNCTNE LYMMMRDCWH AVPSQRPTFK QLVEDLDRIL TLTTNEEYLD LTQPLEQYSP
     SYPDTRSSCS SGDDSVFSPD PMPYEPCLPQ YPHINGSVKT
//