ID   A4QN31_DANRE            Unreviewed;       728 AA.
AC   A4QN31;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Fibroblast growth factor receptor {ECO:0000256|PIRNR:PIRNR000628};
DE            EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR000628};
GN   Name=fgfr2 {ECO:0000313|EMBL:AAI34808.1,
GN   ECO:0000313|RefSeq:NP_001229935.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-030323-1};
GN   Synonyms=fc56c05 {ECO:0000313|RefSeq:NP_001229935.1}, wu:fc56c05
GN   {ECO:0000313|RefSeq:NP_001229935.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI34808.1};
RN   [1] {ECO:0000313|RefSeq:NP_001229935.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229935.1};
RX   PubMed=8622866;
RA   Kiefer P., Mathieu M., Mason I., Dickson C.;
RT   "Secretion and mitogenic activity of zebrafish FGF3 reveal intermediate
RT   properties relative to mouse and Xenopus homologues.";
RL   Oncogene 12:1503-1511(1996).
RN   [2] {ECO:0000313|RefSeq:NP_001229935.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229935.1};
RX   PubMed=14516681; DOI=10.1016/s0925-4773(03)00112-6;
RA   Tonou-Fujimori N., Takahashi M., Onodera H., Kikuta H., Koshida S.,
RA   Takeda H., Yamasu K.;
RT   "Expression of the FGF receptor 2 gene (fgfr2) during embryogenesis in the
RT   zebrafish Danio rerio.";
RL   Mech. Dev. 119 Suppl 1:S173-S178(2002).
RN   [3] {ECO:0000313|RefSeq:NP_001229935.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229935.1};
RX   PubMed=16077091;
RA   Nechiporuk A., Linbo T., Raible D.W.;
RT   "Endoderm-derived Fgf3 is necessary and sufficient for inducing
RT   neurogenesis in the epibranchial placodes in zebrafish.";
RL   Development 132:3717-3730(2005).
RN   [4] {ECO:0000313|RefSeq:NP_001229935.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229935.1};
RX   PubMed=16109975;
RA   Woods I.G., Wilson C., Friedlander B., Chang P., Reyes D.K., Nix R.,
RA   Kelly P.D., Chu F., Postlethwait J.H., Talbot W.S.;
RT   "The zebrafish gene map defines ancestral vertebrate chromosomes.";
RL   Genome Res. 15:1307-1314(2005).
RN   [5] {ECO:0000313|RefSeq:NP_001229935.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229935.1};
RX   PubMed=16488878; DOI=10.1016/j.cub.2006.01.055;
RA   Hirate Y., Okamoto H.;
RT   "Canopy1, a novel regulator of FGF signaling around the midbrain-hindbrain
RT   boundary in zebrafish.";
RL   Curr. Biol. 16:421-427(2006).
RN   [6] {ECO:0000313|EMBL:AAI34808.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000313|EMBL:AAI34808.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [8] {ECO:0000313|RefSeq:NP_001229935.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229935.1};
RX   PubMed=30014845;
RA   Aman A.J., Fulbright A.N., Parichy D.M.;
RT   "Wnt/beta-catenin regulates an ancient signaling network during zebrafish
RT   scale development.";
RL   Elife 7:e37001-e37001(2018).
RN   [9] {ECO:0000313|RefSeq:NP_001229935.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229935.1};
RX   PubMed=30542405;
RA   Chen K., Wang C., Fan Y., Gu J., Han Z., Wang Y., Gao L., Zeng H.;
RT   "Identification of mundoserone by zebrafish in vivo screening as a natural
RT   product with anti-angiogenic activity.";
RL   Exp. Ther. Med. 16:4562-4568(2018).
RN   [10] {ECO:0000313|RefSeq:NP_001229935.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229935.1};
RX   PubMed=30174136;
RA   Wang Y., Han Y., Xu P., Ding S., Li G., Jin H., Meng Y., Meng A., Jia S.;
RT   "prpf4 is essential for cell survival and posterior lateral line primordium
RT   migration in zebrafish.";
RL   J. Genet. Genomics 45:443-453(2018).
RN   [11] {ECO:0000313|RefSeq:NP_001229935.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229935.1};
RX   PubMed=30447699;
RA   Goldshmit Y., Tang J.K.K.Y., Siegel A.L., Nguyen P.D., Kaslin J.,
RA   Currie P.D., Jusuf P.R.;
RT   "Different Fgfs have distinct roles in regulating neurogenesis after spinal
RT   cord injury in zebrafish.";
RL   Neural Dev. 13:24-24(2018).
RN   [12] {ECO:0000313|RefSeq:NP_001229935.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229935.1};
RX   PubMed=30681411;
RA   Lush M.E., Diaz D.C., Koenecke N., Baek S., Boldt H., St Peter M.K.,
RA   Gaitan-Escudero T., Romero-Carvajal A., Busch-Nentwich E.M., Perera A.G.,
RA   Hall K.E., Peak A., Haug J.S., Piotrowski T.;
RT   "scRNA-Seq reveals distinct stem cell populations that drive hair cell
RT   regeneration after loss of Fgf and Notch signaling.";
RL   Elife 8:e44431-e44431(2019).
RN   [13] {ECO:0000313|RefSeq:NP_001229935.1}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001229935.1};
RG   RefSeq;
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   -!- INTERACTION:
CC       A4QN31; Q7SX76: fgfrl1; NbExp=2; IntAct=EBI-10834257, EBI-1579511;
CC       A4QN31; Q5K373: fgfrl1b beta; NbExp=2; IntAct=EBI-10834257, EBI-42470198;
CC       A4QN31; Q8AXB3: kdrl; NbExp=2; IntAct=EBI-10834257, EBI-2267980;
CC       A4QN31; B8JKM0: lrrtm1; NbExp=2; IntAct=EBI-10834257, EBI-2462996;
CC       A4QN31; A0A8M9Q8Q6: vstm4b; NbExp=2; IntAct=EBI-10834257, EBI-42471179;
CC       A4QN31; Q8UVD6: wu:fa16d03; NbExp=2; IntAct=EBI-10834257, EBI-2268159;
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}.
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   EMBL; BC134807; AAI34808.1; -; mRNA.
DR   RefSeq; NP_001229935.1; NM_001243006.1.
DR   IntAct; A4QN31; 7.
DR   GeneID; 352940; -.
DR   AGR; ZFIN:ZDB-GENE-030323-1; -.
DR   CTD; 2263; -.
DR   ZFIN; ZDB-GENE-030323-1; fgfr2.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000000437; Chromosome 13.
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:0016310; P:phosphorylation; 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; cd05858; IgI_3_FGFR2; 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; 2.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF000628; FGFR; 1.
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|PIRNR:PIRNR000628};
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|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};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000628};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001229935.1};
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..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..728
FT                   /note="Fibroblast growth factor receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP,
FT                   ECO:0000313|RefSeq:NP_001229935.1"
FT                   /id="PRO_5035035402"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          70..158
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          167..269
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          388..677
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          37..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..54
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..376
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        533
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-1"
FT   BINDING         394..400
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         424
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         472..474
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         478
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         537
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   BINDING         551
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT   DISULFID        90..142
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT   DISULFID        189..253
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
SQ   SEQUENCE   728 AA;  81771 MW;  14898E3DBE3883F6 CRC64;
     MFARGWLLGA LLLMTLATVS VARPSLKIDL VNTSAPEDAI SSGDDEDDTE RSDDVGADGE
     QMRLPYWTFP EKMEKKLHAV PAANTVKFRC AAAGNPKPKM RWLKNAKPFR QEDRMGGYKV
     RLQHWTLIME SVVPSDKGNY TCLVENQYGS INHTYTLDVV ERSPHRPILQ AGLPANVTVQ
     VGQDAKFVCK VYSDAQPHIQ WLQHYTKNGS RYGPDGLPYV RVLKTAGVNT TDKEIEVLYL
     PNVTFEDAGE YTCLAGNSIG ISYHTAWLTV HPAETNPIET DYPPDYVEIA IYCIGVFLIA
     CMVVIVVVCR MRTSAKKPDF SSQPAVHKLT KQIPLRRQVT VSSDSSSSMS SSTPLVRITT
     RRSSAHDDPI PEYDLPEDPR WEFSRDKLTL GKPLGEGCFG QVVMAEALGI DKDKPKEAVT
     VAVKMLKDDA TEKDLSDLVS EMEMMKMIGR HKNIINLLGA CTQDGPLYVI VEYASKGNLR
     EYLRARRPPG MEYSYDIARV SDEPLTFKDL VSCTYQVARG MEYLASQKCI HRDLAARNVL
     VTESNVMKIA DFGLARDVHN IDYYKKTTNG RLPVKWMAPE ALFDRVYTHQ SDVWSFGVLM
     WEIFTLGGSP YPGIPVEELF KLLKEGHRMD KPANCTNELY MMMKDCWHAI SSHRPTFKQL
     VEDLDRILTL ATNEEYLDLC APVEQYSPSF PDTRSSCSSG DDSVFSHDPL ADEPCLPKYQ
     HINGGIKT
//