ID   A0A3P9B138_9CICH        Unreviewed;       817 AA.
AC   A0A3P9B138;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   10-FEB-2021, entry version 12.
DE   RecName: Full=Fibroblast growth factor receptor {ECO:0000256|PIRNR:PIRNR000628};
DE            EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR000628};
OS   Maylandia zebra (zebra mbuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX   NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005003660, ECO:0000313|Proteomes:UP000265160};
RN   [1] {ECO:0000313|Ensembl:ENSMZEP00005003660, ECO:0000313|Proteomes:UP000265160}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25186727; DOI=10.1038/nature13726;
RA   Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA   Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA   Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA   Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA   Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA   Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA   Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA   Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA   Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA   Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA   Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA   Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA   Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA   Di Palma F.;
RT   "The genomic substrate for adaptive radiation in African cichlid fish.";
RL   Nature 513:375-381(2014).
RN   [2] {ECO:0000313|Ensembl:ENSMZEP00005003660}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2018) 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. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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   Ensembl; ENSMZET00005003813; ENSMZEP00005003660; ENSMZEG00005002787.
DR   GeneTree; ENSGT00940000159880; -.
DR   Proteomes; UP000265160; LG19.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005007; F:fibroblast growth factor-activated receptor activity; IEA:InterPro.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR016248; FGF_rcpt_fam.
DR   InterPro; IPR041159; FGFR_TM.
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   Pfam; PF18123; FGFR3_TM; 1.
DR   Pfam; PF07679; I-set; 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; SSF48726; 3.
DR   SUPFAM; SSF56112; SSF56112; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000628};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000628};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000628,
KW   ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000628};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000628};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {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..41
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           42..817
FT                   /note="Fibroblast growth factor receptor"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018227582"
FT   TRANSMEM        381..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          51..140
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          155..254
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          263..352
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          477..756
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          781..817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        622
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000628-1"
SQ   SEQUENCE   817 AA;  91504 MW;  C5D97EDE06C62DB1 CRC64;
     MLSKLESGLA ALRLTSSPRG MTALWCSLWL SLLLPLTVVP AGLPTAQPTD PVSSETAFLE
     DYVLGIGDTL EMSCDPEEQE DHTEPIVWLK DGAGLVPCNR IRLGQRILRI INVSYDDSGV
     YSCHLARSNT LLSNYTIRVT DSLSSGDDED YDEDPEGAEA PYWTRPERMD KKLLAVPAAN
     TVKFRCAASG NPPPTIHWLK NGKEFKGEQR MGGIKLRHQQ WSLVMESAVP SDRGNYTCVV
     QNKYGSISHT YQLDVLERSP HRPILQAGLP ANQTVVVGSN VEFHCKVYSD AQPHIQWLKH
     IEVNGSRLGP DGVPYVNVLK SVVSKHIETH SKLKLSNVTE KDAGKYWCRA SNFVGKSENA
     FWLNIYKPAV SPQKEDYYAD ILIYVTGCVL FILAVVIAIL CRMRMTTQKT LPTPPVQKLS
     KFPLKRQVSL DSNSSMNSNT PLVRIARLSS SDGPMLANVS ELELPSDPKW EFPRTRLTLG
     KPLGEGCFGQ VVMAEAVGID KEKPNKSLTV AVKMLKDDAT DKDLSDLVSE MEMMKMIGKH
     KNIINLLGAC TQDGPLYVLV EYASKGNLRE YLRARRPPGM DYSFDTCKIP DEQLTFKDLV
     SCAYQVARGM EYLASQKCIH RDLAARNVLV TEDNVMKIAD FGLARDVHNI DYYKKTTNGR
     LPVKWMAPEA LFDRVYTHQS DVWSYGVLLW EIFTLGGSPY PGIPVEELFK LLKEGHRMDK
     PANCTHELYM IMRECWHAVP SQRPTFRQLV EDHDRILSMT STDEYLDLSV PFEQYSPTCQ
     DSNSTCSSGD DSVFAHDPLP DEPCLPKQLP SNGVIRT
//