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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //