ID FGFR_HALRO Reviewed; 763 AA. AC Q95YM9; DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 16-SEP-2015, entry version 73. DE RecName: Full=Fibroblast growth factor receptor; DE Short=HrFGFR; DE EC=2.7.10.1; DE Flags: Precursor; GN Name=FGFR; OS Halocynthia roretzi (Sea squirt) (Cynthia roretzi). OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia; OC Pyuridae; Halocynthia. OX NCBI_TaxID=7729; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE. RX PubMed=11526077; RA Shimauchi Y., Murakami S.D., Satoh N.; RT "FGF signals are involved in the differentiation of notochord cells RT and mesenchyme cells of the ascidian Halocynthia roretzi."; RL Development 128:2711-2721(2001). CC -!- FUNCTION: Receptor for basic fibroblast growth factor. CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a CC [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE- CC ProRule:PRU10028}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- DEVELOPMENTAL STAGE: Maternally expressed transcript was CC ubiquitously distributed in fertilized eggs and in early embryos. CC Zygotic expression became evident by the neurula stage and CC transcripts were detected in epidermal cells of the posterior half CC of embryos. {ECO:0000269|PubMed:11526077}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. Fibroblast growth factor receptor subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like) CC domains. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. 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 EMBL; AB046873; BAB59007.1; -; mRNA. DR ProteinModelPortal; Q95YM9; -. DR PRIDE; Q95YM9; -. DR HOVERGEN; HBG000345; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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 proliferation; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 2. DR InterPro; IPR016248; FGF_rcpt_fam. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR013098; Ig_I-set. DR InterPro; IPR003598; Ig_sub2. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR Pfam; PF07679; I-set; 2. DR Pfam; PF07714; Pkinase_Tyr; 1. DR PIRSF; PIRSF000628; FGFR; 1. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00408; IGc2; 2. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF48726; SSF48726; 2. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS50835; IG_LIKE; 2. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. PE 2: Evidence at transcript level; KW ATP-binding; Disulfide bond; Glycoprotein; Immunoglobulin domain; KW Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Receptor; KW Repeat; Signal; Transferase; Transmembrane; Transmembrane helix; KW Tyrosine-protein kinase. FT SIGNAL 1 27 {ECO:0000255}. FT CHAIN 28 763 Fibroblast growth factor receptor. FT /FTId=PRO_0000249215. FT TOPO_DOM 28 291 Extracellular. {ECO:0000255}. FT TRANSMEM 292 312 Helical. {ECO:0000255}. FT TOPO_DOM 313 763 Cytoplasmic. {ECO:0000255}. FT DOMAIN 73 164 Ig-like C2-type 1. FT DOMAIN 173 270 Ig-like C2-type 2. FT DOMAIN 382 672 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 388 396 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT ACT_SITE 537 537 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10028}. FT BINDING 417 417 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT MOD_RES 568 568 Phosphotyrosine; by autocatalysis. FT {ECO:0000250}. FT CARBOHYD 158 158 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 182 182 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 220 220 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 230 230 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 243 243 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 288 288 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 98 148 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 195 254 {ECO:0000255|PROSITE-ProRule:PRU00114}. SQ SEQUENCE 763 AA; 86741 MW; A34C1871DB796950 CRC64; MKEFEVKVAS TAFVLVLFSL TINQILASET STKFRSPVPA PTVPDWNHLP NEGNEENVVS APKQDGASGG QKPYWTKREK MMKRLHAEPA GNTVRFRCAV DGNPKPQVLW YKNDLIVQKN DRVGGYKYRN QVLILESVVL SDKGNYMCVA RNEYGSINHT YQLDVQERSA SKPILAEGLP QNKSAYIGDD VTFKCKVYSD AHPHIQWLKS INNHNNAAPN YTVLKAAGVN TTDLDMEVLI LKNVSFEEAG EYTCLAGNSI GISHQSAWLS VLPVPPPTTD TITKGIPNET NIIIYVMCGV LVILFGLAVV LVLYYHCYNG KDPPMLVRIE NPDNIPPMTK IEHPTMLFGN TQAWQRMCMP MQEPFEFNIQ LDLQWELQRE DITLVERLDE GFFGQVFKAD LVTCNNTRKE KMVCAVKMLK GNRNEKDVLD LLTEMDQMKR VGKHKNIINL LGVCTQNGPL WLVIEYAAQG NLRDYLRRNR PQNTLCNLVL PSEGRNPDDE LPVPHGDTLT QKDIVSFAFQ VARGLEFLAQ KKCIHRDLAA RNVLVTEELV MKIADFGLAR DIRSCDYYRK HTRGHLPYKW MALEAMSDNI FTHATDVWSF GVLLWEIFSL AGSPYPGIKT HELVKFLRSG ERLDKPQYAS QEMYRLMRDC WEEDPSKRPN FRTLVEDLDR MLAESSTEVY IDFAAGCEAE YSESSEDESE SQNSDEEDDD SVFERMRQID SLSNGNIPFN EEDSSNSDPY VAPLLQNEEN VLQNEHARLR SEA //