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 23-FEB-2022, entry version 92. 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 and RT mesenchyme cells of the ascidian Halocynthia roretzi."; RL Development 128:2711-2721(2001). CC -!- FUNCTION: Receptor for basic fibroblast growth factor. 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:0000255|PROSITE-ProRule:PRU10028}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- DEVELOPMENTAL STAGE: Maternally expressed transcript was ubiquitously CC distributed in fertilized eggs and in early embryos. Zygotic expression CC became evident by the neurula stage and transcripts were detected in CC epidermal cells of the posterior half of embryos. CC {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 --------------------------------------------------------------------------- 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 SMR; Q95YM9; -. 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:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:RHEA. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 2. 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; 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; 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; 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; Kinase; KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Repeat; Signal; KW Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase. FT SIGNAL 1..27 FT /evidence="ECO:0000255" FT CHAIN 28..763 FT /note="Fibroblast growth factor receptor" FT /id="PRO_0000249215" FT TOPO_DOM 28..291 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 292..312 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 313..763 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 73..164 FT /note="Ig-like C2-type 1" FT DOMAIN 173..270 FT /note="Ig-like C2-type 2" FT DOMAIN 382..672 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT NP_BIND 388..396 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 34..74 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 691..742 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 691..709 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 717..742 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 537 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 417 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 568 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250" FT CARBOHYD 158 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 182 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 220 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 230 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 243 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 288 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 98..148 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 195..254 FT /evidence="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 //