FGFR_HALRO
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 03-AUG-2022, entry version 94.
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; DOI=10.1242/dev.128.14.2711;
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}.
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DR EMBL; AB046873; BAB59007.1; -; mRNA.
DR AlphaFoldDB; Q95YM9; -.
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 receptor activity; IEA:InterPro.
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 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 388..396
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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
