ID Q9GSH3_HALRO Unreviewed; 877 AA.
AC Q9GSH3;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE RecName: Full=Fibroblast growth factor receptor {ECO:0000256|PIRNR:PIRNR000628};
DE EC=2.7.10.1 {ECO:0000256|PIRNR:PIRNR000628};
GN Name=FGFR {ECO:0000313|EMBL:AAG27717.1};
OS Halocynthia roretzi (Sea squirt) (Cynthia roretzi).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Stolidobranchia;
OC Pyuridae; Halocynthia.
OX NCBI_TaxID=7729 {ECO:0000313|EMBL:AAG27717.1};
RN [1] {ECO:0000313|EMBL:AAG27717.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=10964694; DOI=10.1006/bbrc.2000.3334;
RA Kamei S., Yajima I., Yamamoto H., Kobayashi A., Makabe K.W., Yamazaki H.,
RA Hayashi S.I., Kunisada T.;
RT "Characterization of a novel member of the FGFR family, HrFGFR, in
RT Halocynthia roretzi.";
RL Biochem. Biophys. Res. Commun. 275:503-508(2000).
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 -!- 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 EMBL; AF303661; AAG27717.1; -; mRNA.
DR AlphaFoldDB; Q9GSH3; -.
DR GO; GO:0016020; C: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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:InterPro.
DR CDD; cd00096; Ig; 1.
DR CDD; cd05053; PTKc_FGFR; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR24416:SF550; FIBROBLAST GROWTH FACTOR RECEPTOR HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000628; FGFR; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000628};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000628-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|PIRNR:PIRNR000628};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000628};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000628};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR000628};
KW 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|PIRNR:PIRNR000628}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..877
FT /note="Fibroblast growth factor receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004330642"
FT TRANSMEM 405..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..141
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 182..273
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 282..385
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 495..785
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 158..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 804..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..822
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 650
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-1"
FT BINDING 501..507
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT BINDING 530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT BINDING 578..580
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT BINDING 584
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT BINDING 654
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT BINDING 668
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-2"
FT DISULFID 207..257
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
FT DISULFID 304..367
FT /evidence="ECO:0000256|PIRSR:PIRSR000628-3"
SQ SEQUENCE 877 AA; 100158 MW; A55C20A90F85AF70 CRC64;
MKEFEVKVAS TAFVLVLFSL TINQILASET STKFRSPVPA PTVPDVTQFR TKSATANKTL
MVKRGETIRI NCRVRGYPKP NVLFYRGKKL LKNPTPDDTD PTIMRVRVLG TTLRIFPAYL
EDSGLYTCIA HNANEKNSSL SYHVEVLDDD SIKDWNHLPN EGNEENVVSA PKQDGASGGQ
KPYWTKREKM MKRLHAEPAG NTVRFRCAVD GNPKPQVLWY KNDLIVQKND RVGGYKYRNQ
VLILESVVLS DKGNYMCVAR NEYGSINHTY QLDVQERSAS RPILKFGLPA NKSVYVGQDV
EFKCEVFSDP HPHVKWLRHI EINGSRVDPK TNRDYVQIIK QSGVNETAVQ TLRLKNVTES
DSGQYTCLAE NYIGNENNSA WLVVQKVPPP TTDTITKGIP NETNIIIYVM CGVLVILFGL
AVVLVLYYHC YNGKDPPMLV RIENPDNIPP MTKIEHPTML FGNTQAWQRM CMPMQEPFEF
NIQLDLQWEL QREDITLVER LDEGFFGQVF KADLVTCNNT RKEKMVCAVK MLKGNRNEKD
VLDLLTEMDQ MKRVGKHKNI INLLGVCTQN GPLWLVIEYA AQGNLRDYLR RNRPQNTLCN
LVLPSEGRNP DDELPVPHGD TLTQKDIVSF AFQVARGLEF LAQKKCIHRD LAARNVLVTE
ELVMKIADFG LARDIRSCDY YRKHTRGHLP YKWMALEAMS DNIFTHATDV WSFGVLLWEI
FSLAGSPYPG IKTHELVKFL RSGERLDKPQ YASQEMYRLM RDCWEEDPSK RPNFRTLVED
LDRMLAESST EVYIDFAAGC EAEYSESSED ESESQNSDEE DDDSVFERMR QIDSLSNGNI
PFNEEADSSN SDPYVAPLLQ NEENVLQNEH ARLRSEA
//
