FGFR_HYDVU
ID FGFR_HYDVU Reviewed; 816 AA.
AC Q86PM4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Fibroblast growth factor receptor;
DE EC=2.7.10.1;
DE AltName: Full=Protein kringelchen;
DE Flags: Precursor;
GN Name=FGFR;
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=15269170; DOI=10.1242/dev.01267;
RA Sudhop S., Coulier F., Bieller A., Vogt A., Hotz T., Hassel M.;
RT "Signalling by the FGFR-like tyrosine kinase, Kringelchen, is essential for
RT bud detachment in Hydra vulgaris.";
RL Development 131:4001-4011(2004).
CC -!- FUNCTION: Receptor for basic fibroblast growth factor. {ECO:0000305}.
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: During tissue displacement in the early bud,
CC transiently present ubiquitously. A few hours later, coincident with
CC the acquisition of organiser properties by the bud tip, a few cells in
CC the apical tip express the gene strongly. About 20 hours after the
CC onset of evagination, expression is switched on in a ring of cells
CC surrounding the bud base, and shortly thereafter vanishes from the
CC apical expression zone. The basal ring persists in the parent during
CC tissue contraction and foot formation in the young polyp, until several
CC hours after bud detachment. Inhibition of bud detachment by head
CC regeneration results in severe distortion, disruption or even complete
CC loss of the well-defined ring-like expression zone.
CC {ECO:0000269|PubMed:15269170}.
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; AY193769; AAO39416.1; -; mRNA.
DR RefSeq; NP_001296694.1; NM_001309765.1.
DR AlphaFoldDB; Q86PM4; -.
DR SMR; Q86PM4; -.
DR PRIDE; Q86PM4; -.
DR GeneID; 100206525; -.
DR KEGG; hmg:100206525; -.
DR OrthoDB; 220433at2759; -.
DR Proteomes; UP000694840; Unplaced.
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; 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; 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; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
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; Reference proteome;
KW Repeat; Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..816
FT /note="Fibroblast growth factor receptor"
FT /id="PRO_0000249211"
FT TOPO_DOM 20..370
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..816
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..105
FT /note="Ig-like C2-type 1"
FT DOMAIN 126..217
FT /note="Ig-like C2-type 2"
FT DOMAIN 474..747
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 612
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 480..488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 643
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 147..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 816 AA; 93395 MW; 0AF9B17CA483DDD9 CRC64;
MISDWCVVLV LLMSRLVFGL NFTEPVNYIL KLGEDSSSRL LDCSVNLPVE LIKKIDWTHN
DIVINNKPNI TLSENGQKLV IAHYQSHNSG RYGCKVTAMN EESVQRVFDL LPASETEGNQ
TIEMMLRIKN DISLLVELVM NKLDLDCTAV GASPINITWI KNDRLIEARS NLSNFRYSFS
PNFLKLSIKE LRLDDAGIYK CILENKYGKI EHIMTVEIYE KMFSKPIVSS TDKHKVFYVN
YGQNLTVPIY VTAFLPHPHF QMLYVYSMTS PNTNETKLAL RVLPTMRELT VLEKGQRRGN
SISHIKLDYF FNNISEQDFG NYTFMAGNKY GFDIYPFQIL HTKYMQTTVF PPMKSSINKI
YKEESVEKTV IFIVITSMLA GLIFVAFVIF FICRVRSKDK FKNSNINYIK PLETVILNLG
DNNTSGVTMV TSVSASYASR RFRHSLNNNL INDKQKLNLK IAPDPAWEIK LEQLETDCLL
GEGAFGRVFR ATARDLPNHT GVQTVAVKML KEDCCEQDLK DFISEIEVMK SIGKHINILN
LLAVSSQQGK LYIVVEYCRH GNLRSFLKDN RPVMQANSVI TKKITLYDLT SFCLQVARGM
NFLASKKCIH RDIAARNVLV GEGYLMKIAD FGLARDIHEQ DYYRKCTDGR LPVKWMAIEA
LFDRVYTTQS DIWSFGILAW EIVTFGGSPY PGIALEKLFD LLKQGYRMER PLNCTDDMYT
LMLNCWKEIP SKRPTFSQLI EDLERMLLDA SSTEYIDLQP IQPERTESFS TSLHTSASML
NTDLHEKNKC DHDEISFTHE DGLSEADILL SHYAVS
