FGFR1_DUGJA
ID FGFR1_DUGJA Reviewed; 854 AA.
AC Q8MY86;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Fibroblast growth factor receptor 1;
DE Short=DjFgfr1;
DE Short=FGFR-1;
DE EC=2.7.10.1;
DE AltName: Full=DjPTK3;
DE Flags: Precursor;
GN Name=FGFR1;
OS Dugesia japonica (Planarian).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Seriata; Tricladida; Continenticola; Geoplanoidea;
OC Dugesiidae; Dugesia.
OX NCBI_TaxID=6161;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=GI;
RX PubMed=12060069; DOI=10.1046/j.1440-169x.2002.00634.x;
RA Ogawa K., Kobayashi C., Hayashi T., Orii H., Watanabe K., Agata K.;
RT "Planarian fibroblast growth factor receptor homologs expressed in stem
RT cells and cephalic ganglions.";
RL Dev. Growth Differ. 44:191-204(2002).
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 type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, stem cells and the mesenchymal
CC cells. {ECO:0000269|PubMed:12060069}.
CC -!- DEVELOPMENTAL STAGE: Expression is observed in the cephalic ganglion
CC and mesenchymal space in intact planarians. In regenerating planarians,
CC accumulation was observed in the blastema and in fragments regenerating
CC either a pharynx or a brain. {ECO:0000269|PubMed:12060069}.
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; AB074425; BAB92085.1; -; mRNA.
DR AlphaFoldDB; Q8MY86; -.
DR SMR; Q8MY86; -.
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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
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 Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 3.
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; Repeat; Signal;
KW Transferase; Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..854
FT /note="Fibroblast growth factor receptor 1"
FT /id="PRO_0000249212"
FT TOPO_DOM 21..383
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..854
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..120
FT /note="Ig-like C2-type 1"
FT DOMAIN 147..259
FT /note="Ig-like C2-type 2"
FT DOMAIN 268..369
FT /note="Ig-like C2-type 3"
FT DOMAIN 551..822
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 689
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 557..565
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 585
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 718
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 166..242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 288..353
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 854 AA; 98633 MW; 9367D217C9B49673 CRC64;
MSGLFFLLSE LLILLGKINS VSKKSLCHPE LFKIDNKLNW RTSEEMVLTC KAVVNEKCKK
SKLQMRWYKD NELLGKKIER GLKMKYRYRK KLKLNDSGNY TCFVFNKNGN SSVFFLINVT
EKENFHVNEN KILDGSEISN NTLYLHPEMG MENYHVIPND EIVMQCRFFS PISINLTVSW
YQHSCDSNYH NAQLLVKDSK FNISSNKESC QSYLSHIPLD SICLYSWLRF IATSDDQSCI
TCLIESDNNS IEKTKFTFTV LVDAGHRPHL TFAPSSTVCQ GSNFTMKCET NVPRPILYIY
KLDPSFNIEN PIIHLSNSTL FVNNYNEDSK RSSQSAEVLI KSMDFNYSGR YLCSLAELPL
FEIMHLSVIK CSNNFFMNSV PLSIFLVIGF FVAIILLSLI IYCFFLQYKN AVDSRKHFSI
RKTVIVEYES PIYKSFINGT KNFKTDVLHT NSLLPDSNPL LPPIIKIKPI KRLSQFRDGN
YGEQLPSTST DRTRLESTRH SQLENEVFEC GSGNNSLSLK YGLRKSSSFE FFSLYEFPCD
AKWEFPREKL KITNKKLGEG AFGMVYEGIA NDIGNRSNPI KVAVKMMRDD FSDSNVHDFV
KEMEIMKHIG RHPNVIQLLG LCTQKGPLRV IVELAPYGNL RDFVRAKNKK YSKSKKIIGN
FTSSILCTYS LQIARGMTYL ASRSVVHRDL SARNILVGEH FEMKIADFGL TRIVDYYYRK
KTDGILPVKW MAPEALLEKK YTTKSDVWSY GILLWEIFTL GDSPYSAILP EKVVDLIRKG
FQNPKPELAN FEIYRLMQHC WSLSSENRPN FFEIVEILID IIQRIDDEPE ENIYHSELNY
LKMESDYLEP KCLV
