FGFR2_DUGJA
ID FGFR2_DUGJA Reviewed; 887 AA.
AC Q8MY85;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Fibroblast growth factor receptor 2;
DE Short=DjFgfr2;
DE Short=FGFR-2;
DE EC=2.7.10.1;
DE AltName: Full=DjPTK1;
DE Flags: Precursor;
GN Name=FGFR2;
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}.
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DR EMBL; AB074426; BAB92086.1; -; mRNA.
DR AlphaFoldDB; Q8MY85; -.
DR SMR; Q8MY85; -.
DR PRIDE; Q8MY85; -.
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; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
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; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..887
FT /note="Fibroblast growth factor receptor 2"
FT /id="PRO_0000249213"
FT TOPO_DOM 19..416
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..887
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..115
FT /note="Ig-like C2-type 1"
FT DOMAIN 180..260
FT /note="Ig-like C2-type 2"
FT DOMAIN 297..387
FT /note="Ig-like C2-type 3"
FT DOMAIN 585..862
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 728
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 591..599
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 619
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 757
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
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 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 313..380
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 887 AA; 101683 MW; E8E847A58F710D86 CRC64;
MLNKFIVIVT MLAMWNYAQD CNFELSKNET VQFTSFLPLI LNCASISKFD TDLCETINDE
RPYNWYFQNK KIGNETKGKI KLVSSSQQMI IFNGSASDEG NYMCETINNN KEFISKTFDA
RMIEPSMTQM ELLLNSFPND HQEEINGRIY WLPEMILNHI RDVVIINQGA ESDLHSFYYV
SGSDSQISTF DVQWYFHYQP KSEDKTIIDH NIKTFYSSCN DLDLLPRKVN GSCYSSRLYL
YNVEIKDQGF YSVEATLRMK NGSSHGLNFT YELKINIANI LDPDKTNSIL STPQISFNLN
SRVCINDRFD WICKVTPVVS YYVTIYKNNS NPNNITVLAE SEVLQMNIDG NSGQGFYLKS
STVNYSVNSV QREHAGVYAC RIINFKDYSS DHQNRHEPEV LMRLTVKDCV GNSYFTIIWY
SISVGIIILV VISFLIIRLY NKYSNGYIVK TVIVQHPNKL YVPHDTCFPL LMPDITIKTI
HKHINSSEDS LLQQKHFTNN SNIPFSQKIS KYFRKSFIFS YRHVDVSSSN LDSPLGVISN
TETNKLTSNS LTVETQRPQL ILQNDANTKY ILPSNIGWIF SRDSLIIGSK IGEGAFGIVY
SALVKSFSEN SASVEVAIKT LHTSFGDQDV INLIQELEMM KIIGRHRHII SLYGACIDNG
HPYMVIELAK HGNLRDFLRA QRSQSKVGEI QNSGGLVTRL TVTDFLRFSI EIAEGMEYLS
SRKIIHRDLA ARNVLVDQYV EMKIADFGLT RIVENYYRKT TDGRLPIKWM APECLLDRVY
TVKSDVWSYG IVLWEIFTMG QTPYPTIQSD GMHQALRNGI RNEKPALASD EMYRLMLTIW
NDDPLERHTF SEIIDKLTHI QLSNGGSSPK RDYLEISSNQ CYSTTIV
