FGFR_STRPU
ID FGFR_STRPU Reviewed; 972 AA.
AC Q26614;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Fibroblast growth factor receptor;
DE Short=SpFGFR;
DE EC=2.7.10.1;
DE Flags: Precursor;
GN Name=FGFR;
OS Strongylocentrotus purpuratus (Purple sea urchin).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC Strongylocentrotus.
OX NCBI_TaxID=7668;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=8702734; DOI=10.1074/jbc.271.33.20119;
RA McCoon P.E., Angerer R.C., Angerer L.M.;
RT "SpFGFR, a new member of the fibroblast growth factor receptor family, is
RT developmentally regulated during early sea urchin development.";
RL J. Biol. Chem. 271:20119-20125(1996).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Ig3L;
CC IsoId=Q26614-1; Sequence=Displayed;
CC Name=2; Synonyms=Ig3S;
CC IsoId=Q26614-2; Sequence=VSP_020370;
CC -!- DEVELOPMENTAL STAGE: Transcripts accumulate when morphogenesis begins
CC with mesenchyme cell ingression and gastrulation. Accumulation in all
CC cell types of the embryo, although hybridization shows that they are
CC somewhat enriched in cells of oral ectoderm and endoderm. Isoform 2
CC transcript is enriched in endomesoderm.
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; U17164; AAC47258.1; -; mRNA.
DR RefSeq; NP_999702.1; NM_214537.1. [Q26614-1]
DR AlphaFoldDB; Q26614; -.
DR SMR; Q26614; -.
DR STRING; 7668.SPU_020677-tr; -.
DR PRIDE; Q26614; -.
DR EnsemblMetazoa; NM_214537; NP_999702; GeneID_373310. [Q26614-1]
DR GeneID; 373310; -.
DR KEGG; spu:373310; -.
DR CTD; 373310; -.
DR eggNOG; KOG0200; Eukaryota.
DR HOGENOM; CLU_000288_74_2_1; -.
DR InParanoid; Q26614; -.
DR OrthoDB; 220433at2759; -.
DR PhylomeDB; Q26614; -.
DR Proteomes; UP000007110; Unassembled WGS sequence.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017134; F:fibroblast growth factor binding; IBA:GO_Central.
DR GO; GO:0005007; F:fibroblast growth factor receptor activity; IBA:GO_Central.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
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; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
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 Alternative splicing; ATP-binding; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..43
FT /evidence="ECO:0000255"
FT CHAIN 44..972
FT /note="Fibroblast growth factor receptor"
FT /id="PRO_0000249214"
FT TOPO_DOM 44..547
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..972
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 57..152
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 150..242
FT /note="Ig-like C2-type 1"
FT DOMAIN 282..374
FT /note="Ig-like C2-type 2"
FT DOMAIN 383..517
FT /note="Ig-like C2-type 3"
FT DOMAIN 639..925
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 781
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 645..653
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 673
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 812
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 176..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 306..358
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 403..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 439..472
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8702734"
FT /id="VSP_020370"
SQ SEQUENCE 972 AA; 110482 MW; E8F2FD841F4CF5E1 CRC64;
MSLPRCPRTR TVMFSRTLTR CYPQRTLWIA ILCVICSWTL STAGATTIRD KEVKPDAPQD
LTAIPVKAEA IVLTWKKPLK GQTDGYIVVY CLKRNKGNGC ERQKIEGGNV TEVEVTNLYA
NHTYQFQVQS WYSDHPKGAS TGYIEASGTP PIPPTLRRNF KGLVEKSLGF EHKIPCPVKA
DPRPYTRWLK NGTDLTPNDP DDNVSFTKTS IVFKRLRFSD AGLYTCVASN FFGQPIHVNF
TLIVVDTHSE SYAESSVLES FSSLELETGP YNETEEEETH FPRFTDTERM EPEKPLPSNT
KVRLECGARG TPTPNITWIK DGVQKWKINV IRPTRVEEKG FVLIIRRAIV RDTGKYTCIV
SNQYGTIEHT YDVKIRERLP VKPIMSPMKN VTATVGSNTS FVCRVVNDLT PHFAWMRFNG
TNNTKQRLTD IDDHISILQQ RWVEEPMLTC DEFLDVFYQN QSKRMLECLH LIQLETQGGM
EEANQLKLYN VQYEDEGPYL CVAGNFYGMS WEGAYLDVVE PTTQAPVRTN PPAVYIPNNM
QPTSKTQLII FSVVGFVVVL ILVTCIAILC KQTQVRHRRP SDKPDISGPK HLYRQTSVDS
TQSIAPLFGG RNRLTSSLTV ISEYDIPLDP EWEFPRDRLT VGKTIGEGAF GKVVIGEAVG
IVCQEKTSTV AVKMLKANAM DREFSDLISE LAMMKMIGKN PNIINLLGCC TQEGPPYVIV
EFAHHGNLRD FLRSRRPPEE YEKSILLTTS QTLTNKDLMS MAYQVARGMD FLASKKCIHR
DLAARNVLVT EDFEMKICDF GLARDIHYID FYRKTTDGRL PVKWMAPEAL FDRMFTTQSD
VWSFGILLWE IMTLGGTPYP SVPVEQMFDY LRSGKRLEKP QNTSLEIYHI LCECWRTSPG
QRPTFCELVE DLDRIISVSS NQDYLDLEAV GDAPVKTFQE SERMAFMGFR APLSPQVYYK
VPQTRDCCPY AN
