FGFR_CIOIN
ID FGFR_CIOIN Reviewed; 747 AA.
AC Q4H3K6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Fibroblast growth factor receptor;
DE Short=Ci-FGFR;
DE EC=2.7.10.1;
DE Flags: Precursor;
GN Name=FGFR;
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15269171; DOI=10.1242/dev.01270;
RA Imai K.S., Hino K., Yagi K., Satoh N., Satou Y.;
RT "Gene expression profiles of transcription factors and signaling molecules
RT in the ascidian embryo: towards a comprehensive understanding of gene
RT networks.";
RL Development 131:4047-4058(2004).
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 -!- 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; AB210416; BAE06421.1; -; mRNA.
DR RefSeq; NP_001037820.1; NM_001044355.1.
DR AlphaFoldDB; Q4H3K6; -.
DR SMR; Q4H3K6; -.
DR STRING; 7719.NP_001037820.1; -.
DR PRIDE; Q4H3K6; -.
DR GeneID; 445706; -.
DR KEGG; cin:445706; -.
DR CTD; 373310; -.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; Q4H3K6; -.
DR OrthoDB; 220433at2759; -.
DR Proteomes; UP000008144; 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:0008284; P:positive regulation of cell population proliferation; IEA:InterPro.
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 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; 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; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000628; FGFR; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..747
FT /note="Fibroblast growth factor receptor"
FT /id="PRO_0000249210"
FT TOPO_DOM 25..288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..747
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 74..167
FT /note="Ig-like C2-type 1"
FT DOMAIN 175..267
FT /note="Ig-like C2-type 2"
FT DOMAIN 377..660
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 47..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 525
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 383..391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 412
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 556
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 198..251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 747 AA; 84957 MW; 36117F21204897E6 CRC64;
MIQLQNTFIF IALTIFTSAS TTSLKNETKP LNTISTLAAQ TNISNPEEDL FDTNGAPKSD
TVNASTTTDR HKIPRWVNEQ KMQKRLHAEP AGNTVQFRCA VQGARPITVD WYKDGEPIKK
NGRLGGYKFR QRNQQISLES VIMSDRAKYM CVAHNKYGSI NHTYELDVVA RIPIPPVLSA
DGMKNQTVKV GSTVTFRCRI VYSDAHPHVE WLKYNVNVTV LKRAGINTTD AEMEKLTLKN
VSFADAGEYT CLAGNSIGVS HVSAWLTVLP VVDENDVWTE EIPQDTHYLI YIFGVVCFII
LLAFIVYMCN SRYQNKDPPR LIPIENPDNI PPMSKMEEPV MLFGNEQAWR RMCLPHADHI
EINIQPDLQW ELKREDILLH ERIDEGFFGQ VFRADLIRCA GGRKEKVDAA VKMLKSTRTE
KDMLDLLTEM DQMKRVGKHK NIVNLLGVCT QNGILWLVTE YAQKGNLRDY LRRNRPSELQ
YELSTPDSPA PPRDEPLTLR ALMSASHQVA RGMEYLSQKK CIHRDLAARN VLVANDFVMK
IADFGLARDI RSNDYYRKET RGHLPYKWMA LEAMTDNMFT HATDVWSFGI LLWEIFSLGG
SPYPGVKTHD LVRFLRNGDR LEQPQFASSE LYRLMRDCWE ESPRRRPQFR QLVEDLDRML
ASSSSLEYID LNSPCEADYL PSDVDSNEDT ESRDSANATG EDSDSVFEPI DGHGAHAYEV
DEAGPLLNPQ PDANIVCNGH ARMQSDV
