ID   FGFR3_CHICK             Reviewed;         806 AA.
AC   P18460;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   02-SEP-2026, entry version 171.
DE   RecName: Full=Fibroblast growth factor receptor 3;
DE            Short=FGFR-3;
DE            EC=2.7.10.1;
DE   AltName: Full=Tyrosine kinase receptor CEK2;
DE   Flags: Precursor;
GN   Name=FGFR3; Synonyms=CEK2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2165604; DOI=10.1073/pnas.87.15.5812;
RA   Pasquale E.B.;
RT   "A distinctive family of embryonic protein-tyrosine kinase receptors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:5812-5816(1990).
CC   -!- FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor
CC       for fibroblast growth factors and plays an essential role in the
CC       regulation of cell proliferation, differentiation and apoptosis. Plays
CC       an essential role in the regulation of chondrocyte differentiation,
CC       proliferation and apoptosis, and is required for normal skeleton
CC       development. Regulates both osteogenesis and postnatal bone
CC       mineralization by osteoblasts. Promotes apoptosis in chondrocytes, but
CC       can also promote cancer cell proliferation. Phosphorylates PLCG1, CBL
CC       and FRS2. Ligand binding leads to the activation of several signaling
CC       cascades. Activation of PLCG1 leads to the production of the cellular
CC       signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate.
CC       Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and
CC       SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the
CC       MAP kinase signaling pathway, as well as of the AKT1 signaling pathway
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence
CC       of bound ligand. Ligand binding leads to dimerization and activation by
CC       autophosphorylation on tyrosine residues (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Homodimer after ligand binding (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The second and third Ig-like domains directly interact with
CC       fibroblast growth factors (FGF) and heparan sulfate proteoglycans.
CC       {ECO:0000250}.
CC   -!- PTM: Autophosphorylated. Binding of FGF family members together with
CC       heparan sulfate proteoglycan or heparin promotes receptor dimerization
CC       and autophosphorylation on tyrosine residues. Autophosphorylation
CC       occurs in trans between the two FGFR molecules present in the dimer (By
CC       similarity). {ECO:0000250}.
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; M35195; AAA48664.1; -; mRNA.
DR   PIR; A35963; A35963.
DR   RefSeq; NP_990840.2; NM_205509.3.
DR   AlphaFoldDB; P18460; -.
DR   SMR; P18460; -.
DR   FunCoup; P18460; 471.
DR   STRING; 9031.ENSGALP00000001710; -.
DR   GlyCosmos; P18460; 8 sites, No reported glycans.
DR   GlyGen; P18460; 8 sites.
DR   PaxDb; 9031-ENSGALP00000001710; -.
DR   GeneID; 396515; -.
DR   KEGG; gga:396515; -.
DR   CTD; 2261; -.
DR   VEuPathDB; HostDB:geneid_396515; -.
DR   eggNOG; KOG0200; Eukaryota.
DR   InParanoid; P18460; -.
DR   OrthoDB; 5984265at2759; -.
DR   PhylomeDB; P18460; -.
DR   BRENDA; 2.7.10.1; 1306.
DR   PRO; PR:P18460; -.
DR   Proteomes; UP000000539; Chromosome 4.
DR   Bgee; ENSGALG00000015708; Expressed in ovary and 10 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0043235; C:signaling receptor complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0048513; P:animal organ development; IEA:UniProtKB-ARBA.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-ARBA.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IBA:GO_Central.
DR   CDD; cd05857; IgI_2_FGFR; 1.
DR   CDD; cd05858; IgI_3_FGFR2; 1.
DR   CDD; cd05100; PTKc_FGFR3; 1.
DR   FunFam; 1.10.510.10:FF:000007; Fibroblast growth factor receptor; 1.
DR   FunFam; 2.60.40.10:FF:000016; Fibroblast growth factor receptor; 1.
DR   FunFam; 2.60.40.10:FF:000020; Fibroblast growth factor receptor; 1.
DR   FunFam; 2.60.40.10:FF:000423; Fibroblast growth factor receptor; 1.
DR   FunFam; 3.30.200.20:FF:000011; Fibroblast growth factor receptor; 1.
DR   Gene3D; 6.10.250.1740; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR013151; Immunoglobulin_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR050122; RTK.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24416:SF505; FIBROBLAST GROWTH FACTOR RECEPTOR 3; 1.
DR   PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR   Pfam; PF21165; FGFR3_TM; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF13927; Ig_3; 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; 3.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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   Apoptosis; ATP-binding; Cell membrane; 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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..806
FT                   /note="Fibroblast growth factor receptor 3"
FT                   /id="PRO_0000016790"
FT   TOPO_DOM        20..364
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        390..806
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          24..124
FT                   /note="Ig-like C2-type 1"
FT   DOMAIN          150..238
FT                   /note="Ig-like C2-type 2"
FT   DOMAIN          247..349
FT                   /note="Ig-like C2-type 3"
FT   DOMAIN          466..755
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          121..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..141
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        611
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         472..480
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         502
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         641
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         642
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         718
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         754
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
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        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        309
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        322
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        61..107
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        170..222
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        269..333
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   806 AA;  89730 MW;  B38B3C6D5F2314B6 CRC64;
     MRAAWGSVWC LCLAAAVGAL PAARRRGAER SGGQAAEYLR SETAFLEELV FGSGDTIELS
     CNTQSSSVSV FWFKDGIGIA PSNRTHIGQK LLKIINVSYD DSGLYSCKPR HSNEVLGNFT
     VRVTDSPSSG DDEDDDDESE DTGVPFWTRP DKMEKKLLAV PAANTVRFRC PAGGNPTPTI
     YWLKNGKEFK GEHRIGGIKL RHQQWSLVME SVVPSDRGNY TCVVENKYGN IRHTYQLDVL
     ERSPHRPILQ AGLPANQTVV VGSNVEFHCK VYSDAQPHIQ WLKHVEVNGS KYGPDGTPYV
     TVLKTAGVNT TDKELEILYL RNVTFEDAGE YTCLAGNSIG FSHHSAWLTV LPAEELMEMD
     DSGSVYAGIL SYGTGLVLFI LVLVIVIICR MKMPNKKAMN TTTVQKVSKF PLKRQQVSLE
     SNSSMNSNTP LVRITRLSSS DGPMLANVSE LELPPDPKWE LARSRLTLGK PLGEGCFGQV
     VMAEAIGIDK DKPNKAITVA VKMLKDDATD KDLSDLVSEM EMMKMIGKHK NIINLLGACT
     QDGPLYVLVE YASKGNLREY LRARRPPGMD YSFDTCKLPE EQLTFKDLVS CAYQVARGME
     YLASQKCIHR DLAARNVLVT EDNVMKIADF GLARDVHNID YYKKTTNGRL PVKWMAPEAL
     FDRVYTHQSD VWSFGVLLWE IFTLGGSPYP GIPVEELFKL LKEGHRMDKP ANCTHDLYMI
     MRECWHAVPS QRPTFKQLVE DLDRVLTMTS TDEYLDLSVP FEQYSPAGQD THSTCSSGDD
     SVFAHDLLPD EPCLPKHVPC NGVIRT
//