FGFR3_CHICK
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 03-AUG-2022, entry version 155.
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 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=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 -!- 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}.
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DR EMBL; M35195; AAA48664.1; -; mRNA.
DR PIR; A35963; A35963.
DR RefSeq; NP_990840.2; NM_205509.2.
DR AlphaFoldDB; P18460; -.
DR SMR; P18460; -.
DR STRING; 9031.ENSGALP00000001710; -.
DR PaxDb; P18460; -.
DR Ensembl; ENSGALT00000001712; ENSGALP00000001710; ENSGALG00000015708.
DR GeneID; 396515; -.
DR KEGG; gga:396515; -.
DR CTD; 2261; -.
DR VEuPathDB; HostDB:geneid_396515; -.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000159880; -.
DR InParanoid; P18460; -.
DR OMA; PTIYWLK; -.
DR OrthoDB; 220433at2759; -.
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 tissues.
DR ExpressionAtlas; P18460; baseline and differential.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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:0043410; P:positive regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 3.
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.
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; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 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; SSF48726; 3.
DR SUPFAM; SSF56112; SSF56112; 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 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
