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Protein

Fibroblast growth factor receptor 3

Gene

fgfr3

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts. Promotes apoptosis in chondrocytes, but can also promote cancer cell proliferation. Phosphorylates PLCG1, CBL and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway (By similarity).By similarity

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Enzyme regulationi

Present in an inactive conformation in the absence of bound ligand. Ligand binding leads to dimerization and activation by autophosphorylation on tyrosine residues (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei498 – 4981ATPPROSITE-ProRule annotation
Active sitei607 – 6071Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi468 – 4769ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor receptor 3 (EC:2.7.10.1)
Short name:
FGFR-3
Gene namesi
Name:fgfr3
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini? – 362ExtracellularSequence analysis
Transmembranei363 – 38321HelicalSequence analysisAdd
BLAST
Topological domaini384 – 802419CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 802Fibroblast growth factor receptor 3PRO_0000249206
Signal peptidei1 – ?Sequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 98PROSITE-ProRule annotation
Glycosylationi74 – 741N-linked (GlcNAc...)Sequence analysis
Glycosylationi87 – 871N-linked (GlcNAc...)Sequence analysis
Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence analysis
Disulfide bondi165 ↔ 217PROSITE-ProRule annotation
Glycosylationi214 – 2141N-linked (GlcNAc...)Sequence analysis
Glycosylationi251 – 2511N-linked (GlcNAc...)Sequence analysis
Disulfide bondi264 ↔ 326PROSITE-ProRule annotation
Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence analysis
Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence analysis
Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence analysis
Modified residuei637 – 6371Phosphotyrosine; by autocatalysisBy similarity
Modified residuei638 – 6381Phosphotyrosine; by autocatalysisBy similarity
Modified residuei714 – 7141Phosphotyrosine; by autocatalysisBy similarity
Modified residuei750 – 7501Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiO42127.

Interactioni

Subunit structurei

Monomer. Homodimer after ligand binding (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliO42127.
SMRiO42127. Positions 449-746.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 11589Ig-like C2-type 1Add
BLAST
Domaini140 – 23394Ig-like C2-type 2Add
BLAST
Domaini242 – 342101Ig-like C2-type 3Add
BLAST
Domaini462 – 751290Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi122 – 13615Asp-richAdd
BLAST
Compositional biasi359 – 3624Poly-Ser

Domaini

The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans.By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG000345.
KOiK05094.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR028176. FGF_rcpt_3.
IPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERiPTHR24416:SF128. PTHR24416:SF128. 1 hit.
PfamiPF07679. I-set. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000628. FGFR. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O42127-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSVNGVPAA RLPVTLPGED RASRKAPDYL MVEQPPFDEL MYTIGETIEL
60 70 80 90 100
SCAAEDASTT TKWCKDGIGI VPNNRTSTRQ GLLKIINVSS DDSGIYSCRL
110 120 130 140 150
WHSTEILRNF TIRVTDLPSS GDDEDDDDDD DDETEDREPP RWTQPERMEK
160 170 180 190 200
KLIAVPAANT IRFRCPAAGN PTPTIHWLKN GKEFRGEHRI GGIKLRHQQW
210 220 230 240 250
SLVMESVVPS DKGNYTCVVE NKYGSIRQTY QLDVLERSSH RPILQAGLPG
260 270 280 290 300
NQTVVLGSDV EFHCKVYSDA QPHIQWLKHV EVNGSKYGPD GDPYVSVLQS
310 320 330 340 350
FINGTEVDST LSLKNVTETN EGQYVCRANN FIGVAEASFW LHIYKPAPAE
360 370 380 390 400
PVEKALTTSS SSITVLIVVT STIVFILLVI IVITHLMKVP SKKSMTAPPV
410 420 430 440 450
HKVSKFPLKR QQVSLESNSS MNSNTPLVRI THLSSSDGTM LANVSELGLP
460 470 480 490 500
LDPKWELLRS RLTLGKPLGE GCFGQVVMAE AIGIDKERPN KPATVAVKML
510 520 530 540 550
KDDATDKDLS DLVSEMEMMK MIGKHKNIIN LLGACTQDGP LYVLVEYASK
560 570 580 590 600
GSLREYLKAR RPPGMDYSFD ACKIPAEQLT FKDLVSCAYQ VARGMEYLAS
610 620 630 640 650
QKCIHRDLAA RNVLVTDDNV MKIADFGLAR DIHNIDYYKK TTNGRLPVKW
660 670 680 690 700
MAPEALFDRI YTHHSDVWSY GVLLWEIFTL GGSPYPGIPV EELFKLLKEG
710 720 730 740 750
HRMDKPANCT HELYMIMREC WHAVPSQRPA FKQLVEDLDR VLTVTSTNEY
760 770 780 790 800
LDLSVAFEQY SPPSQDSHST CSSGDDSVFA HDILPDEPCL PKHQQHNGAI

PT
Length:802
Mass (Da):89,516
Last modified:January 1, 1998 - v1
Checksum:iCC5E5DDF3BD25BD3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007035 mRNA. Translation: BAA22281.1.
RefSeqiNP_001084170.1. NM_001090701.1.
UniGeneiXl.8760.

Genome annotation databases

GeneIDi399347.
KEGGixla:399347.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007035 mRNA. Translation: BAA22281.1.
RefSeqiNP_001084170.1. NM_001090701.1.
UniGeneiXl.8760.

3D structure databases

ProteinModelPortaliO42127.
SMRiO42127. Positions 449-746.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO42127.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi399347.
KEGGixla:399347.

Organism-specific databases

CTDi2261.

Phylogenomic databases

HOVERGENiHBG000345.
KOiK05094.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR028176. FGF_rcpt_3.
IPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERiPTHR24416:SF128. PTHR24416:SF128. 1 hit.
PfamiPF07679. I-set. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000628. FGFR. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "FGF signaling and the anterior neural induction in Xenopus."
    Hongo I., Kengaku M., Okamoto H.
    Dev. Biol. 216:561-581(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiFGFR3_XENLA
AccessioniPrimary (citable) accession number: O42127
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.