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Protein

Fibroblast growth factor receptor 3

Gene

fgfr3

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
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.

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)DescriptionActionsGraphical viewLength
Binding sitei496ATPPROSITE-ProRule annotation1
Active sitei605Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi466 – 474ATPPROSITE-ProRule annotation9

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
OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifieri7955 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
Proteomesi
  • UP000000437 Componenti: Unplaced

Organism-specific databases

ZFINiZDB-GENE-000816-1. fgfr3.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini21 – 363ExtracellularSequence analysisAdd BLAST343
Transmembranei364 – 384HelicalSequence analysisAdd BLAST21
Topological domaini385 – 800CytoplasmicSequence analysisAdd BLAST416

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000024920521 – 800Fibroblast growth factor receptor 3Add BLAST780

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi55 ↔ 101PROSITE-ProRule annotation
Glycosylationi77N-linked (GlcNAc...)Sequence analysis1
Glycosylationi90N-linked (GlcNAc...)Sequence analysis1
Glycosylationi112N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi169 ↔ 221PROSITE-ProRule annotation
Glycosylationi218N-linked (GlcNAc...)Sequence analysis1
Glycosylationi255N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi268 ↔ 332PROSITE-ProRule annotation
Glycosylationi287N-linked (GlcNAc...)Sequence analysis1
Glycosylationi308N-linked (GlcNAc...)Sequence analysis1
Glycosylationi321N-linked (GlcNAc...)Sequence analysis1
Modified residuei635Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei636Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei712Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei748Phosphotyrosine; by autocatalysisBy similarity1

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

PRIDEiQ9I8X3.

Expressioni

Developmental stagei

Expression occurs in the axial mesoderm, the diencephalon, the anterior hindbrain and the anterior spinal cord. In the hindbrain, a differential expression was detected at several levels of intensity, with the highest expression in the posterior rhombomere 1 that is morphologically distinct from the anterior part, which develops into the cerebellum.1 Publication

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ9I8X3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 122Ig-like C2-type 1Add BLAST102
Domaini144 – 237Ig-like C2-type 2Add BLAST94
Domaini246 – 348Ig-like C2-type 3Add BLAST103
Domaini460 – 739Protein kinasePROSITE-ProRule annotationAdd BLAST280

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.
InParanoidiQ9I8X3.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR016248. 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.
[Graphical view]
PfamiPF07679. I-set. 3 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000628. FGFR. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
[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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9I8X3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPLCLLLYL ATLVFPPVYS AHLLSPEPTD WVSSEVEVFL EDYVAGVGDT
60 70 80 90 100
VVLSCTPQDF LLPIVWQKDG DAVSSSNRTR VGQKALRIIN VSYEDSGVYS
110 120 130 140 150
CRHAHKSMLL SNYTVKVIDS LSSGDDEDYD EDEDEAGNGN AEAPYWTRSD
160 170 180 190 200
RMEKKLLAVP AANTVKFRCP AAGNPTPSIH WLKNGKEFKG EQRMGGIKLR
210 220 230 240 250
HQQWSLVMES AVPSDRGNYT CVVQNKYGSI KHTYQLDVLE RSPHRPILQA
260 270 280 290 300
GLPANQTVVV GSDVEFHCKV YSDAQPHIQW LKHIEVNGSQ YGPNGAPYVN
310 320 330 340 350
VLKTAGINTT DKELEILYLT NVSFEDAGQY TCLAGNSIGY NHHSAWLTVL
360 370 380 390 400
PAVEMEREDD YADILIYVTS CVLFILTMVI IILCRMWINT QKTLPAPPVQ
410 420 430 440 450
KLSKFPLKRQ VSLESNSSMN SNTPLVRIAR LSSSDGPMLP NVSELELPSD
460 470 480 490 500
PKWEFTRTKL TLGKPLGEGC FGQVVMAEAI GIDKEKPNKP LTVAVKMLKD
510 520 530 540 550
DGTDKDLSDL VSEMEMMKMI GKHKNIINLL GACTQDGPLY VLVEYASKGN
560 570 580 590 600
LREYLRARRP PGMDYSFDTC KIPNETLTFK DLVSCAYQVA RGMEYLASKK
610 620 630 640 650
CIHRDPAARN VLVTEDNVMK IADFGLARDV HNIDYYKKTT NGRLPVKWMA
660 670 680 690 700
PEALFDRVYT HQSDVWSYGV LLWEIFTLGG SPYPGIPVEE LFKLLKEGHR
710 720 730 740 750
MDKPANCTHE LYMIMRECWH AVPSQRPTFR QLVEDHDRVL SMTSTDEYLD
760 770 780 790 800
LSVPFEQYSP TCPDSNSTCS SGDDSVFAHD PLPEEPCLPK HHHSNGVIRT
Length:800
Mass (Da):89,716
Last modified:October 1, 2000 - v1
Checksum:i8092DC0272A5BAD1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF157560 mRNA. Translation: AAF80344.1.
UniGeneiDr.10434.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF157560 mRNA. Translation: AAF80344.1.
UniGeneiDr.10434.

3D structure databases

ProteinModelPortaliQ9I8X3.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ9I8X3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

ZFINiZDB-GENE-000816-1. fgfr3.

Phylogenomic databases

HOVERGENiHBG000345.
InParanoidiQ9I8X3.

Miscellaneous databases

PROiQ9I8X3.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR016248. 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.
[Graphical view]
PfamiPF07679. I-set. 3 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000628. FGFR. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
[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.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFGFR3_DANRE
AccessioniPrimary (citable) accession number: Q9I8X3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: October 1, 2000
Last modified: October 5, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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.