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Q9I8X3 (FGFR3_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibroblast growth factor receptor 3

Short name=FGFR-3
EC=2.7.10.1
Gene names
Name:fgfr3
OrganismDanio rerio (Zebrafish) (Brachydanio rerio) [Reference proteome]
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length800 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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

Enzyme regulation

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.

Subunit structure

Monomer. Homodimer after ligand binding By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Developmental stage

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. Ref.1

Domain

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

Post-translational modification

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.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 800780Fibroblast growth factor receptor 3
PRO_0000249205

Regions

Topological domain21 – 363343Extracellular Potential
Transmembrane364 – 38421Helical; Potential
Topological domain385 – 800416Cytoplasmic Potential
Domain21 – 122102Ig-like C2-type 1
Domain144 – 23794Ig-like C2-type 2
Domain246 – 348103Ig-like C2-type 3
Domain460 – 739280Protein kinase
Nucleotide binding466 – 4749ATP By similarity

Sites

Active site6051Proton acceptor By similarity
Binding site4961ATP By similarity

Amino acid modifications

Modified residue6351Phosphotyrosine; by autocatalysis By similarity
Modified residue6361Phosphotyrosine; by autocatalysis By similarity
Modified residue7121Phosphotyrosine; by autocatalysis By similarity
Modified residue7481Phosphotyrosine; by autocatalysis By similarity
Glycosylation771N-linked (GlcNAc...) Potential
Glycosylation901N-linked (GlcNAc...) Potential
Glycosylation1121N-linked (GlcNAc...) Potential
Glycosylation2181N-linked (GlcNAc...) Potential
Glycosylation2551N-linked (GlcNAc...) Potential
Glycosylation2871N-linked (GlcNAc...) Potential
Glycosylation3081N-linked (GlcNAc...) Potential
Glycosylation3211N-linked (GlcNAc...) Potential
Disulfide bond55 ↔ 101 By similarity
Disulfide bond169 ↔ 221 By similarity
Disulfide bond268 ↔ 332 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9I8X3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 8092DC0272A5BAD1

FASTA80089,716
        10         20         30         40         50         60 
MVPLCLLLYL ATLVFPPVYS AHLLSPEPTD WVSSEVEVFL EDYVAGVGDT VVLSCTPQDF 

        70         80         90        100        110        120 
LLPIVWQKDG DAVSSSNRTR VGQKALRIIN VSYEDSGVYS CRHAHKSMLL SNYTVKVIDS 

       130        140        150        160        170        180 
LSSGDDEDYD EDEDEAGNGN AEAPYWTRSD RMEKKLLAVP AANTVKFRCP AAGNPTPSIH 

       190        200        210        220        230        240 
WLKNGKEFKG EQRMGGIKLR HQQWSLVMES AVPSDRGNYT CVVQNKYGSI KHTYQLDVLE 

       250        260        270        280        290        300 
RSPHRPILQA GLPANQTVVV GSDVEFHCKV YSDAQPHIQW LKHIEVNGSQ YGPNGAPYVN 

       310        320        330        340        350        360 
VLKTAGINTT DKELEILYLT NVSFEDAGQY TCLAGNSIGY NHHSAWLTVL PAVEMEREDD 

       370        380        390        400        410        420 
YADILIYVTS CVLFILTMVI IILCRMWINT QKTLPAPPVQ KLSKFPLKRQ VSLESNSSMN 

       430        440        450        460        470        480 
SNTPLVRIAR LSSSDGPMLP NVSELELPSD PKWEFTRTKL TLGKPLGEGC FGQVVMAEAI 

       490        500        510        520        530        540 
GIDKEKPNKP LTVAVKMLKD DGTDKDLSDL VSEMEMMKMI GKHKNIINLL GACTQDGPLY 

       550        560        570        580        590        600 
VLVEYASKGN LREYLRARRP PGMDYSFDTC KIPNETLTFK DLVSCAYQVA RGMEYLASKK 

       610        620        630        640        650        660 
CIHRDPAARN VLVTEDNVMK IADFGLARDV HNIDYYKKTT NGRLPVKWMA PEALFDRVYT 

       670        680        690        700        710        720 
HQSDVWSYGV LLWEIFTLGG SPYPGIPVEE LFKLLKEGHR MDKPANCTHE LYMIMRECWH 

       730        740        750        760        770        780 
AVPSQRPTFR QLVEDHDRVL SMTSTDEYLD LSVPFEQYSP TCPDSNSTCS SGDDSVFAHD 

       790        800 
PLPEEPCLPK HHHSNGVIRT 

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References

[1]"fgfr3 and regionalization of anterior neural tube in zebrafish."
Sleptsova-Friedrich I., Li Y., Emelyanov A., Ekker M., Korzh V., Ge R.
Mech. Dev. 102:213-217(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF157560 mRNA. Translation: AAF80344.1.
RefSeqNP_571681.1. NM_131606.1.
UniGeneDr.10434.

3D structure databases

ProteinModelPortalQ9I8X3.
SMRQ9I8X3. Positions 143-354, 446-744.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9I8X3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID58129.
KEGGdre:58129.

Organism-specific databases

CTD2261.
ZFINZDB-GENE-000816-1. fgfr3.

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG000345.
InParanoidQ9I8X3.
KOK05094.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR028176. FGF_rcpt_3.
IPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERPTHR24416:SF128. PTHR24416:SF128. 1 hit.
PfamPF07679. I-set. 3 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF000628. FGFR. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20892380.

Entry information

Entry nameFGFR3_DANRE
AccessionPrimary (citable) accession number: Q9I8X3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families