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Q03364 (FGFR2_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. 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 2

Short name=FGFR-2
EC=2.7.10.1
Gene names
Name:fgfr2
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length813 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, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. 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. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1 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. Golgi apparatus By similarity. Cytoplasmic vesicle By similarity. Note: Detected on osteoblast plasma membrane lipid rafts. After ligand binding, the activated receptor is rapidly internalized and degraded By similarity.

Tissue specificity

Expressed in the anterior neural plate in early neurula stage embryos. Later in development, the protein is also expressed in the eye anlagen, midbrain-hindbrain boundary and otic vesicle.

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.

N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus By similarity.

Ubiquitinated. FGFR2 is rapidly ubiquitinated after autophosphorylation, leading to internalization and degradation. Subject to degradation both in lysosomes and by the proteasome 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 – 1414
Chain15 – 813799Fibroblast growth factor receptor 2
PRO_0000016793

Regions

Topological domain18 – 367350Extracellular Potential
Transmembrane368 – 38821Helical; Potential
Topological domain389 – 813425Cytoplasmic Potential
Domain21 – 11797Ig-like C2-type 1
Domain145 – 23793Ig-like C2-type 2
Domain246 – 348103Ig-like C2-type 3
Domain471 – 760290Protein kinase
Nucleotide binding477 – 4859ATP Potential
Nucleotide binding555 – 5573ATP By similarity
Region152 – 16918Heparin-binding By similarity

Sites

Active site6161Proton acceptor By similarity
Binding site5071ATP Potential
Binding site5611ATP By similarity

Amino acid modifications

Modified residue4561Phosphotyrosine; by autocatalysis By similarity
Modified residue5761Phosphotyrosine; by autocatalysis By similarity
Modified residue6461Phosphotyrosine; by autocatalysis By similarity
Modified residue6471Phosphotyrosine; by autocatalysis By similarity
Modified residue7591Phosphotyrosine; by autocatalysis By similarity
Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation2311N-linked (GlcNAc...) Potential
Glycosylation2551N-linked (GlcNAc...) Potential
Glycosylation2871N-linked (GlcNAc...) Potential
Glycosylation3081N-linked (GlcNAc...) Potential
Glycosylation3211N-linked (GlcNAc...) Potential
Disulfide bond58 ↔ 103 By similarity
Disulfide bond170 ↔ 221 By similarity
Disulfide bond268 ↔ 332 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q03364 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 815436569892A565

FASTA81391,340
        10         20         30         40         50         60 
MLLLALLAFL LVSRTIARPS YSMVDDTTPE PEEPPAKYQI SKADVFPVLP GEPLDLRCPL 

        70         80         90        100        110        120 
ADGPLVTWTK DGAKLEVNNR TLIVRTYLQI KESTTRDSGL YACSVLKNSH FFHVNVTEAS 

       130        140        150        160        170        180 
SSGDDEDDND GSEDFTNDNN NIRAPYWTNT EKMEKKLHAV SAANTVKLRC PAREPHPSNE 

       190        200        210        220        230        240 
WLKNGKEFKQ EHRIGGYKVR NQHWSLIMES VVPSDKGIYT CIVENEHGSI NHTYHLDVIE 

       250        260        270        280        290        300 
RSSHRPILQA GLPANTTAVV GGDAEFVCKV YSDAQPHIRW VRYIEKNGSR FGVDGLPYFK 

       310        320        330        340        350        360 
VLKAAGVNVT DEEIEVLYVR NVSFEDAGEY TCIAGNSIGI SQHSAWLTVH PAPVNPLEDN 

       370        380        390        400        410        420 
PVPYYMEIGI YSTGIFIIFC MVVVCVVCRM RQGAKKKKNF TGPPVHKLTK RIPLHRQVTV 

       430        440        450        460        470        480 
SADSSSSMNS TTPLVRITTR LLNSTDAMPL ANVSEYELPH DPMWEFSRDK LTLGKPLGEG 

       490        500        510        520        530        540 
CFGQVVMAEA LGIDKERPKE SVTVAVKMLK DNATEKDLAD LVSEMEMMKM IGKHKNIINL 

       550        560        570        580        590        600 
LGACTQGGTL YVIVEYAAKG NLRQYLRARR PLEMEYSFDV TRVPDEQMTF KDLVSCTYQI 

       610        620        630        640        650        660 
ARGMEYLASQ KCIHRDLAAR NVLVTENNVM KIADFGLARD VNNIDYYKKT SNGRLPVKWM 

       670        680        690        700        710        720 
APEALFDRVY THQSDVWSFG VLMWEIFTLG GSPYPGIPVE ELFKLLKEGH RMDKPANCTN 

       730        740        750        760        770        780 
ELYMMMRDCW HAIPSHRPTF KQLVEDLDRI LTLTTNEEYL DLSAPLEQYS PSFPDSSCSA 

       790        800        810 
SSSSGDDSVF SPDPMPHDPC LPKFQHVNGV VKT 

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References

[1]"Spatially restricted expression of fibroblast growth factor receptor-2 during Xenopus development."
Friesel R., Brown S.A.N.
Development 116:1051-1058(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65943 mRNA. Translation: CAA46758.1.
PIRA49123.
UniGeneXl.16135.

3D structure databases

ProteinModelPortalQ03364.
SMRQ03364. Positions 141-353, 458-755.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ03364.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

XenbaseXB-GENE-1018301. fgfr2.

Phylogenomic databases

HOVERGENHBG000345.

Enzyme and pathway databases

BRENDA2.7.10.1. 6726.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR028175. FGF_rcpt_2.
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.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERPTHR24416:SF130. PTHR24416:SF130. 1 hit.
PfamPF07679. I-set. 2 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.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFGFR2_XENLA
AccessionPrimary (citable) accession number: Q03364
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 111 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