Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9I8X3

- FGFR3_DANRE

UniProt

Q9I8X3 - FGFR3_DANRE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Fibroblast growth factor receptor 3

Gene

fgfr3

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei496 – 4961ATPPROSITE-ProRule annotation
Active sitei605 – 6051Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi466 – 4749ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. fibroblast growth factor-activated receptor activity Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. positive regulation of cell proliferation Source: InterPro
  3. skeletal system development Source: InterPro
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
ProteomesiUP000000437: Unplaced

Organism-specific databases

ZFINiZDB-GENE-000816-1. fgfr3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 363343ExtracellularSequence AnalysisAdd
BLAST
Transmembranei364 – 38421HelicalSequence AnalysisAdd
BLAST
Topological domaini385 – 800416CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 800780Fibroblast growth factor receptor 3PRO_0000249205Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 101PROSITE-ProRule annotation
Glycosylationi77 – 771N-linked (GlcNAc...)Sequence Analysis
Glycosylationi90 – 901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi112 – 1121N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi169 ↔ 221PROSITE-ProRule annotation
Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi255 – 2551N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi268 ↔ 332PROSITE-ProRule annotation
Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence Analysis
Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis
Modified residuei635 – 6351Phosphotyrosine; by autocatalysisBy similarity
Modified residuei636 – 6361Phosphotyrosine; by autocatalysisBy similarity
Modified residuei712 – 7121Phosphotyrosine; by autocatalysisBy similarity
Modified residuei748 – 7481Phosphotyrosine; 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

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.
SMRiQ9I8X3. Positions 143-354, 446-744.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 122102Ig-like C2-type 1Add
BLAST
Domaini144 – 23794Ig-like C2-type 2Add
BLAST
Domaini246 – 348103Ig-like C2-type 3Add
BLAST
Domaini460 – 739280Protein kinasePROSITE-ProRule annotationAdd
BLAST

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

eggNOGiCOG0515.
HOVERGENiHBG000345.
InParanoidiQ9I8X3.
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.
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]
PANTHERiPTHR24416:SF128. PTHR24416:SF128. 1 hit.
PfamiPF07679. I-set. 3 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000628. FGFR. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. 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.
RefSeqiNP_571681.1. NM_131606.1.
UniGeneiDr.10434.

Genome annotation databases

GeneIDi58129.
KEGGidre:58129.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF157560 mRNA. Translation: AAF80344.1 .
RefSeqi NP_571681.1. NM_131606.1.
UniGenei Dr.10434.

3D structure databases

ProteinModelPortali Q9I8X3.
SMRi Q9I8X3. Positions 143-354, 446-744.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q9I8X3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 58129.
KEGGi dre:58129.

Organism-specific databases

CTDi 2261.
ZFINi ZDB-GENE-000816-1. fgfr3.

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG000345.
InParanoidi Q9I8X3.
KOi K05094.

Miscellaneous databases

NextBioi 20892380.

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
InterProi IPR028176. 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 ]
PANTHERi PTHR24416:SF128. PTHR24416:SF128. 1 hit.
Pfami PF07679. I-set. 3 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view ]
PIRSFi PIRSF000628. FGFR. 1 hit.
PRINTSi PR00109. TYRKINASE.
SMARTi SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

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 29, 2014
This is version 99 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

External Data

Dasty 3