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Protein

Fibroblast growth factor 23

Gene

Fgf23

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulator of phosphate homeostasis (By similarity). Inhibits renal tubular phosphate transport by reducing SLC34A1 levels (By similarity). Acts directly on the parathyroid to decrease PTH secretion (By similarity). Regulator of vitamin-D metabolism (By similarity). Negatively regulates osteoblasts differentiation and matrix mineralization (By similarity). Upregulates EGR1 expression in the presence of KL.By similarity1 Publication

GO - Molecular functioni

  • type 1 fibroblast growth factor receptor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Keywords - Biological processi

Differentiation

Enzyme and pathway databases

ReactomeiR-MMU-109704. PI3K Cascade.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-190322. FGFR4 ligand binding and activation.
R-MMU-190372. FGFR3c ligand binding and activation.
R-MMU-190373. FGFR1c ligand binding and activation.
R-MMU-190374. FGFR1c and Klotho ligand binding and activation.
R-MMU-190375. FGFR2c ligand binding and activation.
R-MMU-5654219. Phospholipase C-mediated cascade: FGFR1.
R-MMU-5654221. Phospholipase C-mediated cascade, FGFR2.
R-MMU-5654227. Phospholipase C-mediated cascade, FGFR3.
R-MMU-5654228. Phospholipase C-mediated cascade, FGFR4.
R-MMU-5654687. Downstream signaling of activated FGFR1.
R-MMU-5654688. SHC-mediated cascade:FGFR1.
R-MMU-5654689. PI-3K cascade:FGFR1.
R-MMU-5654693. FRS-mediated FGFR1 signaling.
R-MMU-5654695. PI-3K cascade:FGFR2.
R-MMU-5654699. SHC-mediated cascade:FGFR2.
R-MMU-5654700. FRS-mediated FGFR2 signaling.
R-MMU-5654704. SHC-mediated cascade:FGFR3.
R-MMU-5654706. FRS-mediated FGFR3 signaling.
R-MMU-5654710. PI-3K cascade:FGFR3.
R-MMU-5654712. FRS-mediated FGFR4 signaling.
R-MMU-5654719. SHC-mediated cascade:FGFR4.
R-MMU-5654720. PI-3K cascade:FGFR4.
R-MMU-5654726. Negative regulation of FGFR1 signaling.
R-MMU-5654727. Negative regulation of FGFR2 signaling.
R-MMU-5654732. Negative regulation of FGFR3 signaling.
R-MMU-5654733. Negative regulation of FGFR4 signaling.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor 23
Short name:
FGF-23
Gene namesi
Name:Fgf23
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1891427. Fgf23.

Subcellular locationi

  • Secreted By similarity

  • Note: Secretion is dependent on O-glycosylation.By similarity

GO - Cellular componenti

  • cell Source: GOC
  • extracellular space Source: MGI
  • intracellular Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Chaini25 – 251227Fibroblast growth factor 23PRO_0000008999Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi95 ↔ 113By similarity
Glycosylationi178 – 1781O-linked (GalNAc)By similarity

Post-translational modificationi

Following secretion this protein is inactivated by cleavage into a N-terminal fragment and a C-terminal fragment. The processing is effected by proprotein convertases (By similarity).By similarity
O-glycosylated by GALT3. Glycosylation is necessary for secretion; it blocks processing by proprotein convertases when the O-glycan is alpha 2,6-sialylated. Competition between proprotein convertase cleavage and block of cleavage by O-glycosylation determines the level of secreted active FGF23 (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9EPC2.
PaxDbiQ9EPC2.
PRIDEiQ9EPC2.

PTM databases

iPTMnetiQ9EPC2.
PhosphoSiteiQ9EPC2.

Expressioni

Tissue specificityi

Mainly expressed in the brain and thymus at low levels. In brain; preferentially expressed in the ventrolateral thalamic nucleus.

Gene expression databases

BgeeiQ9EPC2.
CleanExiMM_FGF23.
ExpressionAtlasiQ9EPC2. baseline and differential.
GenevisibleiQ9EPC2. MM.

Interactioni

Subunit structurei

Interacts with FGFR1, FGFR2, FGFR3 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by KL and heparan sulfate glycosaminoglycans that function as coreceptors (By similarity).By similarity

GO - Molecular functioni

  • type 1 fibroblast growth factor receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi211090. 3 interactions.
STRINGi10090.ENSMUSP00000000186.

Structurei

3D structure databases

ProteinModelPortaliQ9EPC2.
SMRiQ9EPC2. Positions 29-169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3885. Eukaryota.
ENOG4111IPH. LUCA.
GeneTreeiENSGT00530000063469.
HOGENOMiHOG000112573.
HOVERGENiHBG051613.
InParanoidiQ9EPC2.
KOiK04358.
OMAiNIFGSHH.
OrthoDBiEOG71K63W.
PhylomeDBiQ9EPC2.
TreeFamiTF335872.

Family and domain databases

InterProiIPR008996. Cytokine_IL1-like.
IPR028304. FGF23.
IPR002209. Fibroblast_GF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF69. PTHR11486:SF69. 1 hit.
PfamiPF00167. FGF. 1 hit.
[Graphical view]
SMARTiSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS00247. HBGF_FGF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9EPC2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGTCLRLLV GVLCTVCSLG TARAYPDTSP LLGSNWGSLT HLYTATARTS
60 70 80 90 100
YHLQIHRDGH VDGTPHQTIY SALMITSEDA GSVVITGAMT RRFLCMDLHG
110 120 130 140 150
NIFGSLHFSP ENCKFRQWTL ENGYDVYLSQ KHHYLVSLGR AKRIFQPGTN
160 170 180 190 200
PPPFSQFLAR RNEVPLLHFY TVRPRRHTRS AEDPPERDPL NVLKPRPRAT
210 220 230 240 250
PVPVSCSREL PSAEEGGPAA SDPLGVLRRG RGDARGGAGG ADRCRPFPRF

V
Length:251
Mass (Da):27,758
Last modified:March 1, 2001 - v1
Checksum:i110C1F2C735DC360
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037889 mRNA. Translation: BAB13478.1.
AF263536 mRNA. Translation: AAG09916.1.
CCDSiCCDS20562.1.
PIRiJC7513.
RefSeqiNP_073148.1. NM_022657.4.
UniGeneiMm.347933.

Genome annotation databases

EnsembliENSMUST00000000186; ENSMUSP00000000186; ENSMUSG00000000182.
GeneIDi64654.
KEGGimmu:64654.
UCSCiuc009dvp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037889 mRNA. Translation: BAB13478.1.
AF263536 mRNA. Translation: AAG09916.1.
CCDSiCCDS20562.1.
PIRiJC7513.
RefSeqiNP_073148.1. NM_022657.4.
UniGeneiMm.347933.

3D structure databases

ProteinModelPortaliQ9EPC2.
SMRiQ9EPC2. Positions 29-169.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211090. 3 interactions.
STRINGi10090.ENSMUSP00000000186.

PTM databases

iPTMnetiQ9EPC2.
PhosphoSiteiQ9EPC2.

Proteomic databases

MaxQBiQ9EPC2.
PaxDbiQ9EPC2.
PRIDEiQ9EPC2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000186; ENSMUSP00000000186; ENSMUSG00000000182.
GeneIDi64654.
KEGGimmu:64654.
UCSCiuc009dvp.2. mouse.

Organism-specific databases

CTDi8074.
MGIiMGI:1891427. Fgf23.

Phylogenomic databases

eggNOGiKOG3885. Eukaryota.
ENOG4111IPH. LUCA.
GeneTreeiENSGT00530000063469.
HOGENOMiHOG000112573.
HOVERGENiHBG051613.
InParanoidiQ9EPC2.
KOiK04358.
OMAiNIFGSHH.
OrthoDBiEOG71K63W.
PhylomeDBiQ9EPC2.
TreeFamiTF335872.

Enzyme and pathway databases

ReactomeiR-MMU-109704. PI3K Cascade.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-190322. FGFR4 ligand binding and activation.
R-MMU-190372. FGFR3c ligand binding and activation.
R-MMU-190373. FGFR1c ligand binding and activation.
R-MMU-190374. FGFR1c and Klotho ligand binding and activation.
R-MMU-190375. FGFR2c ligand binding and activation.
R-MMU-5654219. Phospholipase C-mediated cascade: FGFR1.
R-MMU-5654221. Phospholipase C-mediated cascade, FGFR2.
R-MMU-5654227. Phospholipase C-mediated cascade, FGFR3.
R-MMU-5654228. Phospholipase C-mediated cascade, FGFR4.
R-MMU-5654687. Downstream signaling of activated FGFR1.
R-MMU-5654688. SHC-mediated cascade:FGFR1.
R-MMU-5654689. PI-3K cascade:FGFR1.
R-MMU-5654693. FRS-mediated FGFR1 signaling.
R-MMU-5654695. PI-3K cascade:FGFR2.
R-MMU-5654699. SHC-mediated cascade:FGFR2.
R-MMU-5654700. FRS-mediated FGFR2 signaling.
R-MMU-5654704. SHC-mediated cascade:FGFR3.
R-MMU-5654706. FRS-mediated FGFR3 signaling.
R-MMU-5654710. PI-3K cascade:FGFR3.
R-MMU-5654712. FRS-mediated FGFR4 signaling.
R-MMU-5654719. SHC-mediated cascade:FGFR4.
R-MMU-5654720. PI-3K cascade:FGFR4.
R-MMU-5654726. Negative regulation of FGFR1 signaling.
R-MMU-5654727. Negative regulation of FGFR2 signaling.
R-MMU-5654732. Negative regulation of FGFR3 signaling.
R-MMU-5654733. Negative regulation of FGFR4 signaling.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.

Miscellaneous databases

PROiQ9EPC2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EPC2.
CleanExiMM_FGF23.
ExpressionAtlasiQ9EPC2. baseline and differential.
GenevisibleiQ9EPC2. MM.

Family and domain databases

InterProiIPR008996. Cytokine_IL1-like.
IPR028304. FGF23.
IPR002209. Fibroblast_GF_fam.
[Graphical view]
PANTHERiPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF69. PTHR11486:SF69. 1 hit.
PfamiPF00167. FGF. 1 hit.
[Graphical view]
SMARTiSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMiSSF50353. SSF50353. 1 hit.
PROSITEiPS00247. HBGF_FGF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification of a novel fibroblast growth factor, FGF-23, preferentially expressed in the ventrolateral thalamic nucleus of the brain."
    Yamashita T., Yoshioka M., Itoh N.
    Biochem. Biophys. Res. Commun. 277:494-498(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Autosomal dominant hypophosphataemic rickets is associated with mutations in FGF23."
    White K.E., Evans W.E., O'Riordan J.L.H., Speer M.C., Econs M.J., Lorenz-Depiereux B., Grabowski M., Meitinger T., Strom T.M.
    Nat. Genet. 26:345-348(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
    Tissue: Embryo.
  3. "Klotho converts canonical FGF receptor into a specific receptor for FGF23."
    Urakawa I., Yamazaki Y., Shimada T., Iijima K., Hasegawa H., Okawa K., Fujita T., Fukumoto S., Yamashita T.
    Nature 444:770-774(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KL AND FGFR1.

Entry informationi

Entry nameiFGF23_MOUSE
AccessioniPrimary (citable) accession number: Q9EPC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 117 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.