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Q8VI82 (FGF23_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. 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 23

Short name=FGF-23
Gene names
Name:Fgf23
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Regulator of phosphate homeostasis By similarity. Inhibits renal tubular phosphate transport by reducing SLC34A1 levels By similarity. Regulator of vitamin-D metabolism By similarity. Negatively regulates osteoblasts differentiation and matrix mineralization By similarity. Acts directly on the parathyroid to decrease PTH secretion. Upregulates EGR1 expression in the presence of KL. Ref.2 Ref.3

Subunit structure

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.

Subcellular location

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

Tissue specificity

Expressed in the parathyroid. Ref.3

Post-translational modification

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.

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.

Sequence similarities

Belongs to the heparin-binding growth factors family.

Ontologies

Keywords
   Biological processDifferentiation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGrowth factor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cellular phosphate ion homeostasis

Inferred from electronic annotation. Source: Ensembl

negative regulation of bone mineralization

Inferred from electronic annotation. Source: Ensembl

negative regulation of hormone secretion

Inferred from direct assay Ref.3. Source: UniProtKB

negative regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

phosphate-containing compound metabolic process

Inferred from expression pattern PubMed 15531762. Source: RGD

positive regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of vitamin D 24-hydroxylase activity

Inferred from electronic annotation. Source: Ensembl

regulation of phosphate transport

Inferred from electronic annotation. Source: Ensembl

vitamin D catabolic process

Inferred from electronic annotation. Source: Ensembl

vitamin D metabolic process

Inferred from expression pattern PubMed 15531762. Source: RGD

   Cellular_componentextracellular space

Inferred from direct assay PubMed 15531762. Source: RGD

   Molecular_functionfibroblast growth factor receptor binding

Traceable author statement PubMed 15531762. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 251227Fibroblast growth factor 23
PRO_0000009000

Amino acid modifications

Glycosylation1781O-linked (GalNAc) By similarity
Disulfide bond95 ↔ 113 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8VI82 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 35A229E1B3900593

FASTA25127,912
        10         20         30         40         50         60 
MLGACLRLLV GALCTVCSLG TARAYSDTSP LLGSNWGSLT HLYTATARNS YHLQIHRDGH 

        70         80         90        100        110        120 
VDGTPHQTIY SALMITSEDA GSVVIIGAMT RRFLCMDLRG NIFGSYHFSP ENCRFRQWTL 

       130        140        150        160        170        180 
ENGYDVYLSP KHHYLVSLGR SKRIFQPGTN PPPFSQFLAR RNEVPLLHFY TARPRRHTRS 

       190        200        210        220        230        240 
AEDPPERDPL NVLKPRPRAT PIPVSCSREL PSAEEGGPAA SDPLGVLRRG RGDARRGAGG 

       250 
TDRCRPFPRF V 

« Hide

References

[1]"Rattus norvegicus fgf23."
Itoh N.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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.
[3]"The parathyroid is a target organ for FGF23 in rats."
Ben-Dov I.Z., Galitzer H., Lavi-Moshayoff V., Goetz R., Kuro-o M., Mohammadi M., Sirkis R., Naveh-Many T., Silver J.
J. Clin. Invest. 117:4003-4008(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB078777 mRNA. Translation: BAB84108.1.
RefSeqNP_570110.1. NM_130754.1.
UniGeneRn.154421.

3D structure databases

ProteinModelPortalQ8VI82.
SMRQ8VI82. Positions 29-169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000026888.

Proteomic databases

PRIDEQ8VI82.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026888; ENSRNOP00000026888; ENSRNOG00000019855.
GeneID170583.
KEGGrno:170583.
UCSCRGD:620178. rat.

Organism-specific databases

CTD8074.
RGD620178. Fgf23.

Phylogenomic databases

eggNOGNOG270405.
GeneTreeENSGT00530000063469.
HOGENOMHOG000112573.
HOVERGENHBG051613.
InParanoidQ8VI82.
KOK04358.
OMADVYHSPQ.
OrthoDBEOG71K63W.
PhylomeDBQ8VI82.
TreeFamTF335872.

Gene expression databases

GenevestigatorQ8VI82.

Family and domain databases

InterProIPR008996. Cytokine_IL1-like.
IPR028304. FGF23.
IPR002209. Fibroblast_GF_fam.
[Graphical view]
PANTHERPTHR11486. PTHR11486. 1 hit.
PTHR11486:SF10. PTHR11486:SF10. 1 hit.
PfamPF00167. FGF. 1 hit.
[Graphical view]
SMARTSM00442. FGF. 1 hit.
[Graphical view]
SUPFAMSSF50353. SSF50353. 1 hit.
PROSITEPS00247. HBGF_FGF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio621084.
PROQ8VI82.

Entry information

Entry nameFGF23_RAT
AccessionPrimary (citable) accession number: Q8VI82
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 81 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