ID   FGF23_MOUSE             Reviewed;         251 AA.
AC   Q9EPC2;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   19-JAN-2010, entry version 67.
DE   RecName: Full=Fibroblast growth factor 23;
DE            Short=FGF-23;
DE   Flags: Precursor;
GN   Name=Fgf23;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20490027; PubMed=11032749; DOI=10.1006/bbrc.2000.3696;
RA   Yamashita T., Yoshioka M., Itoh N.;
RT   "Identification of a novel fibroblast growth factor, FGF-23,
RT   preferentially expressed in the ventrolateral thalamic nucleus of the
RT   brain.";
RL   Biochem. Biophys. Res. Commun. 277:494-498(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Embryo;
RX   MEDLINE=20517346; PubMed=11062477; DOI=10.1038/81664;
RA   White K.E., Evans W.E., O'Riordan J.L.H., Speer M.C., Econs M.J.,
RA   Lorenz-Depiereux B., Grabowski M., Meitinger T., Strom T.M.;
RT   "Autosomal dominant hypophosphataemic rickets is associated with
RT   mutations in FGF23.";
RL   Nat. Genet. 26:345-348(2000).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH KL AND FGFR1.
RX   PubMed=17086194; DOI=10.1038/nature05315;
RA   Urakawa I., Yamazaki Y., Shimada T., Iijima K., Hasegawa H., Okawa K.,
RA   Fujita T., Fukumoto S., Yamashita T.;
RT   "Klotho converts canonical FGF receptor into a specific receptor for
RT   FGF23.";
RL   Nature 444:770-774(2006).
CC   -!- FUNCTION: Regulator of phosphate homeostasis (By similarity).
CC       Inhibits renal tubular phosphate transport by reducing SLC34A1
CC       levels (By similarity). Acts directly on the parathyroid to
CC       decrease PTH secretion (By similarity). Regulator of vitamin-D
CC       metabolism (By similarity). Negatively regulates osteoblasts
CC       differentiation and matrix mineralization (By similarity).
CC       Upregulates EGR1 expression in the presence of KL.
CC   -!- SUBUNIT: Interacts with KL and FGFR1.
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity). Note=Secretion is
CC       dependent on O-glycosylation (By similarity).
CC   -!- TISSUE SPECIFICITY: Mainly expressed in the brain and thymus at
CC       low levels. In brain; preferentially expressed in the
CC       ventrolateral thalamic nucleus.
CC   -!- PTM: Following secretion this protein is inactivated by cleavage
CC       into a N-terminal fragment and a C-terminal fragment. The
CC       processing is effected by proprotein convertases (By similarity).
CC   -!- PTM: O-glycosylated by GALT3. Glycosylation is necessary for
CC       secretion; it blocks processing by proprotein convertases when the
CC       O-glycan is alpha 2,6-sialylated. Competition between proprotein
CC       convertase cleavage and block of cleavage by O-glycosylation
CC       determines the level of secreted active FGF23 (By similarity).
CC   -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
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DR   EMBL; AB037889; BAB13478.1; -; mRNA.
DR   EMBL; AF263536; AAG09916.1; -; mRNA.
DR   IPI; IPI00109761; -.
DR   PIR; JC7513; JC7513.
DR   RefSeq; NP_073148.1; -.
DR   RefSeq; XP_001480965.1; -.
DR   UniGene; Mm.347933; -.
DR   SMR; Q9EPC2; 29-169.
DR   STRING; Q9EPC2; -.
DR   PRIDE; Q9EPC2; -.
DR   Ensembl; ENSMUST00000000186; ENSMUSP00000000186; ENSMUSG00000000182; Mus musculus.
DR   GeneID; 100048681; -.
DR   GeneID; 64654; -.
DR   KEGG; mmu:100048681; -.
DR   KEGG; mmu:64654; -.
DR   UCSC; uc009dvp.1; mouse.
DR   CTD; 64654; -.
DR   MGI; MGI:1891427; Fgf23.
DR   HOGENOM; HBG269053; -.
DR   HOVERGEN; Q9EPC2; -.
DR   InParanoid; Q9EPC2; -.
DR   OMA; ASCSQEL; -.
DR   OrthoDB; EOG9HHRMK; -.
DR   NextBio; 462088; -.
DR   ArrayExpress; Q9EPC2; -.
DR   Bgee; Q9EPC2; -.
DR   CleanEx; MM_FGF23; -.
DR   Genevestigator; Q9EPC2; -.
DR   GermOnline; ENSMUSG00000000182; Mus musculus.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005105; F:type 1 fibroblast growth factor receptor bi...; IPI:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0030643; P:cellular phosphate ion homeostasis; IMP:MGI.
DR   GO; GO:0046888; P:negative regulation of hormone secretion; ISS:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR   GO; GO:0043193; P:positive regulation of gene-specific transc...; IDA:UniProtKB.
DR   GO; GO:0090080; P:positive regulation of MAPKKK cascade by fi...; IGI:MGI.
DR   GO; GO:0030500; P:regulation of bone mineralization; IMP:MGI.
DR   InterPro; IPR008996; Cytokine_IL1-like.
DR   InterPro; IPR002348; IL1_HBGF.
DR   PANTHER; PTHR11486; IL1_HBGF; 1.
DR   Pfam; PF00167; FGF; 1.
DR   SMART; SM00442; FGF; 1.
DR   PROSITE; PS00247; HBGF_FGF; 1.
PE   1: Evidence at protein level;
KW   Differentiation; Disulfide bond; Glycoprotein; Growth factor;
KW   Secreted; Signal.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    251       Fibroblast growth factor 23.
FT                                /FTId=PRO_0000008999.
FT   CARBOHYD    178    178       O-linked (GalNAc) (By similarity).
FT   DISULFID     95    113       By similarity.
SQ   SEQUENCE   251 AA;  27758 MW;  110C1F2C735DC360 CRC64;
     MLGTCLRLLV GVLCTVCSLG TARAYPDTSP LLGSNWGSLT HLYTATARTS YHLQIHRDGH
     VDGTPHQTIY SALMITSEDA GSVVITGAMT RRFLCMDLHG NIFGSLHFSP ENCKFRQWTL
     ENGYDVYLSQ KHHYLVSLGR AKRIFQPGTN PPPFSQFLAR RNEVPLLHFY TVRPRRHTRS
     AEDPPERDPL NVLKPRPRAT PVPVSCSREL PSAEEGGPAA SDPLGVLRRG RGDARGGAGG
     ADRCRPFPRF V
//