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Fibroblast growth factor 23 (FGF-23) (Phosphatonin) (Tumor-derived hypophosphatemia-inducing factor) [Cleaved into: Fibroblast growth factor 23 N-terminal peptide; Fibroblast growth factor 23 C-terminal peptide]

 FGF23_HUMAN             Reviewed;         251 AA.
Q9GZV9; Q4V758;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
05-DEC-2018, entry version 186.
RecName: Full=Fibroblast growth factor 23;
Short=FGF-23;
AltName: Full=Phosphatonin;
AltName: Full=Tumor-derived hypophosphatemia-inducing factor;
Contains:
RecName: Full=Fibroblast growth factor 23 N-terminal peptide;
Contains:
RecName: Full=Fibroblast growth factor 23 C-terminal peptide;
Flags: Precursor;
Name=FGF23; Synonyms=HYPF; ORFNames=UNQ3027/PRO9828;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11032749; DOI=10.1006/bbrc.2000.3696;
Yamashita T., Yoshioka M., Itoh N.;
"Identification of a novel fibroblast growth factor, FGF-23,
preferentially expressed in the ventrolateral thalamic nucleus of the
brain.";
Biochem. Biophys. Res. Commun. 277:494-498(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANTS ADHR GLN-176; GLN-179
AND TRP-179, AND VARIANT MET-239.
PubMed=11062477; DOI=10.1038/81664;
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.;
"Autosomal dominant hypophosphataemic rickets is associated with
mutations in FGF23.";
Nat. Genet. 26:345-348(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11344269; DOI=10.1073/pnas.101545198;
Shimada T., Mizutani S., Muto T., Yoneya T., Hino R., Takeda S.,
Takeuchi Y., Fujita T., Fukumoto S., Yamashita T.;
"Cloning and characterization of FGF23 as a causative factor of tumor-
induced osteomalacia.";
Proc. Natl. Acad. Sci. U.S.A. 98:6500-6505(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-195 AND MET-239.
NIEHS SNPs program;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 25-39.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[8]
FUNCTION, AND CHARACTERIZATION OF VARIANT ADHR GLN-179.
PubMed=11409890; DOI=10.1006/bbrc.2001.5084;
Bowe A.E., Finnegan R., Jan de Beur S.M., Cho J., Levine M.A.,
Kumar R., Schiavi S.C.;
"FGF-23 inhibits renal tubular phosphate transport and is a PHEX
substrate.";
Biochem. Biophys. Res. Commun. 284:977-981(2001).
[9]
PROTEOLYTIC PROCESSING.
PubMed=11157998; DOI=10.1210/jcem.86.2.7408;
White K.E., Jonsson K.B., Carn G., Hampson G., Spector T.D.,
Mannstadt M., Lorenz-Depiereux B., Miyauchi A., Yang I.M.,
Ljunggren O., Meitinger T., Strom T.M., Jueppner H., Econs M.J.;
"The autosomal dominant hypophosphatemic rickets (ADHR) gene is a
secreted polypeptide overexpressed by tumors that cause phosphate
wasting.";
J. Clin. Endocrinol. Metab. 86:497-500(2001).
[10]
PROTEOLYTIC PROCESSING.
PubMed=12130585; DOI=10.1210/endo.143.8.8795;
Shimada T., Muto T., Urakawa I., Yoneya T., Yamazaki Y., Okawa K.,
Takeuchi Y., Fujita T., Fukumoto S., Yamashita T.;
"Mutant FGF-23 responsible for autosomal dominant hypophosphatemic
rickets is resistant to proteolytic cleavage and causes
hypophosphatemia in vivo.";
Endocrinology 143:3179-3182(2002).
[11]
TISSUE SPECIFICITY.
PubMed=12952917; DOI=10.1172/JCI18399;
Riminucci M., Collins M.T., Fedarko N.S., Cherman N., Corsi A.,
White K.E., Waguespack S., Gupta A., Hannon T., Econs M.J., Bianco P.,
Gehron Robey P.;
"FGF-23 in fibrous dysplasia of bone and its relationship to renal
phosphate wasting.";
J. Clin. Invest. 112:683-692(2003).
[12]
PROTEOLYTIC PROCESSING BY PROPROTEIN CONVERTASES.
PubMed=15268897; DOI=10.1016/j.bone.2004.04.002;
Benet-Pages A., Lorenz-Depiereux B., Zischka H., White K.E.,
Econs M.J., Strom T.M.;
"FGF23 is processed by proprotein convertases but not by PHEX.";
Bone 35:455-462(2004).
[13]
FUNCTION.
PubMed=15040831; DOI=10.1359/JBMR.0301264;
Shimada T., Hasegawa H., Yamazaki Y., Muto T., Hino R., Takeuchi Y.,
Fujita T., Nakahara K., Fukumoto S., Yamashita T.;
"FGF-23 is a potent regulator of vitamin D metabolism and phosphate
homeostasis.";
J. Bone Miner. Res. 19:429-435(2004).
[14]
INTERACTION WITH FGFR1; FGFR2; FGFR3 AND FGFR4, AND FUNCTION IN
STIMULATION OF CELL PROLIFERATION.
PubMed=16597617; DOI=10.1074/jbc.M601252200;
Zhang X., Ibrahimi O.A., Olsen S.K., Umemori H., Mohammadi M.,
Ornitz D.M.;
"Receptor specificity of the fibroblast growth factor family. The
complete mammalian FGF family.";
J. Biol. Chem. 281:15694-15700(2006).
[15]
SUBCELLULAR LOCATION, GLYCOSYLATION AT THR-178, CHARACTERIZATION OF
VARIANTS ADHR GLN-176 AND GLN-179, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16638743; DOI=10.1074/jbc.M602469200;
Kato K., Jeanneau C., Tarp M.A., Benet-Pages A., Lorenz-Depiereux B.,
Bennett E.P., Mandel U., Strom T.M., Clausen H.;
"Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis.
Secretion of fibroblast growth factor 23 requires O-glycosylation.";
J. Biol. Chem. 281:18370-18377(2006).
[16]
FUNCTION.
PubMed=18282132; DOI=10.1359/jbmr.080220;
Wang H., Yoshiko Y., Yamamoto R., Minamizaki T., Kozai K., Tanne K.,
Aubin J.E., Maeda N.;
"Overexpression of fibroblast growth factor 23 suppresses osteoblast
differentiation and matrix mineralization in vitro.";
J. Bone Miner. Res. 23:939-948(2008).
[17]
REVIEW.
PubMed=20094046; DOI=10.1038/nrc2780;
Turner N., Grose R.;
"Fibroblast growth factor signalling: from development to cancer.";
Nat. Rev. Cancer 10:116-129(2010).
[18]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 25-179.
PubMed=17339340; DOI=10.1128/MCB.02249-06;
Goetz R., Beenken A., Ibrahimi O.A., Kalinina J., Olsen S.K.,
Eliseenkova A.V., Xu C., Neubert T.A., Zhang F., Linhardt R.J., Yu X.,
White K.E., Inagaki T., Kliewer S.A., Yamamoto M., Kurosu H.,
Ogawa Y., Kuro-o M., Lanske B., Razzaque M.S., Mohammadi M.;
"Molecular insights into the klotho-dependent, endocrine mode of
action of fibroblast growth factor 19 subfamily members.";
Mol. Cell. Biol. 27:3417-3428(2007).
[19]
VARIANT HFTC2 THR-96.
PubMed=16151858; DOI=10.1007/s00439-005-0026-8;
Chefetz I., Heller R., Galli-Tsinopoulou A., Richard G., Wollnik B.,
Indelman M., Koerber F., Topaz O., Bergman R., Sprecher E.,
Schoenau E.;
"A novel homozygous missense mutation in FGF23 causes Familial Tumoral
Calcinosis associated with disseminated visceral calcification.";
Hum. Genet. 118:261-266(2005).
[20]
VARIANT HFTC2 GLY-71.
PubMed=15590700; DOI=10.1093/hmg/ddi034;
Benet-Pages A., Orlik P., Strom T.M., Lorenz-Depiereux B.;
"An FGF23 missense mutation causes familial tumoral calcinosis with
hyperphosphatemia.";
Hum. Mol. Genet. 14:385-390(2005).
[21]
VARIANT HFTC2 PHE-129, AND CHARACTERIZATION OF VARIANT HFTC2 PHE-129.
PubMed=16030159; DOI=10.1210/jc.2005-0301;
Araya K., Fukumoto S., Backenroth R., Takeuchi Y., Nakayama K.,
Ito N., Yoshii N., Yamazaki Y., Yamashita T., Silver J., Igarashi T.,
Fujita T.;
"A novel mutation in fibroblast growth factor 23 gene as a cause of
tumoral calcinosis.";
J. Clin. Endocrinol. Metab. 90:5523-5527(2005).
[22]
VARIANT HFTC2 LEU-157.
PubMed=24680727; DOI=10.1016/j.gene.2014.03.052;
Abbasi F., Ghafouri-Fard S., Javaheri M., Dideban A., Ebrahimi A.,
Ebrahim-Habibi A.;
"A new missense mutation in FGF23 gene in a male with hyperostosis-
hyperphosphatemia syndrome (HHS).";
Gene 542:269-271(2014).
-!- FUNCTION: Regulator of phosphate homeostasis. Inhibits renal
tubular phosphate transport by reducing SLC34A1 levels.
Upregulates EGR1 expression in the presence of KL (By similarity).
Acts directly on the parathyroid to decrease PTH secretion (By
similarity). Regulator of vitamin-D metabolism. Negatively
regulates osteoblast differentiation and matrix mineralization.
{ECO:0000250, ECO:0000269|PubMed:11062477,
ECO:0000269|PubMed:11409890, ECO:0000269|PubMed:15040831,
ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:18282132}.
-!- SUBUNIT: 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). {ECO:0000250}.
-!- INTERACTION:
P11362:FGFR1; NbExp=2; IntAct=EBI-6594125, EBI-1028277;
O35082:Kl (xeno); NbExp=5; IntAct=EBI-6594125, EBI-1570828;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16638743}.
Note=Secretion is dependent on O-glycosylation.
-!- TISSUE SPECIFICITY: Expressed in osteogenic cells particularly
during phases of active bone remodeling. In adult trabecular bone,
expressed in osteocytes and flattened bone-lining cells (inactive
osteoblasts). {ECO:0000269|PubMed:12952917}.
-!- PTM: 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.
-!- PTM: 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.
{ECO:0000269|PubMed:16638743}.
-!- DISEASE: Hypophosphatemic rickets, autosomal dominant (ADHR)
[MIM:193100]: A disease characterized by isolated renal phosphate
wasting, hypophosphatemia, and inappropriately normal 1,25-
dihydroxyvitamin D3 (calcitriol) levels. Patients frequently
present with bone pain, rickets, and tooth abscesses.
{ECO:0000269|PubMed:11062477, ECO:0000269|PubMed:11409890,
ECO:0000269|PubMed:16638743}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Tumoral calcinosis, hyperphosphatemic, familial, 2
(HFTC2) [MIM:617993]: A form of hyperphosphatemic tumoral
calcinosis, a rare autosomal recessive metabolic disorder that
manifests with hyperphosphatemia and massive calcium deposits in
the skin and subcutaneous tissues. Some patients have recurrent,
transient, painful swellings of the long bones associated with the
radiographic findings of periosteal reaction and cortical
hyperostosis and absence of skin involvement.
{ECO:0000269|PubMed:15590700, ECO:0000269|PubMed:16030159,
ECO:0000269|PubMed:16151858, ECO:0000269|PubMed:24680727}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the heparin-binding growth factors family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/fgf23/";
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EMBL; AB037973; BAB13477.1; -; mRNA.
EMBL; AF263537; AAG09917.1; -; mRNA.
EMBL; AB047858; BAB55889.1; -; mRNA.
EMBL; AY358323; AAQ88689.1; -; mRNA.
EMBL; AY566236; AAS59157.1; -; Genomic_DNA.
EMBL; BC069333; AAH69333.1; -; mRNA.
EMBL; BC096713; AAH96713.1; -; mRNA.
EMBL; BC098147; AAH98147.1; -; mRNA.
EMBL; BC098252; AAH98252.1; -; mRNA.
CCDS; CCDS8526.1; -.
RefSeq; NP_065689.1; NM_020638.2.
UniGene; Hs.287370; -.
PDB; 2P39; X-ray; 1.50 A; A=25-179.
PDB; 5W21; X-ray; 3.00 A; B=25-204.
PDBsum; 2P39; -.
PDBsum; 5W21; -.
ProteinModelPortal; Q9GZV9; -.
SMR; Q9GZV9; -.
BioGrid; 113748; 2.
CORUM; Q9GZV9; -.
DIP; DIP-58507N; -.
IntAct; Q9GZV9; 6.
STRING; 9606.ENSP00000237837; -.
ChEMBL; CHEMBL3713913; -.
TCDB; 1.A.108.1.2; the fibroblast growth factor 2 (fgf2) family.
iPTMnet; Q9GZV9; -.
PhosphoSitePlus; Q9GZV9; -.
BioMuta; FGF23; -.
DMDM; 13626688; -.
PaxDb; Q9GZV9; -.
PeptideAtlas; Q9GZV9; -.
PRIDE; Q9GZV9; -.
ProteomicsDB; 80160; -.
Ensembl; ENST00000237837; ENSP00000237837; ENSG00000118972.
GeneID; 8074; -.
KEGG; hsa:8074; -.
UCSC; uc001qmq.1; human.
CTD; 8074; -.
DisGeNET; 8074; -.
EuPathDB; HostDB:ENSG00000118972.1; -.
GeneCards; FGF23; -.
GeneReviews; FGF23; -.
HGNC; HGNC:3680; FGF23.
MalaCards; FGF23; -.
MIM; 193100; phenotype.
MIM; 605380; gene.
MIM; 617993; phenotype.
neXtProt; NX_Q9GZV9; -.
OpenTargets; ENSG00000118972; -.
Orphanet; 89937; Autosomal dominant hypophosphatemic rickets.
Orphanet; 306661; Familial hyperphosphatemic tumoral calcinosis/Hyperphosphatemic hyperostosis syndrome.
PharmGKB; PA28119; -.
eggNOG; KOG3885; Eukaryota.
eggNOG; ENOG4111IPH; LUCA.
GeneTree; ENSGT00940000160821; -.
HOGENOM; HOG000112573; -.
HOVERGEN; HBG051613; -.
InParanoid; Q9GZV9; -.
KO; K22428; -.
OMA; SPESCRF; -.
OrthoDB; EOG091G0NAY; -.
PhylomeDB; Q9GZV9; -.
TreeFam; TF335872; -.
Reactome; R-HSA-109704; PI3K Cascade.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1839122; Signaling by activated point mutants of FGFR1.
Reactome; R-HSA-1839130; Signaling by activated point mutants of FGFR3.
Reactome; R-HSA-190322; FGFR4 ligand binding and activation.
Reactome; R-HSA-190372; FGFR3c ligand binding and activation.
Reactome; R-HSA-190373; FGFR1c ligand binding and activation.
Reactome; R-HSA-190374; FGFR1c and Klotho ligand binding and activation.
Reactome; R-HSA-190375; FGFR2c ligand binding and activation.
Reactome; R-HSA-2033514; FGFR3 mutant receptor activation.
Reactome; R-HSA-2033519; Activated point mutants of FGFR2.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-5654219; Phospholipase C-mediated cascade: FGFR1.
Reactome; R-HSA-5654221; Phospholipase C-mediated cascade, FGFR2.
Reactome; R-HSA-5654227; Phospholipase C-mediated cascade, FGFR3.
Reactome; R-HSA-5654228; Phospholipase C-mediated cascade, FGFR4.
Reactome; R-HSA-5654687; Downstream signaling of activated FGFR1.
Reactome; R-HSA-5654688; SHC-mediated cascade:FGFR1.
Reactome; R-HSA-5654689; PI-3K cascade:FGFR1.
Reactome; R-HSA-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-HSA-5654695; PI-3K cascade:FGFR2.
Reactome; R-HSA-5654699; SHC-mediated cascade:FGFR2.
Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-HSA-5654704; SHC-mediated cascade:FGFR3.
Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-HSA-5654710; PI-3K cascade:FGFR3.
Reactome; R-HSA-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-HSA-5654719; SHC-mediated cascade:FGFR4.
Reactome; R-HSA-5654720; PI-3K cascade:FGFR4.
Reactome; R-HSA-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-HSA-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-HSA-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
Reactome; R-HSA-5658623; FGFRL1 modulation of FGFR1 signaling.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8853338; Signaling by FGFR3 point mutants in cancer.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
EvolutionaryTrace; Q9GZV9; -.
GeneWiki; Fibroblast_growth_factor_23; -.
GenomeRNAi; 8074; -.
PRO; PR:Q9GZV9; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000118972; Expressed in 21 organ(s), highest expression level in right atrium auricular region.
CleanEx; HS_FGF23; -.
Genevisible; Q9GZV9; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; TAS:Reactome.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0005105; F:type 1 fibroblast growth factor receptor binding; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0030643; P:cellular phosphate ion homeostasis; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0071354; P:cellular response to interleukin-6; IEA:Ensembl.
GO; GO:0044320; P:cellular response to leptin stimulus; IEA:Ensembl.
GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl.
GO; GO:0071305; P:cellular response to vitamin D; IEA:Ensembl.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0030502; P:negative regulation of bone mineralization; IDA:UniProtKB.
GO; GO:0046888; P:negative regulation of hormone secretion; ISS:UniProtKB.
GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:UniProtKB.
GO; GO:0055062; P:phosphate ion homeostasis; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0090080; P:positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; TAS:Reactome.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0010980; P:positive regulation of vitamin D 24-hydroxylase activity; IDA:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0010966; P:regulation of phosphate transport; IDA:UniProtKB.
GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
GO; GO:1904383; P:response to sodium phosphate; IEA:Ensembl.
GO; GO:0042369; P:vitamin D catabolic process; IDA:UniProtKB.
CDD; cd00058; FGF; 1.
InterPro; IPR028304; FGF23.
InterPro; IPR002209; Fibroblast_GF_fam.
InterPro; IPR008996; IL1/FGF.
PANTHER; PTHR11486; PTHR11486; 1.
PANTHER; PTHR11486:SF69; PTHR11486:SF69; 1.
Pfam; PF00167; FGF; 1.
SMART; SM00442; FGF; 1.
SUPFAM; SSF50353; SSF50353; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Differentiation;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Growth factor; Polymorphism; Reference proteome;
Secreted; Signal.
SIGNAL 1 24 {ECO:0000269|PubMed:15340161}.
CHAIN 25 251 Fibroblast growth factor 23.
/FTId=PRO_0000008998.
CHAIN 25 179 Fibroblast growth factor 23 N-terminal
peptide.
/FTId=PRO_0000352875.
CHAIN 180 251 Fibroblast growth factor 23 C-terminal
peptide.
/FTId=PRO_0000352876.
SITE 179 180 Cleavage; by proprotein convertases.
CARBOHYD 178 178 O-linked (GalNAc) threonine.
{ECO:0000269|PubMed:16638743}.
DISULFID 95 113
VARIANT 71 71 S -> G (in HFTC2; only the C-terminal
fragment is secreted, whereas the intact
protein is retained in the Golgi complex;
dbSNP:rs104894342).
{ECO:0000269|PubMed:15590700}.
/FTId=VAR_023831.
VARIANT 96 96 M -> T (in HFTC2; dbSNP:rs104894343).
{ECO:0000269|PubMed:16151858}.
/FTId=VAR_071711.
VARIANT 129 129 S -> F (in HFTC2; full-length and N-
terminal fragments are barely detectable,
whereas a C-terminal fragment with the
same molecular weight as that from wild-
type can be detected; dbSNP:rs104894344).
{ECO:0000269|PubMed:16030159}.
/FTId=VAR_071712.
VARIANT 157 157 F -> L (in HFTC2; dbSNP:rs772964687).
{ECO:0000269|PubMed:24680727}.
/FTId=VAR_071713.
VARIANT 176 176 R -> Q (in ADHR; partially resistant to
cleavage by furin; dbSNP:rs104894347).
{ECO:0000269|PubMed:11062477,
ECO:0000269|PubMed:16638743}.
/FTId=VAR_010717.
VARIANT 179 179 R -> Q (in ADHR; C-terminal processing is
abolished; reduced proteolysis by PHEX;
resistant to cleavage by furin;
dbSNP:rs193922702).
{ECO:0000269|PubMed:11062477,
ECO:0000269|PubMed:11409890,
ECO:0000269|PubMed:16638743}.
/FTId=VAR_010719.
VARIANT 179 179 R -> W (in ADHR; C-terminal processing is
abolished; dbSNP:rs28937882).
{ECO:0000269|PubMed:11062477}.
/FTId=VAR_010718.
VARIANT 195 195 P -> S (in dbSNP:rs13312793).
{ECO:0000269|Ref.5}.
/FTId=VAR_018887.
VARIANT 239 239 T -> M (in dbSNP:rs7955866).
{ECO:0000269|PubMed:11062477,
ECO:0000269|Ref.5}.
/FTId=VAR_010720.
STRAND 32 36 {ECO:0000244|PDB:5W21}.
STRAND 40 43 {ECO:0000244|PDB:2P39}.
STRAND 47 49 {ECO:0000244|PDB:2P39}.
STRAND 52 55 {ECO:0000244|PDB:2P39}.
STRAND 61 66 {ECO:0000244|PDB:2P39}.
TURN 69 71 {ECO:0000244|PDB:2P39}.
STRAND 73 77 {ECO:0000244|PDB:2P39}.
HELIX 79 81 {ECO:0000244|PDB:2P39}.
STRAND 82 87 {ECO:0000244|PDB:2P39}.
TURN 88 91 {ECO:0000244|PDB:2P39}.
STRAND 92 96 {ECO:0000244|PDB:2P39}.
STRAND 102 107 {ECO:0000244|PDB:2P39}.
TURN 110 112 {ECO:0000244|PDB:2P39}.
STRAND 115 119 {ECO:0000244|PDB:2P39}.
STRAND 121 123 {ECO:0000244|PDB:5W21}.
STRAND 125 128 {ECO:0000244|PDB:2P39}.
TURN 130 132 {ECO:0000244|PDB:2P39}.
STRAND 138 140 {ECO:0000244|PDB:2P39}.
STRAND 147 149 {ECO:0000244|PDB:5W21}.
HELIX 153 155 {ECO:0000244|PDB:2P39}.
STRAND 157 161 {ECO:0000244|PDB:2P39}.
HELIX 166 168 {ECO:0000244|PDB:2P39}.
SEQUENCE 251 AA; 27954 MW; 6093BD0CC50C2489 CRC64;
MLGARLRLWV CALCSVCSMS VLRAYPNASP LLGSSWGGLI HLYTATARNS YHLQIHKNGH
VDGAPHQTIY SALMIRSEDA GFVVITGVMS RRYLCMDFRG NIFGSHYFDP ENCRFQHQTL
ENGYDVYHSP QYHFLVSLGR AKRAFLPGMN PPPYSQFLSR RNEIPLIHFN TPIPRRHTRS
AEDDSERDPL NVLKPRARMT PAPASCSQEL PSAEDNSPMA SDPLGVVRGG RVNTHAGGTG
PEGCRPFAKF I


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