Fgf23
entrez
64654
canonical
uniprot
Q9EPC2
canonical
ensembl
ENSMUSG00000000182
resolver
ensp
ENSMUSP00000000186
resolver
enst
ENSMUST00000000186
resolver
genesymbol
Fgf23
resolver
uniprot
Q3U1V5
resolver
uniprot_entry
FGF23_MOUSE
resolver
uniprot_entry
Q3U1V5_MOUSE
resolver
amino_acid_sequence
MLGTCLRLLVGVLCTVCSLGTARAYPDTSPLLGSNWGSLTHLYTATARTSYHLQIHRDGHVDGTPHQTIYSALMITSEDAGSVVITGAMTRRFLCMDLHGNIFGSLHFSPENCKFRQWTLENGYDVYLSQKHHYLVSLGRAKRIFQPGTNPPPFSQFLARRNEVPLLHFYTVRPRRHTRSAEDPPERDPLNVLKPRPRATPVPVSCSRELPSAEEGGPAASDPLGVLRRGRGDARGGAGGADRCRPFPRFV
uniprot
proteins
function
FUNCTION: 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). Up-regulates EGR1 expression in the presence of KL (PubMed:17086194). {ECO:0000250|UniProtKB:Q8VI82, ECO:0000250|UniProtKB:Q9GZV9, ECO:0000269|PubMed:17086194}.
uniprot
proteins
mass_dalton
27758
uniprot
proteins
post_translational_modification
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 (By similarity). {ECO:0000250|UniProtKB:Q9GZV9}.; PTM: O-glycosylated at Thr-171 and Thr-178 by GALNT3 and glycosylation of Thr-178 requires previous glycosylation at Thr171. 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). {ECO:0000250|UniProtKB:Q9GZV9}.; PTM: Phosphorylation at Ser-180 mediated by FAM20C slows down glycosylation at Thr-178 notably. {ECO:0000250|UniProtKB:Q9GZV9}.
uniprot
proteins
protein_family
Heparin-binding growth factors family
uniprot
proteins
pubmed
11032749
uniprot
proteins
pubmed
11062477
uniprot
proteins
pubmed
17086194
uniprot
proteins
sequence_length
251
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9GZV9}. Note=Secretion is dependent on O-glycosylation. {ECO:0000250|UniProtKB:Q9GZV9}.
uniprot
proteins