Fgf23
entrez
170583
canonical
uniprot
Q8VI82
canonical
ensembl
ENSRNOG00000066556
resolver
ensembl
ENSRNOG00055010713
resolver
ensembl
ENSRNOG00060017634
resolver
ensembl
ENSRNOG00065033593
resolver
ensp
ENSRNOP00000087703
resolver
ensp
ENSRNOP00055014551
resolver
ensp
ENSRNOP00060024337
resolver
ensp
ENSRNOP00065047503
resolver
enst
ENSRNOT00055018109
resolver
enst
ENSRNOT00060030149
resolver
enst
ENSRNOT00065057716
resolver
genesymbol
Fgf23
resolver
uniprot_entry
FGF23_RAT
resolver
amino_acid_sequence
MLGACLRLLVGALCTVCSLGTARAYSDTSPLLGSNWGSLTHLYTATARNSYHLQIHRDGHVDGTPHQTIYSALMITSEDAGSVVIIGAMTRRFLCMDLRGNIFGSYHFSPENCRFRQWTLENGYDVYLSPKHHYLVSLGRSKRIFQPGTNPPPFSQFLARRNEVPLLHFYTARPRRHTRSAEDPPERDPLNVLKPRPRATPIPVSCSRELPSAEEGGPAASDPLGVLRRGRGDARRGAGGTDRCRPFPRFV
uniprot
proteins
function
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 (PubMed:17992255). Up-regulates EGR1 expression in the presence of KL (PubMed:17086194). {ECO:0000250|UniProtKB:Q9GZV9, ECO:0000269|PubMed:17086194, ECO:0000269|PubMed:17992255}.
uniprot
proteins
mass_dalton
27912
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
17086194
uniprot
proteins
pubmed
17992255
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