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Details on Person UniProt:Q9GZV9 FGF23
| Class:Id | ReferenceGeneProduct:54808 |
|---|---|
| _chainChangeLog | signal peptide:1-24 added on Sat February 7 2015;chain:25-251 added on Sat February 7 2015;chain:25-179 added on Sat February 7 2015;chain:180-251 added on Sat February 7 2015 |
| _displayName | UniProt:Q9GZV9 FGF23 |
| _timestamp | 2024-11-03 19:45:46 |
| chain | signal peptide:1-24 chain:25-251 chain:25-179 chain:180-251 |
| checksum | 6093BD0CC50C2489 |
| comment | FUNCTION Regulator of phosphate homeostasis (PubMed:11062477). Inhibits renal tubular phosphate transport by reducing SLC34A1 levels (PubMed:11409890). Up-regulates 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 (PubMed:15040831). Negatively regulates osteoblast differentiation and matrix mineralization (PubMed:18282132).SUBUNIT Interacts with FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:16597617). Affinity between fibroblast growth factors (FGFs) and their receptors is increased by KL and heparan sulfate glycosaminoglycans that function as coreceptors (By similarity).INTERACTION 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).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 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.PTM Phosphorylation at Ser-180 mediated by FAM20C slows down glycosylation at Thr-178 notably.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the heparin-binding growth factors family. |
| description | recommendedName: Fibroblast growth factor 23 shortName: FGF-23 alternativeName: Phosphatonin alternativeName: Tumor-derived hypophosphatemia-inducing factor component recommendedName: Fibroblast growth factor 23 N-terminal peptide /component component recommendedName: Fibroblast growth factor 23 C-terminal peptide /component |
| geneName | FGF23 HYPF UNQ3027/PRO9828 |
| identifier | Q9GZV9 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Differentiation Direct protein sequencing Disease variant Disulfide bond Glycoprotein Growth factor Phosphoprotein Proteomics identification Reference proteome Secreted Signal |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 |
| name | FGF23 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8993620] ENSEMBL:ENSG00000118972 FGF23 [Homo sapiens] |
| secondaryIdentifier | FGF23_HUMAN Q4V758 |
| sequenceLength | 251 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:189891] FGF23(25-251) [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:8851624] GalNAc-T178-FGF23(25-251) [Golgi lumen] [Homo sapiens] [EntityWithAccessionedSequence:8851630] FGF23(25-251) [Golgi lumen] [Homo sapiens] [EntityWithAccessionedSequence:8851633] GalNAc-T178-FGF23(25-251) [extracellular region] [Homo sapiens] [EntityWithAccessionedSequence:8956697] FGF23 [endoplasmic reticulum lumen] [Homo sapiens] [EntityWithAccessionedSequence:8957077] p-FGF23 [endoplasmic reticulum lumen] [Homo sapiens] |
| (referenceSequence) | [ModifiedResidue:8851623] O-(N-acetylamino)galactosyl-L-threonine at 178 [ModifiedResidue:8956918] phosphorylated residue at unknown position |
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No pathways have been reviewed or authored by UniProt:Q9GZV9 FGF23 (54808)
