##gff-version 3 Q9GZV9 UniProtKB Signal peptide 1 24 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15340161;Dbxref=PMID:15340161 Q9GZV9 UniProtKB Chain 25 251 . . . ID=PRO_0000008998;Note=Fibroblast growth factor 23 Q9GZV9 UniProtKB Chain 25 179 . . . ID=PRO_0000352875;Note=Fibroblast growth factor 23 N-terminal peptide Q9GZV9 UniProtKB Chain 180 251 . . . ID=PRO_0000352876;Note=Fibroblast growth factor 23 C-terminal peptide Q9GZV9 UniProtKB Region 172 221 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9GZV9 UniProtKB Compositional bias 175 193 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9GZV9 UniProtKB Site 179 180 . . . Note=Cleavage%3B by proprotein convertases Q9GZV9 UniProtKB Modified residue 180 180 . . . Note=Phosphoserine%3B by FAM20C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31932717;Dbxref=PMID:31932717 Q9GZV9 UniProtKB Glycosylation 171 171 . . . Note=O-linked (GalNAc) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31932717;Dbxref=PMID:31932717 Q9GZV9 UniProtKB Glycosylation 178 178 . . . Note=O-linked (GalNAc) threonine;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16638743,ECO:0000269|PubMed:31932717;Dbxref=PMID:16638743,PMID:31932717 Q9GZV9 UniProtKB Disulfide bond 95 113 . . . . Q9GZV9 UniProtKB Natural variant 71 71 . . . ID=VAR_023831;Note=In HFTC2%3B only the C-terminal fragment is secreted%2C whereas the intact protein is retained in the Golgi complex. S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15590700;Dbxref=dbSNP:rs104894342,PMID:15590700 Q9GZV9 UniProtKB Natural variant 96 96 . . . ID=VAR_071711;Note=In HFTC2. M->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16151858;Dbxref=dbSNP:rs104894343,PMID:16151858 Q9GZV9 UniProtKB Natural variant 129 129 . . . ID=VAR_071712;Note=In HFTC2%3B full-length and N-terminal fragments are barely detectable%2C whereas a C-terminal fragment with the same molecular weight as that from wild-type can be detected. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16030159;Dbxref=dbSNP:rs104894344,PMID:16030159 Q9GZV9 UniProtKB Natural variant 157 157 . . . ID=VAR_071713;Note=In HFTC2. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24680727;Dbxref=dbSNP:rs772964687,PMID:24680727 Q9GZV9 UniProtKB Natural variant 176 176 . . . ID=VAR_010717;Note=In ADHR%3B partially resistant to cleavage by furin. R->Q;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11062477,ECO:0000269|PubMed:16638743;Dbxref=dbSNP:rs104894347,PMID:11062477,PMID:16638743 Q9GZV9 UniProtKB Natural variant 179 179 . . . ID=VAR_010719;Note=In ADHR%3B C-terminal processing is abolished%3B reduced proteolysis by PHEX%3B resistant to cleavage by furin. R->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11062477,ECO:0000269|PubMed:11409890,ECO:0000269|PubMed:16638743;Dbxref=dbSNP:rs193922702,PMID:11062477,PMID:11409890,PMID:16638743 Q9GZV9 UniProtKB Natural variant 179 179 . . . ID=VAR_010718;Note=In ADHR%3B C-terminal processing is abolished. R->W;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11062477;Dbxref=dbSNP:rs28937882,PMID:11062477 Q9GZV9 UniProtKB Natural variant 195 195 . . . ID=VAR_018887;Note=P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|Ref.5;Dbxref=dbSNP:rs13312793 Q9GZV9 UniProtKB Natural variant 239 239 . . . ID=VAR_010720;Note=T->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11062477,ECO:0000269|Ref.5;Dbxref=dbSNP:rs7955866,PMID:11062477 Q9GZV9 UniProtKB Mutagenesis 178 178 . . . Note=Loss of glycosylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:31932717;Dbxref=PMID:31932717 Q9GZV9 UniProtKB Beta strand 32 34 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7YSH Q9GZV9 UniProtKB Beta strand 36 38 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7YSW Q9GZV9 UniProtKB Beta strand 40 43 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Beta strand 47 49 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Beta strand 52 55 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Beta strand 61 66 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Turn 69 71 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Beta strand 73 77 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Helix 79 81 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Beta strand 82 87 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Turn 88 91 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Beta strand 92 96 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Beta strand 102 107 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Turn 110 112 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Beta strand 115 119 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Beta strand 121 123 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5W21 Q9GZV9 UniProtKB Beta strand 125 128 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Turn 130 132 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Beta strand 138 140 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Beta strand 147 149 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:5W21 Q9GZV9 UniProtKB Helix 153 155 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Beta strand 157 161 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39 Q9GZV9 UniProtKB Helix 166 168 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2P39