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Fibroblast growth factor 9 (FGF-9) (Glia-activating factor) (GAF) (Heparin-binding growth factor 9) (HBGF-9)

 FGF9_HUMAN              Reviewed;         208 AA.
P31371; A8K427; Q3SY32;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 3.
25-OCT-2017, entry version 183.
RecName: Full=Fibroblast growth factor 9;
Short=FGF-9;
AltName: Full=Glia-activating factor;
Short=GAF;
AltName: Full=Heparin-binding growth factor 9;
Short=HBGF-9;
Flags: Precursor;
Name=FGF9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Foreskin;
PubMed=8321227; DOI=10.1128/MCB.13.7.4251;
Miyamoto M., Naruo K., Seko C., Matsumoto S., Kondo T., Kurokawa T.;
"Molecular cloning of a novel cytokine cDNA encoding the ninth member
of the fibroblast growth factor family, which has a unique secretion
property.";
Mol. Cell. Biol. 13:4251-4259(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-94.
NIEHS SNPs program;
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) 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 4-26 AND 34-54.
TISSUE=Glial tumor;
PubMed=8428960;
Naruo K., Seko C., Kuroshima K., Matsutani E., Sasada R., Kondo T.,
Kurokawa T.;
"Novel secretory heparin-binding factors from human glioma cells
(glia-activating factors) involved in glial cell growth. Purification
and biological properties.";
J. Biol. Chem. 268:2857-2864(1993).
[8]
INTERACTION WITH FGFR2 AND FGFR3, AND FUNCTION IN CELL PROLIFERATION.
PubMed=8663044; DOI=10.1074/jbc.271.25.15292;
Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A.,
Coulier F., Gao G., Goldfarb M.;
"Receptor specificity of the fibroblast growth factor family.";
J. Biol. Chem. 271:15292-15297(1996).
[9]
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).
[10]
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).
[11]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), SUBUNIT, AND HEPARIN-BINDING.
PubMed=11223514; DOI=10.1107/S0907444900020813;
Hecht H.J., Adar R., Hofmann B., Bogin O., Weich H., Yayon A.;
"Structure of fibroblast growth factor 9 shows a symmetric dimer with
unique receptor- and heparin-binding interfaces.";
Acta Crystallogr. D 57:378-384(2001).
[12]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 35-208, AND SUBUNIT.
PubMed=11060292; DOI=10.1074/jbc.M006502200;
Plotnikov A.N., Eliseenkova A.V., Ibrahimi O.A., Shriver Z.,
Sasisekharan R., Lemmon M.A., Mohammadi M.;
"Crystal structure of fibroblast growth factor 9 reveals regions
implicated in dimerization and autoinhibition.";
J. Biol. Chem. 276:4322-4329(2001).
[13]
VARIANT SYNS3 ASN-99, AND CHARACTERIZATION OF VARIANT SYNS3 ASN-99.
PubMed=19589401; DOI=10.1016/j.ajhg.2009.06.007;
Wu X.L., Gu M.M., Huang L., Liu X.S., Zhang H.X., Ding X.Y., Xu J.Q.,
Cui B., Wang L., Lu S.Y., Chen X.Y., Zhang H.G., Huang W., Yuan W.T.,
Yang J.M., Gu Q., Fei J., Chen Z., Yuan Z.M., Wang Z.G.;
"Multiple synostoses syndrome is due to a missense mutation in exon 2
of FGF9 gene.";
Am. J. Hum. Genet. 85:53-63(2009).
-!- FUNCTION: Plays an important role in the regulation of embryonic
development, cell proliferation, cell differentiation and cell
migration. May have a role in glial cell growth and
differentiation during development, gliosis during repair and
regeneration of brain tissue after damage, differentiation and
survival of neuronal cells, and growth stimulation of glial
tumors. {ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:8663044}.
-!- SUBUNIT: Monomer. Homodimer. Interacts with FGFR1, FGFR2, FGFR3
and FGFR4. Affinity between fibroblast growth factors (FGFs) and
their receptors is increased by heparan sulfate glycosaminoglycans
that function as coreceptors. {ECO:0000269|PubMed:11060292,
ECO:0000269|PubMed:11223514, ECO:0000269|PubMed:16597617,
ECO:0000269|PubMed:8663044}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Glial cells.
-!- PTM: Three molecular species were found (30 kDa, 29 kDa and 25
kDa), cleaved at Leu-4, Val-13 and Ser-34 respectively. The
smaller ones might be products of proteolytic digestion.
Furthermore, there may be a functional signal sequence in the 30
kDa species which is uncleavable in the secretion step.
-!- PTM: N-glycosylated.
-!- DISEASE: Multiple synostoses syndrome 3 (SYNS3) [MIM:612961]: A
bone disease characterized by multiple progressive joint fusions
that commonly involve proximal interphalangeal, tarsal-carpal,
humeroradial and cervical spine joints. Additional features can
include progressive conductive deafness and facial dysmorphism.
{ECO:0000269|PubMed:19589401}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Biochemical analysis of the Asn-99 mutation reveals
a significantly impaired FGF signaling, as evidenced by diminished
activity of the MAPK1/MAPK2 pathway and decreases CTNNB1 and MYC
expression when compared with wild-type protein. Binding of mutant
protein to the receptor FGFR3 is severely impaired, although
homodimerization of mutant to itself or wild-type is not
detectably affected, providing a basis for the observed defective
FGF9 signaling.
-!- SIMILARITY: Belongs to the heparin-binding growth factors family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/fgf9/";
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EMBL; D14838; BAA03572.1; -; mRNA.
EMBL; AY682094; AAT74624.1; -; Genomic_DNA.
EMBL; AK290792; BAF83481.1; -; mRNA.
EMBL; AL139378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471075; EAX08316.1; -; Genomic_DNA.
EMBL; BC069692; AAH69692.1; -; mRNA.
EMBL; BC103978; AAI03979.1; -; mRNA.
EMBL; BC103979; AAI03980.1; -; mRNA.
CCDS; CCDS9298.1; -.
PIR; A48137; A48137.
RefSeq; NP_002001.1; NM_002010.2.
UniGene; Hs.111; -.
PDB; 1G82; X-ray; 2.60 A; A/B/C/D=49-208.
PDB; 1IHK; X-ray; 2.20 A; A=35-208.
PDB; 5W59; X-ray; 2.50 A; A=35-208.
PDBsum; 1G82; -.
PDBsum; 1IHK; -.
PDBsum; 5W59; -.
ProteinModelPortal; P31371; -.
SMR; P31371; -.
BioGrid; 108545; 17.
DIP; DIP-6036N; -.
STRING; 9606.ENSP00000371790; -.
iPTMnet; P31371; -.
PhosphoSitePlus; P31371; -.
BioMuta; FGF9; -.
DMDM; 544290; -.
PaxDb; P31371; -.
PRIDE; P31371; -.
Ensembl; ENST00000382353; ENSP00000371790; ENSG00000102678.
GeneID; 2254; -.
KEGG; hsa:2254; -.
UCSC; uc001uog.3; human.
CTD; 2254; -.
DisGeNET; 2254; -.
EuPathDB; HostDB:ENSG00000102678.6; -.
GeneCards; FGF9; -.
HGNC; HGNC:3687; FGF9.
HPA; CAB004392; -.
MalaCards; FGF9; -.
MIM; 600921; gene.
MIM; 612961; phenotype.
neXtProt; NX_P31371; -.
OpenTargets; ENSG00000102678; -.
Orphanet; 3237; Multiple synostoses syndrome.
PharmGKB; PA28126; -.
eggNOG; KOG3885; Eukaryota.
eggNOG; ENOG4111IPH; LUCA.
GeneTree; ENSGT00760000118859; -.
HOGENOM; HOG000236341; -.
HOVERGEN; HBG007580; -.
InParanoid; P31371; -.
KO; K04358; -.
OMA; NLYKHGE; -.
OrthoDB; EOG091G0NAY; -.
PhylomeDB; P31371; -.
TreeFam; TF317805; -.
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-190371; FGFR3b 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-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-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-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.
SignaLink; P31371; -.
SIGNOR; P31371; -.
EvolutionaryTrace; P31371; -.
GeneWiki; FGF9; -.
GenomeRNAi; 2254; -.
PRO; PR:P31371; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000102678; -.
CleanEx; HS_FGF9; -.
Genevisible; P31371; HS.
GO; GO:0005604; C:basement membrane; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; TAS:Reactome.
GO; GO:0005104; F:fibroblast growth factor receptor binding; IEA:Ensembl.
GO; GO:0008083; F:growth factor activity; TAS:ProtInc.
GO; GO:0008201; F:heparin binding; 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:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
GO; GO:0048566; P:embryonic digestive tract development; IEA:Ensembl.
GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl.
GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
GO; GO:0001654; P:eye development; IEA:Ensembl.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IGI:MGI.
GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0060484; P:lung-associated mesenchyme development; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
GO; GO:0030238; P:male sex determination; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IEA:Ensembl.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0048505; P:regulation of timing of cell differentiation; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0021762; P:substantia nigra development; IEP:UniProtKB.
CDD; cd00058; FGF; 1.
InterPro; IPR028251; FGF9.
InterPro; IPR002209; Fibroblast_GF_fam.
InterPro; IPR008996; IL1/FGF.
PANTHER; PTHR11486; PTHR11486; 1.
PANTHER; PTHR11486:SF28; PTHR11486:SF28; 1.
Pfam; PF00167; FGF; 1.
PRINTS; PR00263; HBGFFGF.
SMART; SM00442; FGF; 1.
SUPFAM; SSF50353; SSF50353; 1.
PROSITE; PS00247; HBGF_FGF; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Deafness; Developmental protein;
Differentiation; Direct protein sequencing; Disease mutation;
Glycoprotein; Growth factor; Heparin-binding; Mitogen; Polymorphism;
Reference proteome; Secreted.
PROPEP 1 3 {ECO:0000269|PubMed:8428960}.
/FTId=PRO_0000008973.
CHAIN 4 208 Fibroblast growth factor 9.
/FTId=PRO_0000008974.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
VARIANT 94 94 I -> V (in dbSNP:rs12427696).
{ECO:0000269|Ref.2}.
/FTId=VAR_020944.
VARIANT 99 99 S -> N (in SYNS3; expressed and secreted
as efficiently as wild-type; however it
induces compromised chondrocyte
proliferation and differentiation
accompanied by enhanced osteogenic
differentiation and matrix mineralization
of bone marrow-derived mesenchymal stem
cells; dbSNP:rs121918322).
{ECO:0000269|PubMed:19589401}.
/FTId=VAR_063254.
CONFLICT 24 26 VLP -> SLL (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 34 34 S -> A (in Ref. 7; AA sequence).
{ECO:0000305}.
HELIX 53 60 {ECO:0000244|PDB:1IHK}.
STRAND 63 68 {ECO:0000244|PDB:1IHK}.
STRAND 73 76 {ECO:0000244|PDB:1IHK}.
STRAND 82 87 {ECO:0000244|PDB:1IHK}.
HELIX 91 93 {ECO:0000244|PDB:1IHK}.
STRAND 95 101 {ECO:0000244|PDB:1IHK}.
STRAND 104 109 {ECO:0000244|PDB:1IHK}.
TURN 110 112 {ECO:0000244|PDB:1IHK}.
STRAND 115 118 {ECO:0000244|PDB:1IHK}.
STRAND 124 129 {ECO:0000244|PDB:1IHK}.
HELIX 132 134 {ECO:0000244|PDB:1IHK}.
STRAND 136 142 {ECO:0000244|PDB:1IHK}.
STRAND 145 154 {ECO:0000244|PDB:1IHK}.
TURN 156 158 {ECO:0000244|PDB:1IHK}.
STRAND 161 163 {ECO:0000244|PDB:1IHK}.
HELIX 175 177 {ECO:0000244|PDB:1IHK}.
HELIX 183 185 {ECO:0000244|PDB:1IHK}.
STRAND 187 190 {ECO:0000244|PDB:1IHK}.
HELIX 194 196 {ECO:0000244|PDB:1IHK}.
HELIX 200 203 {ECO:0000244|PDB:1IHK}.
SEQUENCE 208 AA; 23441 MW; F32A0E7106EF59C9 CRC64;
MAPLGEVGNY FGVQDAVPFG NVPVLPVDSP VLLSDHLGQS EAGGLPRGPA VTDLDHLKGI
LRRRQLYCRT GFHLEIFPNG TIQGTRKDHS RFGILEFISI AVGLVSIRGV DSGLYLGMNE
KGELYGSEKL TQECVFREQF EENWYNTYSS NLYKHVDTGR RYYVALNKDG TPREGTRTKR
HQKFTHFLPR PVDPDKVPEL YKDILSQS


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