FGF9_MOUSE
ID FGF9_MOUSE Reviewed; 208 AA.
AC P54130; Q499I9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Fibroblast growth factor 9;
DE Short=FGF-9;
DE AltName: Full=Glia-activating factor;
DE Short=GAF;
DE AltName: Full=HBGF-9;
DE Flags: Precursor;
GN Name=Fgf9; Synonyms=Fgf-9;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FVB/NJ;
RX PubMed=8576175; DOI=10.1074/jbc.271.3.1726;
RA Santos-Ocampo S., Colvin J.S., Chellaiah A.T., Ornitz D.M.;
RT "Expression and biological activity of mouse fibroblast growth factor-9.";
RL J. Biol. Chem. 271:1726-1731(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7656983; DOI=10.1016/0014-5793(95)00836-x;
RA Seo M., Noguchi K.;
RT "Retinoic acid induces gene expression of fibroblast growth factor-9 during
RT induction of neuronal differentiation of mouse embryonal carcinoma P19
RT cells.";
RL FEBS Lett. 370:231-235(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8619928; DOI=10.3109/08977199509036882;
RA Hecht D., Zimmerman N., Bedford M., Avivi A., Yayon A.;
RT "Identification of fibroblast growth factor 9 (FGF9) as a high affinity,
RT heparin dependent ligand for FGF receptors 3 and 2 but not for FGF
RT receptors 1 and 4.";
RL Growth Factors 12:223-233(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=10474167;
RX DOI=10.1002/(sici)1097-0177(199909)216:1<72::aid-dvdy9>3.0.co;2-9;
RA Colvin J.S., Feldman B., Nadeau J.H., Goldfarb M., Ornitz D.M.;
RT "Genomic organization and embryonic expression of the mouse fibroblast
RT growth factor 9 gene.";
RL Dev. Dyn. 216:72-88(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Plays an important role in the regulation of embryonic
CC development, cell proliferation, cell differentiation and cell
CC migration. May have a role in glial cell growth and differentiation
CC during development, gliosis during repair and regeneration of brain
CC tissue after damage, differentiation and survival of neuronal cells,
CC and growth stimulation of glial tumors.
CC -!- SUBUNIT: Monomer. Homodimer. Interacts with FGFR1, FGFR2, FGFR3 and
CC FGFR4. Affinity between fibroblast growth factors (FGFs) and their
CC receptors is increased by heparan sulfate glycosaminoglycans that
CC function as coreceptors (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC {ECO:0000305}.
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DR EMBL; U33535; AAC52529.1; -; mRNA.
DR EMBL; D38258; BAA07410.1; -; mRNA.
DR EMBL; S82023; AAB36429.1; -; mRNA.
DR EMBL; AF144626; AAD49222.1; -; Genomic_DNA.
DR EMBL; AF144624; AAD49222.1; JOINED; Genomic_DNA.
DR EMBL; AF144625; AAD49222.1; JOINED; Genomic_DNA.
DR EMBL; AK158782; BAE34661.1; -; mRNA.
DR EMBL; AC125399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154202; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466535; EDL36153.1; -; Genomic_DNA.
DR EMBL; BC099872; AAH99872.1; -; mRNA.
DR EMBL; BC099873; AAH99873.1; -; mRNA.
DR EMBL; BC099874; AAH99874.1; -; mRNA.
DR EMBL; BC099875; AAH99875.1; -; mRNA.
DR EMBL; BC125237; AAI25238.1; -; mRNA.
DR CCDS; CCDS27164.1; -.
DR RefSeq; NP_038546.2; NM_013518.4.
DR AlphaFoldDB; P54130; -.
DR SMR; P54130; -.
DR BioGRID; 199654; 1.
DR DIP; DIP-6032N; -.
DR STRING; 10090.ENSMUSP00000022545; -.
DR GlyGen; P54130; 1 site.
DR PhosphoSitePlus; P54130; -.
DR PaxDb; P54130; -.
DR PRIDE; P54130; -.
DR Antibodypedia; 3827; 412 antibodies from 34 providers.
DR DNASU; 14180; -.
DR Ensembl; ENSMUST00000022545; ENSMUSP00000022545; ENSMUSG00000021974.
DR GeneID; 14180; -.
DR KEGG; mmu:14180; -.
DR UCSC; uc007udx.2; mouse.
DR CTD; 2254; -.
DR MGI; MGI:104723; Fgf9.
DR VEuPathDB; HostDB:ENSMUSG00000021974; -.
DR eggNOG; KOG3885; Eukaryota.
DR GeneTree; ENSGT00940000160956; -.
DR HOGENOM; CLU_081609_0_0_1; -.
DR InParanoid; P54130; -.
DR OMA; FFWIYLS; -.
DR OrthoDB; 1097566at2759; -.
DR PhylomeDB; P54130; -.
DR TreeFam; TF317805; -.
DR Reactome; R-MMU-109704; PI3K Cascade.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-190322; FGFR4 ligand binding and activation.
DR Reactome; R-MMU-190371; FGFR3b ligand binding and activation.
DR Reactome; R-MMU-190372; FGFR3c ligand binding and activation.
DR Reactome; R-MMU-190373; FGFR1c ligand binding and activation.
DR Reactome; R-MMU-190375; FGFR2c ligand binding and activation.
DR Reactome; R-MMU-5654219; Phospholipase C-mediated cascade: FGFR1.
DR Reactome; R-MMU-5654221; Phospholipase C-mediated cascade, FGFR2.
DR Reactome; R-MMU-5654227; Phospholipase C-mediated cascade, FGFR3.
DR Reactome; R-MMU-5654228; Phospholipase C-mediated cascade, FGFR4.
DR Reactome; R-MMU-5654687; Downstream signaling of activated FGFR1.
DR Reactome; R-MMU-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-MMU-5654689; PI-3K cascade:FGFR1.
DR Reactome; R-MMU-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-MMU-5654695; PI-3K cascade:FGFR2.
DR Reactome; R-MMU-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-MMU-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-MMU-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-MMU-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-MMU-5654710; PI-3K cascade:FGFR3.
DR Reactome; R-MMU-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-MMU-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-MMU-5654720; PI-3K cascade:FGFR4.
DR Reactome; R-MMU-5654726; Negative regulation of FGFR1 signaling.
DR Reactome; R-MMU-5654727; Negative regulation of FGFR2 signaling.
DR Reactome; R-MMU-5654732; Negative regulation of FGFR3 signaling.
DR Reactome; R-MMU-5654733; Negative regulation of FGFR4 signaling.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR BioGRID-ORCS; 14180; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Fgf9; mouse.
DR PRO; PR:P54130; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P54130; protein.
DR Bgee; ENSMUSG00000021974; Expressed in mesenchyme of tongue and 250 other tissues.
DR ExpressionAtlas; P54130; baseline and differential.
DR Genevisible; P54130; MM.
DR GO; GO:0005604; C:basement membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005104; F:fibroblast growth factor receptor binding; ISO:MGI.
DR GO; GO:0008083; F:growth factor activity; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0032924; P:activin receptor signaling pathway; IDA:MGI.
DR GO; GO:0001525; P:angiogenesis; IDA:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0003214; P:cardiac left ventricle morphogenesis; TAS:DFLAT.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; IMP:MGI.
DR GO; GO:0003231; P:cardiac ventricle development; TAS:DFLAT.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0007267; P:cell-cell signaling; IMP:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
DR GO; GO:0048566; P:embryonic digestive tract development; IMP:MGI.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR GO; GO:0048706; P:embryonic skeletal system development; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IDA:MGI.
DR GO; GO:0001654; P:eye development; IMP:CACAO.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR GO; GO:0030324; P:lung development; IDA:MGI.
DR GO; GO:0060484; P:lung-associated mesenchyme development; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0030238; P:male sex determination; IMP:MGI.
DR GO; GO:0010463; P:mesenchymal cell proliferation; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:1905931; P:negative regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching; ISO:MGI.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IGI:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IDA:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:MGI.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IDA:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:2000243; P:positive regulation of reproductive process; IMP:MGI.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IDA:MGI.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:DFLAT.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0048505; P:regulation of timing of cell differentiation; IMP:MGI.
DR GO; GO:0060011; P:Sertoli cell proliferation; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IDA:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IDA:MGI.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0060979; P:vasculogenesis involved in coronary vascular morphogenesis; TAS:DFLAT.
DR GO; GO:0016055; P:Wnt signaling pathway; IGI:MGI.
DR CDD; cd00058; FGF; 1.
DR InterPro; IPR028251; FGF9.
DR InterPro; IPR002209; Fibroblast_GF_fam.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR11486; PTHR11486; 1.
DR PANTHER; PTHR11486:SF28; PTHR11486:SF28; 1.
DR Pfam; PF00167; FGF; 1.
DR PRINTS; PR00263; HBGFFGF.
DR SMART; SM00442; FGF; 1.
DR SUPFAM; SSF50353; SSF50353; 1.
DR PROSITE; PS00247; HBGF_FGF; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; Glycoprotein; Growth factor;
KW Heparin-binding; Mitogen; Reference proteome; Secreted.
FT PROPEP 1..3
FT /evidence="ECO:0000250"
FT /id="PRO_0000008975"
FT CHAIN 4..208
FT /note="Fibroblast growth factor 9"
FT /id="PRO_0000008976"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 34
FT /note="S -> N (in Ref. 1; AAC52529 and 4; AAD49222)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 208 AA; 23414 MW; 4A3CE894DFF643EB CRC64;
MAPLGEVGSY FGVQDAVPFG NVPVLPVDSP VLLSDHLGQS EAGGLPRGPA VTDLDHLKGI
LRRRQLYCRT GFHLEIFPNG TIQGTRKDHS RFGILEFISI AVGLVSIRGV DSGLYLGMNE
KGELYGSEKL TQECVFREQF EENWYNTYSS NLYKHVDTGR RYYVALNKDG TPREGTRTKR
HQKFTHFLPR PVDPDKVPEL YKDILSQS
