ID   FGF17_MOUSE             Reviewed;         216 AA.
AC   P63075; O70627;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   24-JAN-2024, entry version 137.
DE   RecName: Full=Fibroblast growth factor 17;
DE            Short=FGF-17;
DE   Flags: Precursor;
GN   Name=Fgf17;
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].
RX   PubMed=9514906; DOI=10.1006/bbrc.1998.8239;
RA   Hoshikawa M., Ohbayashi N., Yonamine A., Konishi M., Ozaki K., Fukui S.,
RA   Itoh N.;
RT   "Structure and expression of a novel fibroblast growth factor, FGF-17,
RT   preferentially expressed in the embryonic brain.";
RL   Biochem. Biophys. Res. Commun. 244:187-191(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
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).
CC   -!- FUNCTION: Plays an important role in the regulation of embryonic
CC       development and as signaling molecule in the induction and patterning
CC       of the embryonic brain. Required for normal brain development.
CC   -!- SUBUNIT: Interacts with FGFR3 and FGFR4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC       {ECO:0000305}.
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DR   EMBL; AB009250; BAA25430.1; -; mRNA.
DR   EMBL; AK077555; BAC36859.1; -; mRNA.
DR   CCDS; CCDS27260.1; -.
DR   RefSeq; NP_032030.1; NM_008004.4.
DR   RefSeq; XP_006518614.1; XM_006518551.3.
DR   RefSeq; XP_011243255.1; XM_011244953.2.
DR   AlphaFoldDB; P63075; -.
DR   SMR; P63075; -.
DR   STRING; 10090.ENSMUSP00000022697; -.
DR   GlyCosmos; P63075; 1 site, No reported glycans.
DR   GlyGen; P63075; 1 site.
DR   PhosphoSitePlus; P63075; -.
DR   PaxDb; 10090-ENSMUSP00000022697; -.
DR   Antibodypedia; 22456; 371 antibodies from 29 providers.
DR   DNASU; 14171; -.
DR   Ensembl; ENSMUST00000022697.7; ENSMUSP00000022697.6; ENSMUSG00000022101.7.
DR   GeneID; 14171; -.
DR   KEGG; mmu:14171; -.
DR   UCSC; uc007uos.1; mouse.
DR   AGR; MGI:1202401; -.
DR   CTD; 8822; -.
DR   MGI; MGI:1202401; Fgf17.
DR   VEuPathDB; HostDB:ENSMUSG00000022101; -.
DR   eggNOG; KOG3885; Eukaryota.
DR   GeneTree; ENSGT00940000161965; -.
DR   HOGENOM; CLU_090682_0_0_1; -.
DR   InParanoid; P63075; -.
DR   OMA; LCCQTQV; -.
DR   OrthoDB; 4098345at2759; -.
DR   PhylomeDB; P63075; -.
DR   TreeFam; TF331233; -.
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-5658623; FGFRL1 modulation of FGFR1 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; 14171; 2 hits in 78 CRISPR screens.
DR   PRO; PR:P63075; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; P63075; Protein.
DR   Bgee; ENSMUSG00000022101; Expressed in embryonic post-anal tail and 63 other cell types or tissues.
DR   ExpressionAtlas; P63075; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR   GO; GO:0005105; F:type 1 fibroblast growth factor receptor binding; ISO:MGI.
DR   GO; GO:0005111; F:type 2 fibroblast growth factor receptor binding; ISO:MGI.
DR   GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR   Gene3D; 2.80.10.50; -; 1.
DR   InterPro; IPR002209; Fibroblast_GF_fam.
DR   InterPro; IPR008996; IL1/FGF.
DR   PANTHER; PTHR11486; FIBROBLAST GROWTH FACTOR; 1.
DR   PANTHER; PTHR11486:SF71; FIBROBLAST GROWTH FACTOR 17; 1.
DR   Pfam; PF00167; FGF; 1.
DR   PRINTS; PR00262; IL1HBGF.
DR   SMART; SM00442; FGF; 1.
DR   SUPFAM; SSF50353; Cytokine; 1.
DR   PROSITE; PS00247; HBGF_FGF; 1.
DR   Genevisible; P63075; MM.
PE   2: Evidence at transcript level;
KW   Developmental protein; Glycoprotein; Growth factor; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..216
FT                   /note="Fibroblast growth factor 17"
FT                   /id="PRO_0000008986"
FT   REGION          195..216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   216 AA;  24924 MW;  2EE94BDF75220F4C CRC64;
     MGAARLLPNL TLCLQLLILC CQTQGENHPS PNFNQYVRDQ GAMTDQLSRR QIREYQLYSR
     TSGKHVQVTG RRISATAEDG NKFAKLIVET DTFGSRVRIK GAESEKYICM NKRGKLIGKP
     SGKSKDCVFT EIVLENNYTA FQNARHEGWF MAFTRQGRPR QASRSRQNQR EAHFIKRLYQ
     GQLPFPNHAE RQKQFEFVGS APTRRTKRTR RPQSQT
//