FGF5_MOUSE
ID FGF5_MOUSE Reviewed; 264 AA.
AC P15656; O88825;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Fibroblast growth factor 5;
DE Short=FGF-5;
DE AltName: Full=Heparin-binding growth factor 5;
DE Short=HBGF-5;
DE Flags: Precursor;
GN Name=Fgf5; Synonyms=Fgf-5;
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] (ISOFORM LONG).
RX PubMed=2318343; DOI=10.1016/0012-1606(90)90211-z;
RA Hebert J.M., Basilico C., Goldfarb M., Haub O., Martin G.R.;
RT "Isolation of cDNAs encoding four mouse FGF family members and
RT characterization of their expression patterns during embryogenesis.";
RL Dev. Biol. 138:454-463(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
RC STRAIN=C57BL/6J;
RX PubMed=1700424; DOI=10.1073/pnas.87.20.8022;
RA Haub O., Drucker B., Goldfarb M.;
RT "Expression of the murine fibroblast growth factor 5 gene in the adult
RT central nervous system.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8022-8026(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX PubMed=9786939; DOI=10.1074/jbc.273.44.29262;
RA Ozawa K., Suzuki S., Asada M., Tomooka Y., Li A.J., Yoneda A., Komi A.,
RA Imamura T.;
RT "An alternatively spliced fibroblast growth factor (FGF)-5 mRNA is abundant
RT in brain and translates into a partial agonist/antagonist for FGF-5
RT neurotrophic activity.";
RL J. Biol. Chem. 273:29262-29271(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 cell
CC proliferation and cell differentiation. Required for normal regulation
CC of the hair growth cycle. Functions as an inhibitor of hair elongation
CC by promoting progression from anagen, the growth phase of the hair
CC follicle, into catagen the apoptosis-induced regression phase (By
CC similarity). {ECO:0000250|UniProtKB:Q20FD0}.
CC -!- SUBUNIT: Interacts with FGFR1 and FGFR2. Affinity between fibroblast
CC growth factors (FGFs) and their receptors is increased by heparan
CC sulfate glycosaminoglycans that function as coreceptors (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P15656-1; Sequence=Displayed;
CC Name=Short; Synonyms=FGF-5S;
CC IsoId=P15656-2; Sequence=VSP_001520, VSP_001521;
CC -!- MISCELLANEOUS: [Isoform Short]: Seems to have an antagonistic effect
CC compared to that of the isoform Long. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M30643; AAA96698.1; -; mRNA.
DR EMBL; M37823; AAB02660.1; -; Genomic_DNA.
DR EMBL; M37821; AAB02660.1; JOINED; Genomic_DNA.
DR EMBL; M37822; AAB02660.1; JOINED; Genomic_DNA.
DR EMBL; M37821; AAB02659.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB016516; BAA33737.1; -; mRNA.
DR EMBL; AK028694; BAC26069.1; -; mRNA.
DR EMBL; AK028894; BAC26179.1; -; mRNA.
DR EMBL; BC071227; AAH71227.1; -; mRNA.
DR CCDS; CCDS19455.1; -. [P15656-1]
DR CCDS; CCDS80344.1; -. [P15656-2]
DR PIR; A36207; A36207.
DR PIR; B36207; B36207.
DR RefSeq; NP_001264197.1; NM_001277268.1. [P15656-2]
DR RefSeq; NP_034333.1; NM_010203.5. [P15656-1]
DR AlphaFoldDB; P15656; -.
DR SMR; P15656; -.
DR STRING; 10090.ENSMUSP00000031280; -.
DR GlyGen; P15656; 1 site.
DR iPTMnet; P15656; -.
DR PhosphoSitePlus; P15656; -.
DR PaxDb; P15656; -.
DR PRIDE; P15656; -.
DR Antibodypedia; 4148; 296 antibodies from 37 providers.
DR DNASU; 14176; -.
DR Ensembl; ENSMUST00000031280; ENSMUSP00000031280; ENSMUSG00000029337. [P15656-1]
DR Ensembl; ENSMUST00000200059; ENSMUSP00000142420; ENSMUSG00000029337. [P15656-2]
DR GeneID; 14176; -.
DR KEGG; mmu:14176; -.
DR UCSC; uc008ygc.2; mouse. [P15656-1]
DR UCSC; uc008ygd.2; mouse. [P15656-2]
DR CTD; 2250; -.
DR MGI; MGI:95519; Fgf5.
DR VEuPathDB; HostDB:ENSMUSG00000029337; -.
DR eggNOG; KOG3885; Eukaryota.
DR GeneTree; ENSGT00940000158449; -.
DR HOGENOM; CLU_081609_7_0_1; -.
DR InParanoid; P15656; -.
DR OMA; TQVKYWP; -.
DR OrthoDB; 1157770at2759; -.
DR PhylomeDB; P15656; -.
DR TreeFam; TF317805; -.
DR Reactome; R-MMU-109704; PI3K Cascade.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
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-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-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-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; 14176; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Fgf5; mouse.
DR PRO; PR:P15656; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P15656; protein.
DR Bgee; ENSMUSG00000029337; Expressed in mesenchyme of tongue and 64 other tissues.
DR Genevisible; P15656; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; ISO:MGI.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0010001; P:glial cell differentiation; 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; ISO: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 GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IDA:MGI.
DR CDD; cd00058; FGF; 1.
DR InterPro; IPR028240; FGF5.
DR InterPro; IPR002209; Fibroblast_GF_fam.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR11486; PTHR11486; 1.
DR PANTHER; PTHR11486:SF23; PTHR11486:SF23; 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 Alternative splicing; Glycoprotein; Growth factor; Mitogen;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..264
FT /note="Fibroblast growth factor 5"
FT /id="PRO_0000008959"
FT REGION 25..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 118..121
FT /note="ILEI -> QIYG (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:9786939"
FT /id="VSP_001520"
FT VAR_SEQ 122..264
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:9786939"
FT /id="VSP_001521"
SQ SEQUENCE 264 AA; 29103 MW; F6A9C8153EE923D1 CRC64;
MSLSLLFLIF CSHLIHSAWA HGEKRLTPEG QPAPPRNPGD SSGSRGRSSA TFSSSSASSP
VAASPGSQGS GSEHSSFQWS PSGRRTGSLY CRVGIGFHLQ IYPDGKVNGS HEASVLSILE
IFAVSQGIVG IRGVFSNKFL AMSKKGKLHA SAKFTDDCKF RERFQENSYN TYASAIHRTE
KTGREWYVAL NKRGKAKRGC SPRVKPQHVS THFLPRFKQS EQPELSFTVT VPEKKKPPVK
PKVPLSQPRR SPSPVKYRLK FRFG
