FGF5_RAT
ID FGF5_RAT Reviewed; 266 AA.
AC P48807; Q63402;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC STRAIN=Wistar;
RX PubMed=8611621; DOI=10.1016/0167-4781(19)60001-1;
RA Hattori Y., Yamasaki M., Itoh N.;
RT "The rat FGF-5 mRNA variant generated by alternative splicing encodes a
RT novel truncated form of FGF-5.";
RL Biochim. Biophys. Acta 1306:31-33(1996).
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=P48807-1; Sequence=Displayed;
CC Name=Short; Synonyms=FGF-5S;
CC IsoId=P48807-2; Sequence=VSP_001522, VSP_001523;
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}.
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DR EMBL; D64085; BAA10966.1; -; mRNA.
DR EMBL; D64086; BAA10967.1; -; mRNA.
DR PIR; S68144; S68144.
DR PIR; S68145; S68145.
DR RefSeq; NP_071547.1; NM_022211.1. [P48807-1]
DR RefSeq; XP_006250763.1; XM_006250701.3. [P48807-2]
DR AlphaFoldDB; P48807; -.
DR SMR; P48807; -.
DR STRING; 10116.ENSRNOP00000029046; -.
DR GlyGen; P48807; 1 site.
DR PaxDb; P48807; -.
DR PRIDE; P48807; -.
DR GeneID; 60662; -.
DR KEGG; rno:60662; -.
DR UCSC; RGD:620129; rat. [P48807-1]
DR CTD; 2250; -.
DR RGD; 620129; Fgf5.
DR eggNOG; KOG3885; Eukaryota.
DR InParanoid; P48807; -.
DR OrthoDB; 1157770at2759; -.
DR PhylomeDB; P48807; -.
DR Reactome; R-RNO-109704; PI3K Cascade.
DR Reactome; R-RNO-1257604; PIP3 activates AKT signaling.
DR Reactome; R-RNO-190372; FGFR3c ligand binding and activation.
DR Reactome; R-RNO-190373; FGFR1c ligand binding and activation.
DR Reactome; R-RNO-190375; FGFR2c ligand binding and activation.
DR Reactome; R-RNO-5654219; Phospholipase C-mediated cascade: FGFR1.
DR Reactome; R-RNO-5654221; Phospholipase C-mediated cascade, FGFR2.
DR Reactome; R-RNO-5654227; Phospholipase C-mediated cascade, FGFR3.
DR Reactome; R-RNO-5654687; Downstream signaling of activated FGFR1.
DR Reactome; R-RNO-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-RNO-5654689; PI-3K cascade:FGFR1.
DR Reactome; R-RNO-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-RNO-5654695; PI-3K cascade:FGFR2.
DR Reactome; R-RNO-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-RNO-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-RNO-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-RNO-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-RNO-5654710; PI-3K cascade:FGFR3.
DR Reactome; R-RNO-5654726; Negative regulation of FGFR1 signaling.
DR Reactome; R-RNO-5654727; Negative regulation of FGFR2 signaling.
DR Reactome; R-RNO-5654732; Negative regulation of FGFR3 signaling.
DR Reactome; R-RNO-5658623; FGFRL1 modulation of FGFR1 signaling.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR PRO; PR:P48807; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000022631; Expressed in frontal cortex and 2 other tissues.
DR ExpressionAtlas; P48807; 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:0005104; F:fibroblast growth factor receptor binding; ISO:RGD.
DR GO; GO:0008083; F:growth factor activity; IDA:RGD.
DR GO; GO:0005163; F:nerve growth factor receptor binding; TAS:RGD.
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; IDA:RGD.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0010001; P:glial cell differentiation; ISO:RGD.
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:RGD.
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; ISO:RGD.
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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..266
FT /note="Fibroblast growth factor 5"
FT /id="PRO_0000008960"
FT REGION 23..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..256
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 -> QIYR (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8611621"
FT /id="VSP_001522"
FT VAR_SEQ 122..266
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8611621"
FT /id="VSP_001523"
SQ SEQUENCE 266 AA; 29264 MW; 95B0A0CA7C0A200C CRC64;
MSLSLLFLIF CSHLILSAPA QGEKRLTPEG QPAPPRNPGD SSGSRGRSSA TFASSSASSP
VAASPGSQGS GSEHSSFQWS PSGRRTGSLY CRVGIGFHLQ IYPDGKVNGS HEASVLSILE
IFAVSQGIVG IRGVFSNKFL AMSKKGKLHA SAKFTDDCKF RERFQENSYN TYASAIHRTE
KTGREWYVAL NKRGKAKRGC SPRVKPQHVS THFLPRFKQS EQPELSFTVT VPEKKKPPRP
WKPKVPLSPS RRSPSPVKYR LKFRFG
