FGF2_RABIT
ID FGF2_RABIT Reviewed; 137 AA.
AC P48799;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Fibroblast growth factor 2;
DE Short=FGF-2;
DE AltName: Full=Basic fibroblast growth factor;
DE Short=bFGF;
DE AltName: Full=Heparin-binding growth factor 2;
DE Short=HBGF-2;
DE Flags: Fragment;
GN Name=FGF2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Smooth muscle;
RX PubMed=8342599;
RA Winkles J.A., Friesel R., Alberts G.F., Janat M.F., Liau G.;
RT "Elevated expression of basic fibroblast growth factor in an immortalized
RT rabbit smooth muscle cell line.";
RL Am. J. Pathol. 143:518-527(1993).
CC -!- FUNCTION: Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4 (By
CC similarity). Also acts as an integrin ligand which is required for FGF2
CC signaling (By similarity). Binds to integrin ITGAV:ITGB3 (By
CC similarity). Plays an important role in the regulation of cell
CC survival, cell division, cell differentiation and cell migration (By
CC similarity). Functions as a potent mitogen in vitro (By similarity).
CC Can induce angiogenesis (By similarity). Mediates phosphorylation of
CC ERK1/2 and thereby promotes retinal lens fiber differentiation (By
CC similarity). {ECO:0000250|UniProtKB:P09038}.
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. Interacts with CSPG4, FGFBP1 and TEC. Found in
CC a complex with FGFBP1, FGF1 and FGF2. Interacts with FGFBP3. Interacts
CC with integrin ITGAV:ITGB3; the interaction is required for FGF2
CC signaling. Interacts with SNORC (via the extracellular domain).
CC Interacts with glypican GPC3. {ECO:0000250|UniProtKB:P09038,
CC ECO:0000250|UniProtKB:P13109, ECO:0000250|UniProtKB:P15655}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P09038}. Nucleus
CC {ECO:0000250|UniProtKB:P09038}. Note=Exported from cells by an
CC endoplasmic reticulum (ER)/Golgi-independent mechanism (By similarity).
CC Unconventional secretion of FGF2 occurs by direct translocation across
CC the plasma membrane (By similarity). Binding of exogenous FGF2 to FGFR
CC facilitates endocytosis followed by translocation of FGF2 across
CC endosomal membrane into the cytosol (By similarity). Nuclear import
CC from the cytosol requires the classical nuclear import machinery,
CC involving proteins KPNA1 and KPNB1, as well as CEP57 (By similarity).
CC {ECO:0000250|UniProtKB:P09038}.
CC -!- PTM: Phosphorylation at Tyr-73 regulates FGF2 unconventional secretion.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC {ECO:0000305}.
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DR EMBL; L12034; AAA31248.1; -; mRNA.
DR PIR; I46711; I46711.
DR AlphaFoldDB; P48799; -.
DR BMRB; P48799; -.
DR SMR; P48799; -.
DR CORUM; P48799; -.
DR STRING; 9986.ENSOCUP00000000416; -.
DR eggNOG; KOG3885; Eukaryota.
DR InParanoid; P48799; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005104; F:fibroblast growth factor receptor binding; IEA:InterPro.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:InterPro.
DR GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:1902748; P:positive regulation of lens fiber cell differentiation; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISS:UniProtKB.
DR CDD; cd00058; FGF; 1.
DR InterPro; IPR028223; FGF2.
DR InterPro; IPR002209; Fibroblast_GF_fam.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR11486; PTHR11486; 1.
DR PANTHER; PTHR11486:SF83; PTHR11486:SF83; 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 Angiogenesis; Developmental protein; Differentiation; Growth factor;
KW Heparin-binding; Isopeptide bond; Mitogen; Nucleus; Phosphoprotein;
KW Reference proteome; Secreted; Ubl conjugation.
FT CHAIN 1..>137
FT /note="Fibroblast growth factor 2"
FT /id="PRO_0000147600"
FT REGION 119..135
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT SITE 119
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P09038"
FT SITE 120
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P09038"
FT SITE 125
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P09038"
FT MOD_RES 73
FT /note="Phosphotyrosine; by TEC"
FT /evidence="ECO:0000250|UniProtKB:P09038"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P09038"
FT NON_TER 137
SQ SEQUENCE 137 AA; 15419 MW; 0D9EE457B88E8C51 CRC64;
PALPEDGGSG AFPPGHFKDP KRLYCKNGGF FLRIHPDGRV DGVREKSDPH IKLQLQAEER
GVVSIKGVCA NRYLAMKEDG RLLASKCVTD ECFFFERLES NNYNTYRSRK YSSWYVALKR
TGQYKLGSKT GPGQKAI
