FGF2_PANTR
ID FGF2_PANTR Reviewed; 288 AA.
AC Q5IS69;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Fibroblast growth factor 2 {ECO:0000312|EMBL:AAV74297.1};
DE Short=FGF-2;
DE AltName: Full=Basic fibroblast growth factor {ECO:0000250|UniProtKB:P09038};
DE Short=bFGF;
DE AltName: Full=Heparin-binding growth factor 2 {ECO:0000250|UniProtKB:P09038};
DE Short=HBGF-2 {ECO:0000250|UniProtKB:P09038};
DE Flags: Precursor;
GN Name=FGF2 {ECO:0000250|UniProtKB:P09038};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1] {ECO:0000312|EMBL:AAV74297.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
RA Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
RA Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
RT "Accelerated evolution of nervous system genes in the origin of Homo
RT sapiens.";
RL Cell 119:1027-1040(2004).
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-215 regulates FGF2 unconventional
CC secretion. {ECO:0000250}.
CC -!- MISCELLANEOUS: This protein binds heparin more strongly than does aFGF.
CC {ECO:0000250|UniProtKB:P09038}.
CC -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV74297.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
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DR EMBL; AY665259; AAV74297.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001103711.1; NM_001110241.1.
DR AlphaFoldDB; Q5IS69; -.
DR BMRB; Q5IS69; -.
DR SMR; Q5IS69; -.
DR STRING; 9598.ENSPTRP00000028196; -.
DR PaxDb; Q5IS69; -.
DR GeneID; 641462; -.
DR KEGG; ptr:641462; -.
DR CTD; 2247; -.
DR eggNOG; KOG3885; Eukaryota.
DR InParanoid; Q5IS69; -.
DR OrthoDB; 1157770at2759; -.
DR Proteomes; UP000002277; 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:0014843; P:growth factor dependent regulation of skeletal muscle satellite cell proliferation; ISS:AgBase.
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; Methylation; Mitogen; Nucleus;
KW Phosphoprotein; Reference proteome; Secreted; Ubl conjugation.
FT PROPEP 1..142
FT /evidence="ECO:0000250|UniProtKB:P09038"
FT /id="PRO_0000386593"
FT CHAIN 143..288
FT /note="Fibroblast growth factor 2"
FT /id="PRO_0000386594"
FT REGION 1..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..277
FT /note="Heparin-binding"
FT /evidence="ECO:0000250|UniProtKB:P05230"
FT MOTIF 179..181
FT /note="Cell attachment site; atypical"
FT /evidence="ECO:0000255"
FT MOTIF 221..223
FT /note="Cell attachment site; atypical"
FT /evidence="ECO:0000255"
FT COMPBIAS 65..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:P05230"
FT SITE 261
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P09038"
FT SITE 262
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P09038"
FT SITE 267
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P09038"
FT MOD_RES 108
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60487"
FT MOD_RES 108
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60487"
FT MOD_RES 110
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60487"
FT MOD_RES 110
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60487"
FT MOD_RES 112
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60487"
FT MOD_RES 112
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q60487"
FT MOD_RES 215
FT /note="Phosphotyrosine; by TEC"
FT /evidence="ECO:0000250|UniProtKB:P09038"
FT CROSSLNK 228
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P09038"
SQ SEQUENCE 288 AA; 30736 MW; 91FF2FDA20C46012 CRC64;
MVGVGGGDVE DVTPRPGGCQ ISGRGARGCN GIPGAAAWEA ALPRRRPRRH PSVNPRSRAA
GSPRTRGRRT KERPSGSRLG DHGRGRALPG GRVGGRGRGR APERVGGRGR GRGTAAPRAA
PAARGSRPGP AGTMAAGSIT TLPALPEDGG SGAFPPGHFK DPKRLYCKNG GFFLRIHPDG
RVDGVREKSD PHIKLQLQAE ERGVVSIKGV CANRYLAMKE DGRLLASKCV TDECFFFERL
ESNNYNTYRS RKYTSWYVAL KRTGQYKLGS KTGPGQKAIL FLPMSAKS
