FGF2_CAVPO
ID FGF2_CAVPO Reviewed; 170 AA.
AC Q60487;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 123.
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 AltName: Full=Prostatic growth factor;
DE Flags: Fragments;
GN Name=FGF2;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL PROTEIN SEQUENCE, AND ALTERNATIVE
RP INITIATION.
RX PubMed=2730645; DOI=10.1016/s0006-291x(89)80140-8;
RA Sommer A., Moscatelli D., Rifkin D.B.;
RT "An amino-terminally extended and post-translationally modified form of a
RT 25kD basic fibroblast growth factor.";
RL Biochem. Biophys. Res. Commun. 160:1267-1274(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 53-170.
RC TISSUE=Prostate;
RA Ricciardelli C.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PARTIAL PROTEIN SEQUENCE, AND METHYLATION AT ARG-4; ARG-6 AND ARG-8.
RX PubMed=1713785; DOI=10.1091/mbc.2.2.87;
RA Burgess W.H., Bizik J., Mehlman T., Quarto N., Rifkin D.B.;
RT "Direct evidence for methylation of arginine residues in high molecular
RT weight forms of basic fibroblast growth factor.";
RL Cell Regul. 2:87-93(1991).
RN [4]
RP CHARACTERIZATION.
RC TISSUE=Brain;
RX PubMed=3475702; DOI=10.1073/pnas.84.16.5778;
RA Moscatelli D., Joseph-Silverstein J., Manejias R., Rifkin D.B.;
RT "Mr 25,000 heparin-binding protein from guinea pig brain is a high
RT molecular weight form of basic fibroblast growth factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5778-5782(1987).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1; Synonyms=25 kDa;
CC IsoId=Q60487-1; Sequence=Displayed;
CC Name=2; Synonyms=18 kDa;
CC IsoId=Q60487-2; Sequence=VSP_018726;
CC -!- PTM: The N-terminus of isoform 2 is blocked. {ECO:0000305}.
CC -!- PTM: Phosphorylation at Tyr-97 regulates FGF2 unconventional secretion.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA85394.1; Type=Frameshift; Note=The correction of the frameshifts allows to extend the similarity to the human sequence and is based on partial amino-acid sequencing.; Evidence={ECO:0000305};
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DR EMBL; L75974; AAA85394.1; ALT_FRAME; mRNA.
DR AlphaFoldDB; Q60487; -.
DR SMR; Q60487; -.
DR STRING; 10141.ENSCPOP00000004847; -.
DR iPTMnet; Q60487; -.
DR PRIDE; Q60487; -.
DR eggNOG; KOG3885; Eukaryota.
DR InParanoid; Q60487; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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 1: Evidence at protein level;
KW Alternative initiation; Angiogenesis; Developmental protein;
KW Differentiation; Direct protein sequencing; Growth factor; Heparin-binding;
KW Isopeptide bond; Methylation; Mitogen; Nucleus; Phosphoprotein;
KW Reference proteome; Secreted; Ubl conjugation.
FT CHAIN <1..170
FT /note="Fibroblast growth factor 2"
FT /id="PRO_0000008930"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..159
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT SITE 143
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P09038"
FT SITE 144
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P09038"
FT SITE 149
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P09038"
FT MOD_RES 4
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:1713785"
FT MOD_RES 4
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:1713785"
FT MOD_RES 6
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:1713785"
FT MOD_RES 6
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:1713785"
FT MOD_RES 8
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:1713785"
FT MOD_RES 8
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:1713785"
FT MOD_RES 97
FT /note="Phosphotyrosine; by TEC"
FT /evidence="ECO:0000250|UniProtKB:P09038"
FT CROSSLNK 110
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P09038"
FT VAR_SEQ <1..21
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018726"
FT NON_CONS 15..16
FT /evidence="ECO:0000305"
FT NON_CONS 50..51
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 170 AA; 18354 MW; F36BDBC736E5FEBE CRC64;
VGGRGRGRGT AAAARREPGG AMAAGSITTL PALPEGGDGG AFAPGHFKDP NGGFFLRIHP
DGRVDGVREK TDPHIKLQLQ AEDRGVVSIK GVCANRYLAM KEDGRLLASK CVTDECFFFE
RLESNNYNTY RSRKYSSWYV ALKRTGQYKL GSKTGPGQKA ILFLPMSAKS
