FGF1_NOTVI
ID FGF1_NOTVI Reviewed; 132 AA.
AC Q7SIF8;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Fibroblast growth factor 1;
DE Short=FGF-1;
DE AltName: Full=Acidic fibroblast growth factor;
DE Short=aFGF;
DE AltName: Full=Heparin-binding growth factor 1;
DE Short=HBGF-1;
DE Flags: Fragment;
GN Name=fgf1; Synonyms=fgf-1;
OS Notophthalmus viridescens (Eastern newt) (Triturus viridescens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae;
OC Notophthalmus.
OX NCBI_TaxID=8316;
RN [1]
RP STRUCTURE BY NMR IN COMPLEX WITH SUBSTRATE ANALOG.
RX PubMed=12205097; DOI=10.1074/jbc.m207814200;
RA Arunkumar A.I., Srisailam S., Kumar T.K., Kathir K.M., Chi Y.H., Wang H.M.,
RA Chang G.G., Chiu I., Yu C.;
RT "Structure and stability of an acidic fibroblast growth factor from
RT Notophthalmus viridescens.";
RL J. Biol. Chem. 277:46424-46432(2002).
CC -!- FUNCTION: Plays an important role in the regulation of cell survival,
CC cell division, angiogenesis, cell differentiation and cell migration.
CC Functions as potent mitogen in vitro. Acts as a ligand for FGFR1 and
CC integrins. Binds to FGFR1 in the presence of heparin leading to FGFR1
CC dimerization and activation via sequential autophosphorylation on
CC tyrosine residues which act as docking sites for interacting proteins,
CC leading to the activation of several signaling cascades. Binds to
CC integrins. Its binding to integrins and subsequent ternary complex
CC formation with integrins and FGFR1 are essential for FGF1 signaling.
CC {ECO:0000250|UniProtKB:P05230}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}.
CC Nucleus {ECO:0000250}. Note=Lacks a cleavable signal sequence. Within
CC the cytoplasm, it is transported to the cell membrane and then secreted
CC by a non-classical pathway that requires Cu(2+) ions and S100A13 (By
CC similarity). Binding of exogenous FGF1 to FGFR facilitates endocytosis
CC followed by translocation of FGF1 across endosomal membrane into the
CC cytosol. Nuclear import from the cytosol requires the classical nuclear
CC import machinery (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC {ECO:0000305}.
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DR PDB; 1FMM; NMR; -; S=1-132.
DR PDBsum; 1FMM; -.
DR AlphaFoldDB; Q7SIF8; -.
DR BMRB; Q7SIF8; -.
DR SMR; Q7SIF8; -.
DR EvolutionaryTrace; Q7SIF8; -.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005104; F:fibroblast growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0044548; F:S100 protein binding; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0060681; P:branch elongation involved in ureteric bud branching; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0072163; P:mesonephric epithelium development; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; ISS:UniProtKB.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR CDD; cd00058; FGF; 1.
DR InterPro; IPR028210; FGF1.
DR InterPro; IPR002209; Fibroblast_GF_fam.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR11486; PTHR11486; 1.
DR PANTHER; PTHR11486:SF86; PTHR11486:SF86; 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 3D-structure; Angiogenesis; Cytoplasm; Developmental protein;
KW Differentiation; Growth factor; Heparin-binding; Mitogen; Nucleus;
KW Secreted.
FT CHAIN <1..132
FT /note="Fibroblast growth factor 1"
FT /id="PRO_0000147599"
FT BINDING 10
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT BINDING 108..120
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT NON_TER 1
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:1FMM"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:1FMM"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:1FMM"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1FMM"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:1FMM"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:1FMM"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1FMM"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:1FMM"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:1FMM"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1FMM"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:1FMM"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:1FMM"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1FMM"
SQ SEQUENCE 132 AA; 15015 MW; 76CABAF337B29C7B CRC64;
QKPKLLYCSN GGYFLRIFPD GKVDGTRDRS DPYIQLQFYA ESVGEVYIKS LETGQYLAMD
SDGQLYASQS PSEECLFLER LEENNYNTYK SKVHADKDWF VGIKKNGKTK PGSRTHFGQK
AILFLPLPVS SD
