FGF1_CYNPY
ID FGF1_CYNPY Reviewed; 148 AA.
AC Q6I6M7;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
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: Precursor; Fragment;
GN Name=fgf1; Synonyms=fgf-1;
OS Cynops pyrrhogaster (Japanese fire-bellied newt) (Molge pyrrhogaster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae; Cynops.
OX NCBI_TaxID=8330;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15172683; DOI=10.1016/j.mod.2004.04.010;
RA Hayashi T., Mizuno N., Ueda Y., Okamoto M., Kondoh H.;
RT "FGF2 triggers iris-derived lens regeneration in newt eye.";
RL Mech. Dev. 121:519-526(2004).
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 EMBL; AB175665; BAD24666.1; -; mRNA.
DR AlphaFoldDB; Q6I6M7; -.
DR SMR; Q6I6M7; -.
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 2: Evidence at transcript level;
KW Angiogenesis; Cytoplasm; Developmental protein; Differentiation;
KW Growth factor; Heparin-binding; Mitogen; Nucleus; Secreted.
FT PROPEP <1..11
FT /evidence="ECO:0000250"
FT /id="PRO_0000008923"
FT CHAIN 12..>148
FT /note="Fibroblast growth factor 1"
FT /id="PRO_0000008924"
FT REGION 123..139
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 148
SQ SEQUENCE 148 AA; 16946 MW; C74C2200FCA37AD8 CRC64;
EITTFAALTE RFNLPNGNYQ RPKLLYCSNG GHFLRILPDG KVDGTRDRSD PYIQLQFYAE
SVGEVYIKSL ETGQYLAMDS DGRLYASQSP SEECLFLERL EENHYNTYKS KMHADKDWFV
GIKKNGKTKL GSRTHFGQKA ILFLPLPV
