FGF1_DANRE
ID FGF1_DANRE Reviewed; 147 AA.
AC Q6PBT8; Q5TLE3;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Putative 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;
GN Name=fgf1; Synonyms=fgf-1; ORFNames=zgc:73249;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Itoh N.;
RT "Danio rerio fibroblast growth factor 1 (fgf1) mRNA.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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; AB194698; BAD69615.1; -; mRNA.
DR EMBL; BC059588; AAH59588.1; -; mRNA.
DR RefSeq; NP_957054.1; NM_200760.1.
DR AlphaFoldDB; Q6PBT8; -.
DR SMR; Q6PBT8; -.
DR STRING; 7955.ENSDARP00000008825; -.
DR PaxDb; Q6PBT8; -.
DR GeneID; 393733; -.
DR KEGG; dre:393733; -.
DR CTD; 393733; -.
DR ZFIN; ZDB-GENE-040426-1729; fgf1a.
DR eggNOG; KOG3885; Eukaryota.
DR InParanoid; Q6PBT8; -.
DR OrthoDB; 1157770at2759; -.
DR PhylomeDB; Q6PBT8; -.
DR TreeFam; TF317805; -.
DR Reactome; R-DRE-109704; PI3K Cascade.
DR Reactome; R-DRE-1257604; PIP3 activates AKT signaling.
DR Reactome; R-DRE-190322; FGFR4 ligand binding and activation.
DR Reactome; R-DRE-190370; FGFR1b ligand binding and activation.
DR Reactome; R-DRE-190371; FGFR3b ligand binding and activation.
DR Reactome; R-DRE-190372; FGFR3c ligand binding and activation.
DR Reactome; R-DRE-190373; FGFR1c ligand binding and activation.
DR Reactome; R-DRE-190375; FGFR2c ligand binding and activation.
DR Reactome; R-DRE-190377; FGFR2b ligand binding and activation.
DR Reactome; R-DRE-5654219; Phospholipase C-mediated cascade: FGFR1.
DR Reactome; R-DRE-5654221; Phospholipase C-mediated cascade, FGFR2.
DR Reactome; R-DRE-5654227; Phospholipase C-mediated cascade, FGFR3.
DR Reactome; R-DRE-5654228; Phospholipase C-mediated cascade, FGFR4.
DR Reactome; R-DRE-5654687; Downstream signaling of activated FGFR1.
DR Reactome; R-DRE-5654688; SHC-mediated cascade:FGFR1.
DR Reactome; R-DRE-5654689; PI-3K cascade:FGFR1.
DR Reactome; R-DRE-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-DRE-5654695; PI-3K cascade:FGFR2.
DR Reactome; R-DRE-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-DRE-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-DRE-5654704; SHC-mediated cascade:FGFR3.
DR Reactome; R-DRE-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-DRE-5654710; PI-3K cascade:FGFR3.
DR Reactome; R-DRE-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-DRE-5654719; SHC-mediated cascade:FGFR4.
DR Reactome; R-DRE-5654720; PI-3K cascade:FGFR4.
DR Reactome; R-DRE-5654726; Negative regulation of FGFR1 signaling.
DR Reactome; R-DRE-5654727; Negative regulation of FGFR2 signaling.
DR Reactome; R-DRE-5654732; Negative regulation of FGFR3 signaling.
DR Reactome; R-DRE-5654733; Negative regulation of FGFR4 signaling.
DR Reactome; R-DRE-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DRE-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR PRO; PR:Q6PBT8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
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:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0060681; P:branch elongation involved in ureteric bud branching; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; IMP:ZFIN.
DR GO; GO:0030324; P:lung development; IBA:GO_Central.
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:0010595; P:positive regulation of endothelial cell migration; IBA:GO_Central.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IBA:GO_Central.
DR GO; GO:0010628; P:positive regulation of gene expression; IBA:GO_Central.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IBA:GO_Central.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IBA:GO_Central.
DR GO; GO:0042060; P:wound healing; IBA:GO_Central.
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.
PE 2: Evidence at transcript level;
KW Angiogenesis; Cytoplasm; Developmental protein; Differentiation;
KW Growth factor; Heparin-binding; Mitogen; Nucleus; Reference proteome;
KW Secreted.
FT CHAIN 1..147
FT /note="Putative fibroblast growth factor 1"
FT /id="PRO_0000147598"
FT REGION 117..133
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT CONFLICT 108
FT /note="Y -> H (in Ref. 1; BAD69615)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16638 MW; D154A580D95A7326 CRC64;
MTEADIAVKS SPRDYKKLTR LYCMNGGFHL QILADGTVAG AADENTYSIL RIKATSPGVV
VIEGSETGLY LSMNEHGKLY ASSLVTDESY FLEKMEENHY NTYQSQKYGE NWYVGIKKNG
KMKRGPRTHI GQKAIFFLPR QVEQEED
