ID   FGFP1_RAT               Reviewed;         238 AA.
AC   Q9QY10;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Fibroblast growth factor-binding protein 1;
DE            Short=FGF-BP;
DE            Short=FGF-BP1;
DE            Short=FGF-binding protein 1;
DE            Short=FGFBP-1;
DE            Short=Growth factor-binding protein 1;
DE   Flags: Precursor;
GN   Name=Fgfbp1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=Sprague-Dawley; TISSUE=Skin;
RX   PubMed=10831072; DOI=10.3109/08977190009003233;
RA   Aigner A., Malerczyk C., Houghtling R., Wellstein A.;
RT   "Tissue distribution and retinoid-mediated downregulation of an FGF-binding
RT   protein (FGF-BP) in the rat.";
RL   Growth Factors 18:51-62(2000).
CC   -!- FUNCTION: Acts as a carrier protein that release fibroblast-binding
CC       factors (FGFs) from the extracellular matrix (EM) storage and thus
CC       enhance the mitogenic activity of FGFs. Enhances FGF2 signaling during
CC       tissue repair, angiogenesis and in tumor growth (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Found in a complex with FGFBP1, FGF1 and FGF2. Interacts with
CC       FGF1, FGF2, FGF7, FGF10, FGF22 and HSPG2 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000250|UniProtKB:Q14512}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q14512}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q14512}. Note=Extracellular and plasma membrane-
CC       associated. {ECO:0000250|UniProtKB:Q14512}.
CC   -!- TISSUE SPECIFICITY: Expressed in gut, eye, thymus, skin, lung, tongue,
CC       Purkinje cells and cerebral chorioid plexus (at protein level).
CC       {ECO:0000269|PubMed:10831072}.
CC   -!- INDUCTION: Down-regulated by retinoids. {ECO:0000269|PubMed:10831072}.
CC   -!- SIMILARITY: Belongs to the fibroblast growth factor-binding protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF142758; AAF23079.1; -; mRNA.
DR   RefSeq; NP_072125.1; NM_022603.1.
DR   AlphaFoldDB; Q9QY10; -.
DR   SMR; Q9QY10; -.
DR   STRING; 10116.ENSRNOP00000004128; -.
DR   GlyGen; Q9QY10; 1 site.
DR   PaxDb; Q9QY10; -.
DR   PRIDE; Q9QY10; -.
DR   GeneID; 64535; -.
DR   KEGG; rno:64535; -.
DR   CTD; 9982; -.
DR   RGD; 621211; Fgfbp1.
DR   eggNOG; ENOG502RZQ6; Eukaryota.
DR   InParanoid; Q9QY10; -.
DR   OrthoDB; 1046740at2759; -.
DR   PhylomeDB; Q9QY10; -.
DR   Reactome; R-RNO-190377; FGFR2b ligand binding and activation.
DR   PRO; PR:Q9QY10; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0005576; C:extracellular region; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017134; F:fibroblast growth factor binding; ISO:RGD.
DR   GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
DR   GO; GO:0007267; P:cell-cell signaling; IDA:RGD.
DR   GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISO:RGD.
DR   GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISO:RGD.
DR   InterPro; IPR010510; FGF1-bd.
DR   PANTHER; PTHR15258; PTHR15258; 1.
DR   Pfam; PF06473; FGF-BP1; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Growth factor binding;
KW   Membrane; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..238
FT                   /note="Fibroblast growth factor-binding protein 1"
FT                   /id="PRO_0000245514"
FT   REGION          25..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..238
FT                   /note="Sufficient for interaction with FGF2 and FGF2-
FT                   induced effects"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        33..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        164
FT                   /note="O-linked (GalNAc...) serine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..88
FT                   /evidence="ECO:0000250"
FT   DISULFID        97..130
FT                   /evidence="ECO:0000250"
FT   DISULFID        106..142
FT                   /evidence="ECO:0000250"
FT   DISULFID        201..238
FT                   /evidence="ECO:0000250"
FT   DISULFID        218..226
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   238 AA;  26887 MW;  DF18D3720FA536CE CRC64;
     MRIHGLILLS FLLLAAQVLS EKVRKTAKNV PDSTTEEDMS PSLGKARNKQ RSRTSKSMTH
     GRFVTKDQAT CRWAVTEEEL GINLKVQCTR ADQEFSCVFA GDPTGCLKYD KDQTYWKQVA
     RTLRKQKNIC ENSKSVLKTR VCRKKFPESN LKVVNPRKEK AEVSPREHNK VQEAVSMEPN
     KVKVDITTSP AATVAVKDSE CLEDPDVLTQ RKTALEFCGE SWSSFCTFFL NMLQATSC