FGFP1_BOVIN
ID FGFP1_BOVIN Reviewed; 234 AA.
AC Q9MZ06; Q0IID1;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Flags: Precursor;
GN Name=FGFBP1; Synonyms=FGFBP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-81; 88-135; 149-167 AND
RP 208-234, INTERACTION WITH FGF2, GLYCOSYLATION AT ASN-155 AND SER-172, AND
RP DISULFIDE BONDS.
RC TISSUE=Mammary gland;
RX PubMed=10867016; DOI=10.1074/jbc.m002550200;
RA Lametsch R., Rasmussen J.T., Johnsen L.B., Purup S., Sejrsen K.,
RA Petersen T.E., Heegaard C.W.;
RT "Structural characterization of the fibroblast growth factor-binding
RT protein purified from bovine prepartum mammary gland secretion.";
RL J. Biol. Chem. 275:19469-19474(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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, FGF7, FGF10, FGF22 and HSPG2 (By similarity). Interacts with
CC FGF2. {ECO:0000250, ECO:0000269|PubMed:10867016}.
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 -!- SIMILARITY: Belongs to the fibroblast growth factor-binding protein
CC family. {ECO:0000305}.
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DR EMBL; AF271896; AAF75792.1; -; mRNA.
DR EMBL; BC122703; AAI22704.1; -; mRNA.
DR RefSeq; NP_776762.1; NM_174337.2.
DR AlphaFoldDB; Q9MZ06; -.
DR SMR; Q9MZ06; -.
DR STRING; 9913.ENSBTAP00000042121; -.
DR iPTMnet; Q9MZ06; -.
DR PaxDb; Q9MZ06; -.
DR PeptideAtlas; Q9MZ06; -.
DR PRIDE; Q9MZ06; -.
DR Ensembl; ENSBTAT00000044642; ENSBTAP00000042121; ENSBTAG00000031497.
DR GeneID; 281812; -.
DR KEGG; bta:281812; -.
DR CTD; 9982; -.
DR VEuPathDB; HostDB:ENSBTAG00000031497; -.
DR eggNOG; ENOG502RZQ6; Eukaryota.
DR GeneTree; ENSGT00940000154372; -.
DR HOGENOM; CLU_102227_0_0_1; -.
DR InParanoid; Q9MZ06; -.
DR OMA; LKVECTR; -.
DR OrthoDB; 1046740at2759; -.
DR TreeFam; TF335877; -.
DR Reactome; R-BTA-190377; FGFR2b ligand binding and activation.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000031497; Expressed in rumen papilla and 45 other tissues.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IEA:Ensembl.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Growth factor binding; Membrane; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..234
FT /note="Fibroblast growth factor-binding protein 1"
FT /id="PRO_0000245511"
FT REGION 25..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..234
FT /note="Sufficient for interaction with FGF2 and FGF2-
FT induced effects"
FT /evidence="ECO:0000250"
FT COMPBIAS 175..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10867016"
FT CARBOHYD 172
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:10867016"
FT DISULFID 71..88
FT /evidence="ECO:0000269|PubMed:10867016"
FT DISULFID 97..130
FT /evidence="ECO:0000269|PubMed:10867016"
FT DISULFID 106..142
FT /evidence="ECO:0000269|PubMed:10867016"
FT DISULFID 198..234
FT /evidence="ECO:0000269|PubMed:10867016"
FT DISULFID 214..222
FT /evidence="ECO:0000269|PubMed:10867016"
SQ SEQUENCE 234 AA; 26188 MW; 48263C9790032921 CRC64;
MRTHGLTLLS LLLLAVPMLL VEAKKEGRNR RGSKASADES LALGKPGKEP RSQPTNYPIK
GKFVTPDHAD CRWAVTKQEE GIVLKVECTQ RDNTFSCFFT GNPTSCLELH KNNAYWKQIG
RNLRSQKVIC GDAKSVLKTR VCRKKFPESN LKLVNSTLIR IKKPSQELME PSPMDTVEVT
TSSSPEKTQT MATKDPQCEE EDLKNQRKAA LEYCGETWGS LCNFFLSMVQ GSSC
