ID   FGFP1_HUMAN             Reviewed;         234 AA.
AC   Q14512;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   07-JUL-2009, entry version 64.
DE   RecName: Full=Fibroblast growth factor-binding protein 1;
DE            Short=FGF-binding protein 1;
DE            Short=FGF-BP1;
DE            Short=FGFBP-1;
DE            Short=FGF-BP;
DE   AltName: Full=17 kDa heparin-binding growth factor-binding protein;
DE            Short=17 kDa HBGF-binding protein;
DE   AltName: Full=HBp17;
DE   Flags: Precursor;
GN   Name=FGFBP1; Synonyms=FGFBP, HBP17;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEIN SEQUENCE OF 34-67;
RP   92-118 AND 146-158, IDENTIFICATION IN A COMPLEX WITH FGF1 AND FGF2,
RP   INTERACTION WITH FGF1, AND TISSUE SPECIFICITY.
RC   TISSUE=Epidermal carcinoma;
RX   MEDLINE=91358475; PubMed=1885605;
RA   Wu D.Q., Kan M.K., Sato G.H., Okamoto T., Sato J.D.;
RT   "Characterization and molecular cloning of a putative binding protein
RT   for heparin-binding growth factors.";
RL   J. Biol. Chem. 266:16778-16785(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Shi S., Sato J.D.;
RT   "Gene sequence for the human FGF-binding protein HBp17.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary, and Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION.
RX   PubMed=9334727; DOI=10.1038/nm1097-1137;
RA   Czubayko F., Liaudet-Coopman E.D., Aigner A., Tuveson A.T.,
RA   Berchem G.J., Wellstein A.;
RT   "A secreted FGF-binding protein can serve as the angiogenic switch in
RT   human cancer.";
RL   Nat. Med. 3:1137-1140(1997).
RN   [5]
RP   INTERACTION WITH HSPG2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=11148217; DOI=10.1074/jbc.M011493200;
RA   Mongiat M., Otto J., Oldershaw R., Ferrer F., Sato J.D., Iozzo R.V.;
RT   "Fibroblast growth factor-binding protein is a novel partner for
RT   perlecan protein core.";
RL   J. Biol. Chem. 276:10263-10271(2001).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH FGF2.
RX   PubMed=11509569; DOI=10.1074/jbc.M104933200;
RA   Tassi E., Al-Attar A., Aigner A., Swift M.R., McDonnell K.,
RA   Karavanov A., Wellstein A.;
RT   "Enhancement of fibroblast growth factor (FGF) activity by an FGF-
RT   binding protein.";
RL   J. Biol. Chem. 276:40247-40253(2001).
RN   [7]
RP   FUNCTION, INTERACTION WITH FGF7; FGF10 AND FGF22, INDUCTION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15806171; DOI=10.1038/sj.onc.1208560;
RA   Beer H.-D., Bittner M., Niklaus G., Munding C., Max N., Goppelt A.,
RA   Werner S.;
RT   "The fibroblast growth factor binding protein is a novel interaction
RT   partner of FGF-7, FGF-10 and FGF-22 and regulates FGF activity:
RT   implications for epithelial repair.";
RL   Oncogene 24:5269-5277(2005).
RN   [8]
RP   INTERACTION WITH FGF2, AND MUTAGENESIS OF CYS-214.
RX   PubMed=16257968; DOI=10.1074/jbc.M510754200;
RA   Xie B., Tassi E., Swift M.R., McDonnell K., Bowden E.T., Wang S.,
RA   Ueda Y., Tomita Y., Riegel A.T., Wellstein A.;
RT   "Identification of the fibroblast growth factor (FGF)-interacting
RT   domain in a secreted FGF-binding protein by phage display.";
RL   J. Biol. Chem. 281:1137-1144(2006).
CC   -!- FUNCTION: Acts as a carrier protein that release fibroblast-
CC       binding factors (FGFs) from the extracellular matrix (EM) storage
CC       and thus enhance the mitogenic activity of FGFs. Enhances FGF2
CC       signaling during tissue repair, angiogenesis and in tumor growth.
CC   -!- SUBUNIT: Found in a complex with FGFBP1, FGF1 and FGF2. Interacts
CC       with FGF1, FGF2, FGF7, FGF10, FGF22 and HSPG2.
CC   -!- INTERACTION:
CC       P09038:FGF2; NbExp=3; IntAct=EBI-953742, EBI-977447;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space. Cell
CC       membrane; Peripheral membrane protein. Note=Extracellular and
CC       plasma membrane-associated. Colocalizes with HSPG2 in the
CC       pericellular environment of squamous cell carcinomas.
CC   -!- TISSUE SPECIFICITY: Expressed in the suprabasal region of the
CC       epidermis, in hair follicles, the basement membrane at the dermo-
CC       epidermal junction (occasionally extending into the basement
CC       membrane of dermal blood vessels), wounded skin and several
CC       invasive squamous cell carcinomas (at protein level). Expressed in
CC       normal and wounded skin and various squamous cell carcinomas.
CC   -!- INDUCTION: Up-regulated in epithelial cells after skin injury.
CC       Keratinocyte mitogens.
CC   -!- MISCELLANEOUS: Expression is significantly up-regulated in
CC       carcinogen-induced skin tumors, various squamous cell carcinomas,
CC       some colon cancer cell lines and tumors.
CC   -!- SIMILARITY: Belongs to the fibroblast growth factor-binding
CC       protein family.
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DR   EMBL; M60047; AAA58636.1; -; mRNA.
DR   EMBL; AF149412; AAD39216.1; -; Genomic_DNA.
DR   EMBL; BC003628; AAH03628.1; -; mRNA.
DR   EMBL; BC008910; AAH08910.1; -; mRNA.
DR   IPI; IPI00021399; -.
DR   PIR; A41178; A41178.
DR   RefSeq; NP_005121.1; -.
DR   UniGene; Hs.1690; -.
DR   IntAct; Q14512; 2.
DR   PhosphoSite; Q14512; -.
DR   PRIDE; Q14512; -.
DR   Ensembl; ENSG00000137440; Homo sapiens.
DR   GeneID; 9982; -.
DR   KEGG; hsa:9982; -.
DR   UCSC; uc003gom.1; human.
DR   GeneCards; GC04M015546; -.
DR   H-InvDB; HIX0004114; -.
DR   HGNC; HGNC:19695; FGFBP1.
DR   HPA; HPA004332; -.
DR   MIM; 607737; gene.
DR   PharmGKB; PA134880558; -.
DR   HOGENOM; Q14512; -.
DR   HOVERGEN; Q14512; -.
DR   OMA; Q14512; KTRVCRK.
DR   NextBio; 37692; -.
DR   ArrayExpress; Q14512; -.
DR   Bgee; Q14512; -.
DR   CleanEx; HS_FGFBP1; -.
DR   GermOnline; ENSG00000137440; Homo sapiens.
DR   GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; TAS:ProtInc.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
DR   GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR   InterPro; IPR010510; FGF1_bd.
DR   PANTHER; PTHR15258; FGF1_bd; 1.
DR   Pfam; PF06473; FGF-BP1; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Growth factor binding; Membrane;
KW   Secreted; Signal.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24    234       Fibroblast growth factor-binding protein
FT                                1.
FT                                /FTId=PRO_0000245512.
FT   REGION      193    234       Sufficient for interaction with FGF2 and
FT                                FGF2-induced effects.
FT   CARBOHYD    169    169       O-linked (GalNAc...) (By similarity).
FT   DISULFID     68     85       By similarity.
FT   DISULFID     94    127       By similarity.
FT   DISULFID    103    139       By similarity.
FT   DISULFID    197    234       By similarity.
FT   DISULFID    214    222       By similarity.
FT   MUTAGEN     214    214       C->A: Strongly reduces interaction with
FT                                FGF2.
SQ   SEQUENCE   234 AA;  26264 MW;  AAF4209F29F2D058 CRC64;
     MKICSLTLLS FLLLAAQVLL VEGKKKVKNG LHSKVVSEQK DTLGNTQIKQ KSRPGNKGKF
     VTKDQANCRW AATEQEEGIS LKVECTQLDH EFSCVFAGNP TSCLKLKDER VYWKQVARNL
     RSQKDICRYS KTAVKTRVCR KDFPESSLKL VSSTLFGNTK PRKEKTEMSP REHIKGKETT
     PSSLAVTQTM ATKAPECVED PDMANQRKTA LEFCGETWSS LCTFFLSIVQ DTSC
//