FGFP1_MOUSE
ID FGFP1_MOUSE Reviewed; 251 AA.
AC O70514; Q62399;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FGF2, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=129;
RX PubMed=9178765; DOI=10.1038/sj.onc.1201117;
RA Kurtz A., Wang H.-L., Darwiche N., Harris V., Wellstein A.;
RT "Expression of a binding protein for FGF is associated with epithelial
RT development and skin carcinogenesis.";
RL Oncogene 14:2671-2681(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Keratinocyte;
RA Whitney R.G., Sato J.D.;
RT "Coding region for the murine homolog of human FGF binding protein HBp17.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=11819092; DOI=10.1007/s00418-001-0360-4;
RA Aigner A., Ray P.E., Czubayko F., Wellstein A.;
RT "Immunolocalization of an FGF-binding protein reveals a widespread
RT expression pattern during different stages of mouse embryo development.";
RL Histochem. Cell Biol. 117:1-11(2002).
RN [6]
RP 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).
CC -!- FUNCTION: Acts as a carrier protein that releases fibroblast-binding
CC factors (FGFs) from the extracellular matrix (EM) storage and thus
CC enhances 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:9178765}.
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 intestine, ovary, lung, placenta and
CC normal and wounded skin. {ECO:0000269|PubMed:15806171,
CC ECO:0000269|PubMed:9178765}.
CC -!- DEVELOPMENTAL STAGE: Expressed in digestive system, skin, hair
CC follicles, the dental germ, respiratory tract, various glandular
CC tissues, kidney, liver and certain areas of the central nervous system
CC between 8 and 16 dpc (at protein level). Expressed. in embryo between 9
CC to 18 dpc. Expressed at 14 dpc in the epithelial cells and 18 dpc in
CC basal epithelial cells of intestinal crypts. Expressed in mesenchymal
CC and epidermal structures of the body wall at 9 dpc. Expressed in basal
CC cells of the subepidermal layer of the skin at 12 dpc. Expressed in
CC hair follicles at 14 dpc. {ECO:0000269|PubMed:11819092,
CC ECO:0000269|PubMed:9178765}.
CC -!- MISCELLANEOUS: Expression is significantly up-regulated in skin
CC papillomas and carcinomas.
CC -!- SIMILARITY: Belongs to the fibroblast growth factor-binding protein
CC family. {ECO:0000305}.
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DR EMBL; U49641; AAB05227.1; -; mRNA.
DR EMBL; AF065441; AAC17439.1; -; mRNA.
DR EMBL; AK146625; BAE27314.1; -; mRNA.
DR EMBL; BC065774; AAH65774.1; -; mRNA.
DR CCDS; CCDS19268.1; -.
DR RefSeq; NP_001258545.1; NM_001271616.1.
DR RefSeq; NP_032035.2; NM_008009.4.
DR RefSeq; XP_006503774.1; XM_006503711.3.
DR RefSeq; XP_006503775.1; XM_006503712.3.
DR AlphaFoldDB; O70514; -.
DR SMR; O70514; -.
DR BioGRID; 199655; 4.
DR STRING; 10090.ENSMUSP00000056900; -.
DR GlyGen; O70514; 1 site.
DR PhosphoSitePlus; O70514; -.
DR PaxDb; O70514; -.
DR PRIDE; O70514; -.
DR ProteomicsDB; 272998; -.
DR Antibodypedia; 977; 255 antibodies from 26 providers.
DR DNASU; 14181; -.
DR Ensembl; ENSMUST00000061299; ENSMUSP00000056900; ENSMUSG00000048373.
DR Ensembl; ENSMUST00000199481; ENSMUSP00000143011; ENSMUSG00000048373.
DR Ensembl; ENSMUST00000199894; ENSMUSP00000142520; ENSMUSG00000048373.
DR GeneID; 14181; -.
DR KEGG; mmu:14181; -.
DR UCSC; uc008xid.3; mouse.
DR CTD; 9982; -.
DR MGI; MGI:1096350; Fgfbp1.
DR VEuPathDB; HostDB:ENSMUSG00000048373; -.
DR eggNOG; ENOG502RZQ6; Eukaryota.
DR GeneTree; ENSGT00940000154372; -.
DR InParanoid; O70514; -.
DR OMA; LKVECTR; -.
DR OrthoDB; 1046740at2759; -.
DR PhylomeDB; O70514; -.
DR TreeFam; TF335877; -.
DR Reactome; R-MMU-190377; FGFR2b ligand binding and activation.
DR BioGRID-ORCS; 14181; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Fgfbp1; mouse.
DR PRO; PR:O70514; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O70514; protein.
DR Bgee; ENSMUSG00000048373; Expressed in mammary bud and 154 other tissues.
DR Genevisible; O70514; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
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; IPI:UniProtKB.
DR GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; ISO:MGI.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IGI:MGI.
DR GO; GO:0051450; P:myoblast proliferation; IGI:MGI.
DR GO; GO:1903589; P:positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IGI:MGI.
DR GO; GO:2000288; P:positive regulation of myoblast proliferation; IGI:MGI.
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..251
FT /note="Fibroblast growth factor-binding protein 1"
FT /id="PRO_0000245513"
FT REGION 25..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..251
FT /note="Sufficient for interaction with FGF2 and FGF2-
FT induced effects"
FT /evidence="ECO:0000250"
FT COMPBIAS 46..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 175
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT DISULFID 74..91
FT /evidence="ECO:0000250"
FT DISULFID 100..133
FT /evidence="ECO:0000250"
FT DISULFID 109..145
FT /evidence="ECO:0000250"
FT DISULFID 214..251
FT /evidence="ECO:0000250"
FT DISULFID 231..239
FT /evidence="ECO:0000250"
FT CONFLICT 135
FT /note="N -> D (in Ref. 1; AAB05227)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="V -> I (in Ref. 1; AAB05227)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="A -> T (in Ref. 1; AAB05227)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 251 AA; 28294 MW; 3449252921A9E98C CRC64;
MRLHSLILLS FLLLATQAFS EKVRKRAKNA PHSTAEEGVE GSAPSLGKAQ NKQRSRTSKS
LTHGKFVTKD QATCRWAVTE EEQGISLKVQ CTQADQEFSC VFAGDPTDCL KHDKDQIYWK
QVARTLRKQK NICRNAKSVL KTRVCRKRFP ESNLKLVNPN ARGNTKPRKE KAEVSAREHN
KVQEAVSTEP NRVKEDITLN PAATQTMAIR DPECLEDPDV LNQRKTALEF CGESWSSICT
FFLNMLQATS C
