FGFP3_MOUSE
ID FGFP3_MOUSE Reviewed; 245 AA.
AC Q1HCM0; Q7TNS6; Q8CDW7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Fibroblast growth factor-binding protein 3;
DE Short=FGF-BP3;
DE Short=FGF-binding protein 3;
DE Short=FGFBP-3;
DE Flags: Precursor;
GN Name=Fgfbp3;
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].
RA Swift M.R., Tassi E., Wellstein A.;
RT "Identification and characterization of a novel member of the fibroblast
RT growth factor-binding protein family, FGF-BP3.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-245.
RC STRAIN=C57BL/6J; TISSUE=Head;
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 INTERACTION WITH FGF2, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=20851768; DOI=10.1016/j.mcn.2010.09.003;
RA Yamanaka Y., Kitano A., Takao K., Prasansuklab A., Mushiroda T.,
RA Yamazaki K., Kumada T., Shibata M., Takaoka Y., Awaya T., Kato T., Abe T.,
RA Iwata N., Miyakawa T., Nakamura Y., Nakahata T., Heike T.;
RT "Inactivation of fibroblast growth factor binding protein 3 causes anxiety-
RT related behaviors.";
RL Mol. Cell. Neurosci. 46:200-212(2011).
CC -!- FUNCTION: Heparin-binding protein which binds to FGF2, prevents binding
CC of FGF2 to heparin and probably inhibits immobilization of FGF2 on
CC extracellular matrix glycosaminoglycans, allowing its release and
CC subsequent activation of FGFR signaling which leads to increased
CC vascular permeability. {ECO:0000250|UniProtKB:Q8TAT2}.
CC -!- SUBUNIT: Interacts with FGF2. {ECO:0000269|PubMed:20851768}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8TAT2}.
CC -!- TISSUE SPECIFICITY: In the adult, highly expressed in brain with lower
CC levels in ovary. In the embryo, highest levels are found in the brain
CC and spinal cord at 14 dpc and expression is almost completely
CC restricted to the brain by 18 dpc. In the adult and postnatal brain,
CC highly expressed in the orbitofrontal cortex where it is concentrated
CC primarily in differentiated neurons. {ECO:0000269|PubMed:20851768}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected at 10 dpc and reaches
CC a peak at birth. After birth, levels decrease and remain constant
CC throughout postnatal development. {ECO:0000269|PubMed:20851768}.
CC -!- DISRUPTION PHENOTYPE: Mutants display a range of anxiety-related
CC behaviors including reduced time spent in the central area of the open-
CC field arena, reduced activity in lit areas of a light/dark transition
CC test and prolonged latency to feeding in a novelty induced hypophagia
CC test which assesses the drive to drink a sweetened milk solution.
CC {ECO:0000269|PubMed:20851768}.
CC -!- SIMILARITY: Belongs to the fibroblast growth factor-binding protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABF56583.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ503577; ABF56583.1; ALT_INIT; mRNA.
DR EMBL; BC055778; AAH55778.1; -; mRNA.
DR EMBL; AK029452; BAC26455.1; -; mRNA.
DR RefSeq; NP_082539.2; NM_028263.1.
DR AlphaFoldDB; Q1HCM0; -.
DR STRING; 10090.ENSMUSP00000059682; -.
DR PhosphoSitePlus; Q1HCM0; -.
DR PaxDb; Q1HCM0; -.
DR PRIDE; Q1HCM0; -.
DR Antibodypedia; 52908; 85 antibodies from 22 providers.
DR DNASU; 72514; -.
DR Ensembl; ENSMUST00000057337; ENSMUSP00000059682; ENSMUSG00000047632.
DR GeneID; 72514; -.
DR KEGG; mmu:72514; -.
DR UCSC; uc008hhv.1; mouse.
DR CTD; 143282; -.
DR MGI; MGI:1919764; Fgfbp3.
DR VEuPathDB; HostDB:ENSMUSG00000047632; -.
DR eggNOG; ENOG502S2Z7; Eukaryota.
DR GeneTree; ENSGT00940000154372; -.
DR InParanoid; Q1HCM0; -.
DR OrthoDB; 1532497at2759; -.
DR PhylomeDB; Q1HCM0; -.
DR TreeFam; TF335877; -.
DR Reactome; R-MMU-190377; FGFR2b ligand binding and activation.
DR BioGRID-ORCS; 72514; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Fgfbp3; mouse.
DR PRO; PR:Q1HCM0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q1HCM0; protein.
DR Bgee; ENSMUSG00000047632; Expressed in cerebral cortex ventricular layer and 194 other tissues.
DR ExpressionAtlas; Q1HCM0; baseline and differential.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
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:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0030534; P:adult behavior; IMP:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0031646; P:positive regulation of nervous system process; IMP:UniProtKB.
DR GO; GO:0043117; P:positive regulation of vascular permeability; ISO:MGI.
DR InterPro; IPR010510; FGF1-bd.
DR PANTHER; PTHR15258; PTHR15258; 1.
DR Pfam; PF06473; FGF-BP1; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Growth factor binding; Heparin-binding; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..245
FT /note="Fibroblast growth factor-binding protein 3"
FT /id="PRO_0000322978"
FT REGION 33..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 60..81
FT /evidence="ECO:0000250"
FT DISULFID 91..125
FT /evidence="ECO:0000250"
FT DISULFID 228..236
FT /evidence="ECO:0000250"
SQ SEQUENCE 245 AA; 26217 MW; 0C09C4617F512F06 CRC64;
MSPPRPRASL SPLTLLLLLG GCLLSAAGRD KGAAGREVTR ASRPTVGSSG RFVSPEQHAC
SWQLLVPAPG TPTGGELALR CQTPGGASLH CAYRGHPERC AATGARRAHY WRRLLGALRR
RPRPCLDPAP LPPRLCARKT AGSDLHSPAH PSLPARPSEP PRSRARSPAR SRQSVRSPSS
QPEKKPLLVK SNSGGRKAGS DPVPEPPAAA GFQPNGLDQN AELTETYCTE KWHSLCNFFV
NFWNG
