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Folate receptor alpha (FR-alpha) (Folate receptor 1) (Folate-binding protein 1)

 FOLR1_MOUSE             Reviewed;         255 AA.
P35846; Q9R222;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
11-DEC-2013, sequence version 2.
25-OCT-2017, entry version 119.
RecName: Full=Folate receptor alpha;
Short=FR-alpha;
AltName: Full=Folate receptor 1;
AltName: Full=Folate-binding protein 1;
Flags: Precursor;
Name=Folr1; Synonyms=Fbp1, Folbp1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=1894617;
Brigle K.E., Westin E.H., Houghton M.T., Goldman I.D.;
"Characterization of two cDNAs encoding folate-binding proteins from
L1210 murine leukemia cells. Increased expression associated with a
genomic rearrangement.";
J. Biol. Chem. 266:17243-17249(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
PubMed=10216260; DOI=10.1016/S0378-1119(99)00081-5;
Bolton J.A., Wood S.A., Kennedy D., Don R.H., Mattick J.S.;
"Retinoic acid-dependent upregulation of mouse folate receptor-alpha
expression in embryonic stem cells, and conservation of alternative
splicing patterns.";
Gene 230:215-224(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
PubMed=1429588;
Brigle K.E., Westin E.H., Houghton M.T., Goldman I.D.;
"Insertion of an intracisternal A particle within the 5'-regulatory
region of a gene encoding folate-binding protein in L1210 leukemia
cells in response to low folate selection. Association with increased
protein expression.";
J. Biol. Chem. 267:22351-22355(1992).
[7]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=10508523; DOI=10.1038/13861;
Piedrahita J.A., Oetama B., Bennett G.D., van Waes J., Kamen B.A.,
Richardson J., Lacey S.W., Anderson R.G., Finnell R.H.;
"Mice lacking the folic acid-binding protein Folbp1 are defective in
early embryonic development.";
Nat. Genet. 23:228-232(1999).
[8]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=12854656; DOI=10.1002/bdra.10045;
Tang L.S., Finnell R.H.;
"Neural and orofacial defects in Folp1 knockout mice.";
Birth Defects Res. A Clin. Mol. Teratol. 67:209-218(2003).
[9]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=15259034; DOI=10.1002/bdra.20043;
Tang L.S., Wlodarczyk B.J., Santillano D.R., Miranda R.C.,
Finnell R.H.;
"Developmental consequences of abnormal folate transport during murine
heart morphogenesis.";
Birth Defects Res. A Clin. Mol. Teratol. 70:449-458(2004).
[10]
DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=15703271; DOI=10.1681/ASN.2004080711;
Birn H., Spiegelstein O., Christensen E.I., Finnell R.H.;
"Renal tubular reabsorption of folate mediated by folate binding
protein 1.";
J. Am. Soc. Nephrol. 16:608-615(2005).
[11]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=17286298; DOI=10.1002/bdra.20347;
Zhu H., Wlodarczyk B.J., Scott M., Yu W., Merriweather M.,
Gelineau-van Waes J., Schwartz R.J., Finnell R.H.;
"Cardiovascular abnormalities in Folr1 knockout mice and folate
rescue.";
Birth Defects Res. A Clin. Mol. Teratol. 79:257-268(2007).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Binds to folate and reduced folic acid derivatives and
mediates delivery of 5-methyltetrahydrofolate and folate analogs
into the interior of cells. Has high affinity for folate and folic
acid analogs at neutral pH. Exposure to slightly acidic pH after
receptor endocytosis triggers a conformation change that strongly
reduces its affinity for folates and mediates their release.
Required for normal embryonic development and normal cell
proliferation. Required for renal folate reabsorption.
{ECO:0000269|PubMed:10508523, ECO:0000269|PubMed:12854656,
ECO:0000269|PubMed:15259034, ECO:0000269|PubMed:15703271,
ECO:0000269|PubMed:17286298, ECO:0000269|PubMed:1894617}.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
Secreted {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}.
Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}.
Endosome {ECO:0000250}. Apical cell membrane. Note=Endocytosed
into cytoplasmic vesicles and then recycled to the cell membrane
(By similarity). Detected at proximal tubule apical membranes.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in kidney proximal tubules (at
protein level). {ECO:0000269|PubMed:15703271}.
-!- PTM: The secreted form is derived from the membrane-bound form
either by cleavage of the GPI anchor, or/and by proteolysis
catalyzed by a metalloprotease. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality at about 10.5 dpc, due
to gross developmental defects, including defects of neural tube
closure, craniofacial defects and defects in heart development.
Embryos can be rescued by maternal folate supplementation.
{ECO:0000269|PubMed:10508523, ECO:0000269|PubMed:12854656,
ECO:0000269|PubMed:15259034, ECO:0000269|PubMed:15703271,
ECO:0000269|PubMed:17286298}.
-!- SIMILARITY: Belongs to the folate receptor family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M64782; AAA37595.1; -; mRNA.
EMBL; AF096319; AAD19353.1; -; mRNA.
EMBL; AC167240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466531; EDL16530.1; -; Genomic_DNA.
EMBL; CH466531; EDL16532.1; -; Genomic_DNA.
EMBL; CH466531; EDL16533.1; -; Genomic_DNA.
EMBL; CH466531; EDL16534.1; -; Genomic_DNA.
EMBL; CH466531; EDL16535.1; -; Genomic_DNA.
EMBL; CH466531; EDL16536.1; -; Genomic_DNA.
EMBL; CH466531; EDL16537.1; -; Genomic_DNA.
EMBL; CH466531; EDL16538.1; -; Genomic_DNA.
EMBL; BC138781; AAI38782.1; -; mRNA.
EMBL; BC138795; AAI38796.1; -; mRNA.
EMBL; BC145414; AAI45415.1; -; mRNA.
EMBL; M97700; AAA37596.1; -; Genomic_DNA.
EMBL; M97701; AAA37598.1; -; Genomic_DNA.
CCDS; CCDS21517.1; -.
PIR; A40969; A40969.
RefSeq; NP_001239481.1; NM_001252552.1.
RefSeq; NP_001239482.1; NM_001252553.1.
RefSeq; NP_001239483.1; NM_001252554.1.
RefSeq; NP_032060.2; NM_008034.3.
RefSeq; XP_006507423.1; XM_006507360.3.
RefSeq; XP_006507424.1; XM_006507361.2.
RefSeq; XP_006507426.1; XM_006507363.3.
RefSeq; XP_006507427.1; XM_006507364.2.
RefSeq; XP_006507428.1; XM_006507365.3.
RefSeq; XP_006507429.1; XM_006507366.2.
RefSeq; XP_006507430.1; XM_006507367.3.
RefSeq; XP_006507431.1; XM_006507368.3.
RefSeq; XP_006507432.1; XM_006507369.3.
RefSeq; XP_006507433.1; XM_006507370.3.
UniGene; Mm.2135; -.
UniGene; Mm.490265; -.
ProteinModelPortal; P35846; -.
SMR; P35846; -.
IntAct; P35846; 1.
MINT; MINT-4130923; -.
STRING; 10090.ENSMUSP00000001882; -.
PaxDb; P35846; -.
PeptideAtlas; P35846; -.
PRIDE; P35846; -.
Ensembl; ENSMUST00000106981; ENSMUSP00000102594; ENSMUSG00000001827.
Ensembl; ENSMUST00000106982; ENSMUSP00000102595; ENSMUSG00000001827.
Ensembl; ENSMUST00000106983; ENSMUSP00000102596; ENSMUSG00000001827.
Ensembl; ENSMUST00000106985; ENSMUSP00000102598; ENSMUSG00000001827.
Ensembl; ENSMUST00000106986; ENSMUSP00000102599; ENSMUSG00000001827.
GeneID; 14275; -.
KEGG; mmu:14275; -.
UCSC; uc009ipm.1; mouse.
CTD; 2348; -.
MGI; MGI:95568; Folr1.
eggNOG; ENOG410IFFP; Eukaryota.
eggNOG; ENOG4111IU4; LUCA.
GeneTree; ENSGT00390000010470; -.
HOGENOM; HOG000006539; -.
HOVERGEN; HBG039612; -.
InParanoid; P35846; -.
KO; K13649; -.
OMA; WNWTSGF; -.
OrthoDB; EOG091G0GIA; -.
TreeFam; TF328532; -.
Reactome; R-MMU-204005; COPII (Coat Protein 2) Mediated Vesicle Transport.
Reactome; R-MMU-5694530; Cargo concentration in the ER.
Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
PRO; PR:P35846; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000001827; -.
CleanEx; MM_FBP1; -.
CleanEx; MM_FOLR1; -.
ExpressionAtlas; P35846; baseline and differential.
Genevisible; P35846; MM.
GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016020; C:membrane; TAS:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0008144; F:drug binding; ISO:MGI.
GO; GO:0005542; F:folic acid binding; ISS:UniProtKB.
GO; GO:0008517; F:folic acid transporter activity; ISS:UniProtKB.
GO; GO:0051870; F:methotrexate binding; ISO:MGI.
GO; GO:0004872; F:receptor activity; TAS:MGI.
GO; GO:0061713; P:anterior neural tube closure; IMP:BHF-UCL.
GO; GO:0031103; P:axon regeneration; IMP:BHF-UCL.
GO; GO:0003253; P:cardiac neural crest cell migration involved in outflow tract morphogenesis; IMP:BHF-UCL.
GO; GO:0071231; P:cellular response to folic acid; ISO:MGI.
GO; GO:0046655; P:folic acid metabolic process; IMP:MGI.
GO; GO:0015884; P:folic acid transport; ISS:UniProtKB.
GO; GO:0001947; P:heart looping; IMP:BHF-UCL.
GO; GO:0003147; P:neural crest cell migration involved in heart formation; IMP:BHF-UCL.
GO; GO:0061626; P:pharyngeal arch artery morphogenesis; IMP:BHF-UCL.
GO; GO:0006620; P:posttranslational protein targeting to endoplasmic reticulum membrane; TAS:MGI.
GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0048678; P:response to axon injury; IMP:BHF-UCL.
InterPro; IPR004269; Folate_rcpt.
InterPro; IPR018143; Folate_rcpt-like.
InterPro; IPR032935; FOLR1.
PANTHER; PTHR10517; PTHR10517; 1.
PANTHER; PTHR10517:SF15; PTHR10517:SF15; 1.
Pfam; PF03024; Folate_rec; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasmic vesicle; Disulfide bond;
Endosome; Folate-binding; Glycoprotein; GPI-anchor; Lipoprotein;
Membrane; Receptor; Reference proteome; Secreted; Signal; Transport.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 232 Folate receptor alpha.
/FTId=PRO_0000008804.
PROPEP 233 255 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000008805.
REGION 122 126 Folate binding.
{ECO:0000250|UniProtKB:P15328}.
REGION 155 160 Folate binding.
{ECO:0000250|UniProtKB:P15328}.
BINDING 101 101 Folate. {ECO:0000250|UniProtKB:P15328}.
BINDING 105 105 Folate. {ECO:0000250|UniProtKB:P15328}.
BINDING 194 194 Folate. {ECO:0000250|UniProtKB:P15328}.
LIPID 232 232 GPI-anchor amidated serine.
{ECO:0000250|UniProtKB:P15328}.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 159 159 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 35 63 {ECO:0000250|UniProtKB:P15328}.
DISULFID 55 103 {ECO:0000250|UniProtKB:P15328}.
DISULFID 64 107 {ECO:0000250|UniProtKB:P15328}.
DISULFID 87 173 {ECO:0000250|UniProtKB:P15328}.
DISULFID 94 144 {ECO:0000250|UniProtKB:P15328}.
DISULFID 133 207 {ECO:0000250|UniProtKB:P15328}.
DISULFID 137 187 {ECO:0000250|UniProtKB:P15328}.
DISULFID 150 167 {ECO:0000250|UniProtKB:P15328}.
CONFLICT 236 236 F -> L (in Ref. 1; AAA37595).
{ECO:0000305}.
SEQUENCE 255 AA; 29449 MW; A12ACA978BC8E134 CRC64;
MAHLMTVQLL LLVMWMAECA QSRATRARTE LLNVCMDAKH HKEKPGPEDN LHDQCSPWKT
NSCCSTNTSQ EAHKDISYLY RFNWNHCGTM TSECKRHFIQ DTCLYECSPN LGPWIQQVDQ
SWRKERILDV PLCKEDCQQW WEDCQSSFTC KSNWHKGWNW SSGHNECPVG ASCHPFTFYF
PTSAALCEEI WSHSYKLSNY SRGSGRCIQM WFDPAQGNPN EEVARFYAEA MSGAGFHGTW
PLLCSLSLVL LWVIS


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