FOLR2_MOUSE
ID FOLR2_MOUSE Reviewed; 251 AA.
AC Q05685;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Folate receptor beta;
DE Short=FR-beta;
DE AltName: Full=Folate receptor 2;
DE AltName: Full=Folate-binding protein 2;
DE Flags: Precursor;
GN Name=Folr2; Synonyms=Fbp2, Folbp2;
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].
RX PubMed=1894617; DOI=10.1016/s0021-9258(19)47365-1;
RA Brigle K.E., Westin E.H., Houghton M.T., Goldman I.D.;
RT "Characterization of two cDNAs encoding folate-binding proteins from L1210
RT murine leukemia cells. Increased expression associated with a genomic
RT rearrangement.";
RL J. Biol. Chem. 266:17243-17249(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 [GENOMIC DNA] OF 1-49.
RX PubMed=8307991; DOI=10.1016/s0021-9258(17)41773-x;
RA Brigle K.E., Seither R.L., Westin E.H., Goldman I.D.;
RT "Increased expression and genomic organization of a folate-binding protein
RT homologous to the human placental isoform in L1210 murine leukemia cell
RT lines with a defective reduced folate carrier.";
RL J. Biol. Chem. 269:4267-4272(1994).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=10508523; DOI=10.1038/13861;
RA Piedrahita J.A., Oetama B., Bennett G.D., van Waes J., Kamen B.A.,
RA Richardson J., Lacey S.W., Anderson R.G., Finnell R.H.;
RT "Mice lacking the folic acid-binding protein Folbp1 are defective in early
RT embryonic development.";
RL Nat. Genet. 23:228-232(1999).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=15703271; DOI=10.1681/asn.2004080711;
RA Birn H., Spiegelstein O., Christensen E.I., Finnell R.H.;
RT "Renal tubular reabsorption of folate mediated by folate binding protein
RT 1.";
RL J. Am. Soc. Nephrol. 16:608-615(2005).
CC -!- FUNCTION: Binds to folate and reduced folic acid derivatives and
CC mediates delivery of 5-methyltetrahydrofolate and folate analogs into
CC the interior of cells. Has high affinity for folate and folic acid
CC analogs at neutral pH. Exposure to slightly acidic pH after receptor
CC endocytosis triggers a conformation change that strongly reduces its
CC affinity for folates and mediates their release (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:10508523, ECO:0000269|PubMed:15703271}.
CC -!- SIMILARITY: Belongs to the folate receptor family. {ECO:0000305}.
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DR EMBL; M64817; AAA37599.1; -; mRNA.
DR EMBL; BC022108; AAH22108.1; -; mRNA.
DR EMBL; L25338; AAA37594.1; -; Genomic_DNA.
DR CCDS; CCDS21516.1; -.
DR PIR; B40969; B40969.
DR RefSeq; NP_001290160.1; NM_001303231.1.
DR RefSeq; NP_001290168.1; NM_001303239.1.
DR RefSeq; NP_032061.1; NM_008035.2.
DR AlphaFoldDB; Q05685; -.
DR SMR; Q05685; -.
DR BioGRID; 199725; 1.
DR STRING; 10090.ENSMUSP00000091692; -.
DR GlyGen; Q05685; 2 sites.
DR PhosphoSitePlus; Q05685; -.
DR MaxQB; Q05685; -.
DR PaxDb; Q05685; -.
DR PRIDE; Q05685; -.
DR ProteomicsDB; 267391; -.
DR ABCD; Q05685; 1 sequenced antibody.
DR Antibodypedia; 30818; 351 antibodies from 32 providers.
DR DNASU; 14276; -.
DR Ensembl; ENSMUST00000094141; ENSMUSP00000091692; ENSMUSG00000032725.
DR Ensembl; ENSMUST00000210598; ENSMUSP00000147920; ENSMUSG00000032725.
DR GeneID; 14276; -.
DR KEGG; mmu:14276; -.
DR UCSC; uc009ipk.2; mouse.
DR CTD; 2350; -.
DR MGI; MGI:95569; Folr2.
DR VEuPathDB; HostDB:ENSMUSG00000032725; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00950000183144; -.
DR HOGENOM; CLU_070826_1_1_1; -.
DR InParanoid; Q05685; -.
DR OMA; ACHTFEF; -.
DR OrthoDB; 1534387at2759; -.
DR PhylomeDB; Q05685; -.
DR TreeFam; TF328532; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Reactome; R-MMU-196757; Metabolism of folate and pterines.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 14276; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Folr2; mouse.
DR PRO; PR:Q05685; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q05685; protein.
DR Bgee; ENSMUSG00000032725; Expressed in stroma of bone marrow and 108 other tissues.
DR ExpressionAtlas; Q05685; baseline and differential.
DR Genevisible; Q05685; MM.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005542; F:folic acid binding; ISS:UniProtKB.
DR GO; GO:0061714; F:folic acid receptor activity; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:1904447; P:folate import across plasma membrane; IEA:InterPro.
DR GO; GO:0015884; P:folic acid transport; ISS:UniProtKB.
DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; TAS:MGI.
DR GO; GO:0035036; P:sperm-egg recognition; IBA:GO_Central.
DR InterPro; IPR004269; Folate_rcpt.
DR InterPro; IPR018143; Folate_rcpt-like.
DR InterPro; IPR032937; FOLR2.
DR PANTHER; PTHR10517; PTHR10517; 1.
DR PANTHER; PTHR10517:SF8; PTHR10517:SF8; 1.
DR Pfam; PF03024; Folate_rec; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Folate-binding; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Receptor; Reference proteome; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..227
FT /note="Folate receptor beta"
FT /id="PRO_0000008808"
FT PROPEP 228..251
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000008809"
FT BINDING 95
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000250|UniProtKB:P14207"
FT BINDING 99
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000250|UniProtKB:P14207"
FT BINDING 116..120
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000250|UniProtKB:P14207"
FT BINDING 149..154
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000250|UniProtKB:P14207"
FT BINDING 188
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000250|UniProtKB:P14207"
FT LIPID 227
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250|UniProtKB:P14207, ECO:0000255"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..58
FT /evidence="ECO:0000250|UniProtKB:P14207"
FT DISULFID 50..97
FT /evidence="ECO:0000250|UniProtKB:P14207"
FT DISULFID 59..101
FT /evidence="ECO:0000250|UniProtKB:P14207"
FT DISULFID 81..167
FT /evidence="ECO:0000250|UniProtKB:P14207"
FT DISULFID 88..138
FT /evidence="ECO:0000250|UniProtKB:P14207"
FT DISULFID 127..201
FT /evidence="ECO:0000250|UniProtKB:P14207"
FT DISULFID 131..181
FT /evidence="ECO:0000250|UniProtKB:P14207"
FT DISULFID 144..161
FT /evidence="ECO:0000250|UniProtKB:P14207"
SQ SEQUENCE 251 AA; 28821 MW; 8404EACEB1BFECC7 CRC64;
MAWKQTPLLL LVYMVTTGSG RDRTDLLNVC MDAKHHKTKP GPEDKLHDQC SPWKKNACCS
VNTSQELHKA DSRLYFNWDH CGKMEPACKS HFIQDSCLYE CSPNLGPWIQ QVDQSWRKER
FLDVPLCKED CHQWWEACRT SFTCKRDWHK GWDWSSGINK CPNTAPCHTF EYYFPTPASL
CEGLWSHSYK VSNYSRGSGR CIQMWFDSTQ GNPNEDVVKF YASFMTSGTV PHAAVLLVPS
LAPVLSLWLP G
