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Folate receptor beta (FR-beta) (Folate receptor 2) (Folate receptor, fetal/placental) (Placental folate-binding protein) (FBP)

 FOLR2_HUMAN             Reviewed;         255 AA.
P14207; Q05CA5; Q6GTE8;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 4.
27-SEP-2017, entry version 154.
RecName: Full=Folate receptor beta;
Short=FR-beta;
AltName: Full=Folate receptor 2;
AltName: Full=Folate receptor, fetal/placental;
AltName: Full=Placental folate-binding protein;
Short=FBP;
Flags: Precursor;
Name=FOLR2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
PubMed=8445646; DOI=10.1006/jmbi.1993.1116;
Page S.T., Owen W.C., Price K., Elwood P.C.;
"Expression of the human placental folate receptor transcript is
regulated in human tissues. Organization and full nucleotide sequence
of the gene.";
J. Mol. Biol. 229:1175-1183(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, TISSUE
SPECIFICITY, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
TISSUE=Placenta;
PubMed=2605182; DOI=10.1021/bi00446a042;
Ratnam M., Marquardt H., Duhring J.L., Freisheim J.H.;
"Homologous membrane folate binding proteins in human placenta:
cloning and sequence of a cDNA.";
Biochemistry 28:8249-8254(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=8106441;
Sadasivan E., Cedeno M.M., Rothenberg S.P.;
"Characterization of the gene encoding a folate-binding protein
expressed in human placenta. Identification of promoter activity in a
G-rich SP1 site linked with the tandemly repeated GGAAG motif for the
ets encoded GA-binding protein.";
J. Biol. Chem. 269:4725-4735(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas, and Placenta;
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]
PROTEIN SEQUENCE OF 68-86; 102-120 AND 173-184.
PubMed=2561247; DOI=10.1016/0065-2571(89)90091-5;
Freisheim J.H., Price E.M., Ratnam M.;
"Folate coenzyme and antifolate transport proteins in normal and
neoplastic cells.";
Adv. Enzyme Regul. 29:13-26(1989).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=4066659;
Antony A.C., Kane M.A., Portillo R.M., Elwood P.C., Kolhouse J.F.;
"Studies of the role of a particulate folate-binding protein in the
uptake of 5-methyltetrahydrofolate by cultured human KB cells.";
J. Biol. Chem. 260:14911-14917(1985).
[8]
GPI-ANCHOR AT ASN-230.
PubMed=7578066; DOI=10.1021/bi00044a039;
Yan W., Ratnam M.;
"Preferred sites of glycosylphosphatidylinositol modification in
folate receptors and constraints in the primary structure of the
hydrophobic portion of the signal.";
Biochemistry 34:14594-14600(1995).
[9]
PROTEOLYTIC PROCESSING.
PubMed=9398177; DOI=10.1021/bi970845w;
Wang J., Shen F., Yan W., Wu M., Ratnam M.;
"Proteolysis of the carboxyl-terminal GPI signal independent of GPI
modification as a mechanism for selective protein secretion.";
Biochemistry 36:14583-14592(1997).
[10]
INDUCTION BY RETINOIC ACID.
PubMed=20632143; DOI=10.1007/s13277-010-0074-0;
Xu Y., Wang T., Tang R., Tang S.;
"All-trans retinoic acid is capable of inducing folate receptor beta
expression in KG-1 cells.";
Tumor Biol. 31:589-595(2010).
[11]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 24-228 IN COMPLEXES WITH
FOLATE AND THE ANTIFOLATES METHOTREXATE; AMINOPTERIN AND PEMETREXED,
FUNCTION, GLYCOSYLATION AT ASN-195, AND DISULFIDE BONDS.
PubMed=23934049; DOI=10.1073/pnas.1308827110;
Wibowo A.S., Singh M., Reeder K.M., Carter J.J., Kovach A.R., Meng W.,
Ratnam M., Zhang F., Dann C.E. III;
"Structures of human folate receptors reveal biological trafficking
states and diversity in folate and antifolate recognition.";
Proc. Natl. Acad. Sci. U.S.A. 110:15180-15188(2013).
[12]
VARIANT [LARGE SCALE ANALYSIS] ASN-236.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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.
{ECO:0000269|PubMed:23934049, ECO:0000269|PubMed:2605182,
ECO:0000269|PubMed:4066659}.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
Secreted {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in placenta and hematopoietic cells.
Expression is increased in malignant tissues.
{ECO:0000269|PubMed:2605182, ECO:0000269|PubMed:8445646}.
-!- INDUCTION: Up-regulated by retinoic acid.
{ECO:0000269|PubMed:20632143}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:23934049,
ECO:0000269|PubMed:2605182}.
-!- SIMILARITY: Belongs to the folate receptor family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X69516; CAA49267.1; -; Genomic_DNA.
EMBL; J02876; AAA35821.1; -; mRNA.
EMBL; U02714; AAA17370.1; -; Genomic_DNA.
EMBL; U02716; AAA17370.1; JOINED; Genomic_DNA.
EMBL; AK222643; BAD96363.1; -; mRNA.
EMBL; BC058036; AAH58036.1; -; mRNA.
EMBL; BC027894; AAH27894.1; -; mRNA.
CCDS; CCDS8212.1; -.
PIR; A53315; A33417.
RefSeq; NP_000794.3; NM_000803.4.
RefSeq; NP_001107006.1; NM_001113534.1.
RefSeq; NP_001107007.1; NM_001113535.1.
RefSeq; NP_001107008.1; NM_001113536.1.
UniGene; Hs.433159; -.
PDB; 4KMY; X-ray; 1.80 A; A=24-228.
PDB; 4KMZ; X-ray; 2.30 A; A=24-228.
PDB; 4KN0; X-ray; 2.10 A; A=24-228.
PDB; 4KN1; X-ray; 2.30 A; A=24-228.
PDB; 4KN2; X-ray; 2.60 A; A/B/C=24-227.
PDBsum; 4KMY; -.
PDBsum; 4KMZ; -.
PDBsum; 4KN0; -.
PDBsum; 4KN1; -.
PDBsum; 4KN2; -.
ProteinModelPortal; P14207; -.
SMR; P14207; -.
STRING; 9606.ENSP00000298223; -.
BindingDB; P14207; -.
ChEMBL; CHEMBL5064; -.
DrugBank; DB05168; EC145.
DrugBank; DB00158; Folic Acid.
BioMuta; FOLR2; -.
DMDM; 116241366; -.
PaxDb; P14207; -.
PeptideAtlas; P14207; -.
PRIDE; P14207; -.
DNASU; 2350; -.
Ensembl; ENST00000298223; ENSP00000298223; ENSG00000165457.
GeneID; 2350; -.
KEGG; hsa:2350; -.
UCSC; uc001ose.5; human.
CTD; 2350; -.
DisGeNET; 2350; -.
EuPathDB; HostDB:ENSG00000165457.13; -.
GeneCards; FOLR2; -.
HGNC; HGNC:3793; FOLR2.
MIM; 136425; gene.
neXtProt; NX_P14207; -.
OpenTargets; ENSG00000165457; -.
PharmGKB; PA28209; -.
eggNOG; ENOG410IFFP; Eukaryota.
eggNOG; ENOG4111IU4; LUCA.
GeneTree; ENSGT00390000010470; -.
HOGENOM; HOG000006539; -.
HOVERGEN; HBG039612; -.
InParanoid; P14207; -.
KO; K13649; -.
OMA; KNACCSA; -.
OrthoDB; EOG091G0GIA; -.
PhylomeDB; P14207; -.
TreeFam; TF328532; -.
Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
Reactome; R-HSA-196757; Metabolism of folate and pterines.
GeneWiki; FOLR2; -.
GenomeRNAi; 2350; -.
PRO; PR:P14207; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000165457; -.
CleanEx; HS_FOLR2; -.
ExpressionAtlas; P14207; baseline and differential.
Genevisible; P14207; HS.
GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0008144; F:drug binding; IPI:BHF-UCL.
GO; GO:0005542; F:folic acid binding; IDA:UniProtKB.
GO; GO:0061714; F:folic acid receptor activity; IC:BHF-UCL.
GO; GO:0008517; F:folic acid transporter activity; IDA:UniProtKB.
GO; GO:0051870; F:methotrexate binding; IDA:BHF-UCL.
GO; GO:0006501; P:C-terminal protein lipidation; TAS:Reactome.
GO; GO:0046655; P:folic acid metabolic process; TAS:Reactome.
GO; GO:0015884; P:folic acid transport; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; NAS:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; IC:BHF-UCL.
GO; GO:0050758; P:regulation of thymidylate synthase biosynthetic process; IC:BHF-UCL.
InterPro; IPR004269; Folate_rcpt.
InterPro; IPR018143; Folate_rcpt-like.
InterPro; IPR032937; FOLR2.
PANTHER; PTHR10517; PTHR10517; 1.
PANTHER; PTHR10517:SF24; PTHR10517:SF24; 1.
Pfam; PF03024; Folate_rec; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Folate-binding;
Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Polymorphism;
Receptor; Reference proteome; Secreted; Signal; Transport.
SIGNAL 1 16
CHAIN 17 230 Folate receptor beta.
/FTId=PRO_0000008806.
PROPEP 231 255 Removed in mature form.
/FTId=PRO_0000008807.
REGION 118 122 Folate binding. {ECO:0000244|PDB:4KMZ}.
REGION 151 156 Folate binding. {ECO:0000244|PDB:4KMZ}.
BINDING 97 97 Folate. {ECO:0000244|PDB:4KMZ}.
BINDING 101 101 Folate. {ECO:0000244|PDB:4KMZ}.
BINDING 190 190 Folate. {ECO:0000244|PDB:4KMZ}.
LIPID 230 230 GPI-anchor amidated asparagine.
{ECO:0000269|PubMed:7578066}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4KN0}.
CARBOHYD 195 195 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4KMZ,
ECO:0000244|PDB:4KN0,
ECO:0000244|PDB:4KN1,
ECO:0000244|PDB:4KN2,
ECO:0000269|PubMed:23934049}.
DISULFID 31 59 {ECO:0000244|PDB:4KMY,
ECO:0000244|PDB:4KMZ,
ECO:0000244|PDB:4KN0,
ECO:0000244|PDB:4KN1,
ECO:0000244|PDB:4KN2,
ECO:0000269|PubMed:23934049}.
DISULFID 51 99 {ECO:0000244|PDB:4KMY,
ECO:0000244|PDB:4KMZ,
ECO:0000244|PDB:4KN0,
ECO:0000244|PDB:4KN1,
ECO:0000244|PDB:4KN2,
ECO:0000269|PubMed:23934049}.
DISULFID 60 103 {ECO:0000244|PDB:4KMY,
ECO:0000244|PDB:4KMZ,
ECO:0000244|PDB:4KN0,
ECO:0000244|PDB:4KN1,
ECO:0000244|PDB:4KN2,
ECO:0000269|PubMed:23934049}.
DISULFID 83 169 {ECO:0000244|PDB:4KMY,
ECO:0000244|PDB:4KMZ,
ECO:0000244|PDB:4KN0,
ECO:0000244|PDB:4KN1,
ECO:0000244|PDB:4KN2,
ECO:0000269|PubMed:23934049}.
DISULFID 90 140 {ECO:0000244|PDB:4KMY,
ECO:0000244|PDB:4KMZ,
ECO:0000244|PDB:4KN0,
ECO:0000244|PDB:4KN1,
ECO:0000244|PDB:4KN2,
ECO:0000269|PubMed:23934049}.
DISULFID 129 203 {ECO:0000244|PDB:4KMY,
ECO:0000244|PDB:4KMZ,
ECO:0000244|PDB:4KN0,
ECO:0000244|PDB:4KN1,
ECO:0000244|PDB:4KN2,
ECO:0000269|PubMed:23934049}.
DISULFID 133 183 {ECO:0000244|PDB:4KMY,
ECO:0000244|PDB:4KMZ,
ECO:0000244|PDB:4KN0,
ECO:0000244|PDB:4KN1,
ECO:0000244|PDB:4KN2,
ECO:0000269|PubMed:23934049}.
DISULFID 146 163 {ECO:0000244|PDB:4KMY,
ECO:0000244|PDB:4KMZ,
ECO:0000244|PDB:4KN0,
ECO:0000244|PDB:4KN1,
ECO:0000244|PDB:4KN2,
ECO:0000269|PubMed:23934049}.
VARIANT 236 236 H -> N (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036408.
CONFLICT 103 103 C -> V (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 111 112 IQ -> VR (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 115 115 N -> D (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 117 117 S -> T (in Ref. 2; AAA35821, 3; AAA17370
and 6; AA sequence). {ECO:0000305}.
CONFLICT 141 141 H -> L (in Ref. 3; AAA17370).
{ECO:0000305}.
CONFLICT 244 244 S -> R (in Ref. 3; AAA17370).
{ECO:0000305}.
HELIX 24 27 {ECO:0000244|PDB:4KMY}.
STRAND 33 36 {ECO:0000244|PDB:4KMZ}.
HELIX 49 54 {ECO:0000244|PDB:4KMY}.
STRAND 57 60 {ECO:0000244|PDB:4KMY}.
HELIX 62 68 {ECO:0000244|PDB:4KMY}.
STRAND 74 76 {ECO:0000244|PDB:4KMY}.
TURN 80 83 {ECO:0000244|PDB:4KMY}.
HELIX 88 103 {ECO:0000244|PDB:4KMY}.
HELIX 108 110 {ECO:0000244|PDB:4KMY}.
STRAND 111 116 {ECO:0000244|PDB:4KMY}.
STRAND 119 123 {ECO:0000244|PDB:4KMY}.
STRAND 126 128 {ECO:0000244|PDB:4KN0}.
HELIX 130 140 {ECO:0000244|PDB:4KMY}.
STRAND 144 146 {ECO:0000244|PDB:4KMY}.
STRAND 150 152 {ECO:0000244|PDB:4KN0}.
HELIX 172 175 {ECO:0000244|PDB:4KMY}.
HELIX 179 185 {ECO:0000244|PDB:4KMY}.
TURN 186 188 {ECO:0000244|PDB:4KMY}.
STRAND 189 191 {ECO:0000244|PDB:4KMY}.
STRAND 200 204 {ECO:0000244|PDB:4KMY}.
HELIX 216 223 {ECO:0000244|PDB:4KMY}.
SEQUENCE 255 AA; 29280 MW; F585715CF5631C98 CRC64;
MVWKWMPLLL LLVCVATMCS AQDRTDLLNV CMDAKHHKTK PGPEDKLHDQ CSPWKKNACC
TASTSQELHK DTSRLYNFNW DHCGKMEPAC KRHFIQDTCL YECSPNLGPW IQQVNQSWRK
ERFLDVPLCK EDCQRWWEDC HTSHTCKSNW HRGWDWTSGV NKCPAGALCR TFESYFPTPA
ALCEGLWSHS YKVSNYSRGS GRCIQMWFDS AQGNPNEEVA RFYAAAMHVN AGEMLHGTGG
LLLSLALMLQ LWLLG


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