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Folate receptor alpha (FR-alpha) (Folate receptor 1) (Folate-binding protein 1) (FBP) (Milk folate-binding protein)

 FOLR1_BOVIN             Reviewed;         241 AA.
P02702;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
11-DEC-2013, sequence version 3.
25-OCT-2017, entry version 95.
RecName: Full=Folate receptor alpha;
Short=FR-alpha;
AltName: Full=Folate receptor 1;
AltName: Full=Folate-binding protein 1;
Short=FBP;
AltName: Full=Milk folate-binding protein;
Flags: Precursor;
Name=FOLR1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Smith T.P.L., Roberts A.J., Echternkamp S.E., Chitko-McKown C.G.,
Wray J.E., Keele J.W.;
"A second set of bovine ESTs from pooled-tissue normalized
libraries.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[2]
PROTEIN SEQUENCE OF 20-241.
TISSUE=Milk;
Svendsen I., Hansen S.I., Holm J., Lyngbye J.;
"The complete amino acid sequence of the folate-binding protein from
cow's milk.";
Carlsberg Res. Commun. 49:123-131(1984).
[3]
PROTEIN SEQUENCE OF 20-81; 91-121 AND 211-241, SUBCELLULAR LOCATION,
GLYCOSYLATION, TISSUE SPECIFICITY, AND DISULFIDE BONDS.
TISSUE=Milk;
Svendsen I., Martin B., Pedersen T.G., Hansen S.I., Holm J.,
Lyngbye J.;
"Isolation and characterization of the folate-binding protein from
cow's milk.";
Carlsberg Res. Commun. 44:89-99(1979).
-!- 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 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor,
GPI-anchor {ECO:0000250}. Secreted {ECO:0000269|Ref.3}.
Cytoplasmic vesicle {ECO:0000250}. Cytoplasmic vesicle, clathrin-
coated vesicle {ECO:0000250}. Endosome {ECO:0000250}. Apical cell
membrane {ECO:0000250}. Note=Endocytosed into cytoplasmic vesicles
and then recycled to the cell membrane. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in milk (at protein level).
{ECO:0000269|Ref.3}.
-!- 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}.
-!- SIMILARITY: Belongs to the folate receptor family. {ECO:0000305}.
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EMBL; DN512948; -; NOT_ANNOTATED_CDS; mRNA.
PIR; A03161; BFBO.
RefSeq; NP_001193456.1; NM_001206527.1.
RefSeq; NP_001193459.1; NM_001206530.1.
RefSeq; NP_001265501.1; NM_001278572.1.
RefSeq; NP_001265502.1; NM_001278573.1.
UniGene; Bt.62067; -.
SMR; P02702; -.
STRING; 9913.ENSBTAP00000027602; -.
PaxDb; P02702; -.
PeptideAtlas; P02702; -.
PRIDE; P02702; -.
Ensembl; ENSBTAT00000027602; ENSBTAP00000027602; ENSBTAG00000038532.
GeneID; 516067; -.
KEGG; bta:516067; -.
CTD; 2352; -.
eggNOG; ENOG410IFFP; Eukaryota.
eggNOG; ENOG4111IU4; LUCA.
GeneTree; ENSGT00390000010470; -.
HOGENOM; HOG000006539; -.
HOVERGEN; HBG039612; -.
InParanoid; P02702; -.
KO; K13649; -.
OMA; WNWTSGF; -.
OrthoDB; EOG091G0GIA; -.
Reactome; R-BTA-204005; COPII (Coat Protein 2) Mediated Vesicle Transport.
Reactome; R-BTA-5694530; Cargo concentration in the ER.
Reactome; R-BTA-6807878; COPI-mediated anterograde transport.
Proteomes; UP000009136; Chromosome 15.
Bgee; ENSBTAG00000038532; -.
GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005542; F:folic acid binding; ISS:UniProtKB.
GO; GO:0008517; F:folic acid transporter activity; ISS:UniProtKB.
GO; GO:0015884; P:folic acid transport; ISS:UniProtKB.
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;
Direct protein sequencing; Disulfide bond; Endosome; Folate-binding;
Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Milk protein;
Receptor; Reference proteome; Secreted; Signal; Transport.
SIGNAL 1 19 {ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
CHAIN 20 234 Folate receptor alpha.
/FTId=PRO_0000147394.
PROPEP 235 241 Removed in mature form.
/FTId=PRO_0000424694.
REGION 123 127 Folate binding.
{ECO:0000250|UniProtKB:P15328}.
REGION 156 161 Folate binding.
{ECO:0000250|UniProtKB:P15328}.
BINDING 102 102 Folate. {ECO:0000250|UniProtKB:P15328}.
BINDING 106 106 Folate. {ECO:0000250|UniProtKB:P15328}.
BINDING 195 195 Folate. {ECO:0000250|UniProtKB:P15328}.
LIPID 234 234 GPI-anchor amidated serine.
{ECO:0000250|UniProtKB:P15328}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000269|Ref.3}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000269|Ref.3}.
DISULFID 36 64 {ECO:0000250|UniProtKB:P15328}.
DISULFID 56 104 {ECO:0000250|UniProtKB:P15328}.
DISULFID 65 108 {ECO:0000250|UniProtKB:P15328}.
DISULFID 88 174 {ECO:0000250|UniProtKB:P15328}.
DISULFID 95 145 {ECO:0000250|UniProtKB:P15328}.
DISULFID 134 208 {ECO:0000250|UniProtKB:P15328}.
DISULFID 138 188 {ECO:0000250|UniProtKB:P15328}.
DISULFID 151 168 {ECO:0000250|UniProtKB:P15328}.
CONFLICT 174 175 CH -> HC (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 241 AA; 27922 MW; AC6EDC070594C2B2 CRC64;
MAWQMTQLLL LALVAAAWGA QAPRTPRART DLLNVCMDAK HHKAEPGPED SLHEQCSPWR
KNACCSVNTS IEAHKDISYL YRFNWDHCGK MEPACKRHFI QDTCLYECSP NLGPWIREVN
QRWRKERVLG VPLCKEDCQS WWEDCRTSYT CKSNWHKGWN WTSGYNQCPV KAACHRFDFY
FPTPAALCNE IWSHSYKVSN YSRGSGRCIQ MWFDPFQGNP NEEVARFYAE NPTSGSTPQG
I


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