FOLR1_BOVIN
ID FOLR1_BOVIN Reviewed; 241 AA.
AC P02702;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Folate receptor alpha;
DE Short=FR-alpha;
DE AltName: Full=Folate receptor 1;
DE AltName: Full=Folate-binding protein 1;
DE Short=FBP;
DE AltName: Full=Milk folate-binding protein;
DE Flags: Precursor;
GN Name=FOLR1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Smith T.P.L., Roberts A.J., Echternkamp S.E., Chitko-McKown C.G.,
RA Wray J.E., Keele J.W.;
RT "A second set of bovine ESTs from pooled-tissue normalized libraries.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 20-241.
RC TISSUE=Milk;
RA Svendsen I., Hansen S.I., Holm J., Lyngbye J.;
RT "The complete amino acid sequence of the folate-binding protein from cow's
RT milk.";
RL Carlsberg Res. Commun. 49:123-131(1984).
RN [3]
RP PROTEIN SEQUENCE OF 20-81; 91-121 AND 211-241, SUBCELLULAR LOCATION,
RP GLYCOSYLATION AT ASN-68 AND ASN-160, TISSUE SPECIFICITY, AND DISULFIDE
RP BONDS.
RC TISSUE=Milk;
RA Svendsen I., Martin B., Pedersen T.G., Hansen S.I., Holm J., Lyngbye J.;
RT "Isolation and characterization of the folate-binding protein from cow's
RT milk.";
RL Carlsberg Res. Commun. 44:89-99(1979).
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 Required for normal embryonic development and normal cell proliferation
CC (By similarity). {ECO:0000250|UniProtKB:P15328,
CC ECO:0000250|UniProtKB:P35846}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15328};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P15328}. Apical cell
CC membrane {ECO:0000250|UniProtKB:P15328}; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:P15328}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:P15328}; Lipid-anchor, GPI-like-anchor
CC {ECO:0000250|UniProtKB:P15328}. Secreted {ECO:0000269|Ref.3}.
CC Cytoplasmic vesicle {ECO:0000250|UniProtKB:P15328}. Cytoplasmic
CC vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:P15328}.
CC Endosome {ECO:0000250|UniProtKB:P15328}. Note=Endocytosed into
CC cytoplasmic vesicles and then recycled to the cell membrane.
CC {ECO:0000250|UniProtKB:P15328}.
CC -!- TISSUE SPECIFICITY: Detected in milk (at protein level).
CC {ECO:0000269|Ref.3}.
CC -!- PTM: The secreted form is derived from the membrane-bound form either
CC by cleavage of the GPI anchor, or/and by proteolysis catalyzed by a
CC metalloprotease. {ECO:0000250|UniProtKB:P15328}.
CC -!- SIMILARITY: Belongs to the folate receptor family. {ECO:0000305}.
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DR EMBL; DN512948; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A03161; BFBO.
DR RefSeq; NP_001193456.1; NM_001206527.1.
DR RefSeq; NP_001193459.1; NM_001206530.1.
DR RefSeq; NP_001265501.1; NM_001278572.1.
DR RefSeq; NP_001265502.1; NM_001278573.1.
DR AlphaFoldDB; P02702; -.
DR SMR; P02702; -.
DR PaxDb; P02702; -.
DR PeptideAtlas; P02702; -.
DR PRIDE; P02702; -.
DR GeneID; 516067; -.
DR KEGG; bta:516067; -.
DR CTD; 2352; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_070826_1_1_1; -.
DR InParanoid; P02702; -.
DR OrthoDB; 1224404at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031362; C:anchored component of external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0035036; P:sperm-egg recognition; IBA:GO_Central.
DR InterPro; IPR004269; Folate_rcpt.
DR InterPro; IPR018143; Folate_rcpt-like.
DR InterPro; IPR032935; FOLR1.
DR PANTHER; PTHR10517; PTHR10517; 1.
DR PANTHER; PTHR10517:SF15; PTHR10517:SF15; 1.
DR Pfam; PF03024; Folate_rec; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Direct protein sequencing;
KW Disulfide bond; Endosome; Folate-binding; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Milk protein; Receptor; Reference proteome;
KW Secreted; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.3"
FT CHAIN 20..234
FT /note="Folate receptor alpha"
FT /id="PRO_0000147394"
FT PROPEP 235..241
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000424694"
FT BINDING 102
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000250|UniProtKB:P15328"
FT BINDING 106
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000250|UniProtKB:P15328"
FT BINDING 123..127
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000250|UniProtKB:P15328"
FT BINDING 156..161
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000250|UniProtKB:P15328"
FT BINDING 195
FT /ligand="folate"
FT /ligand_id="ChEBI:CHEBI:62501"
FT /evidence="ECO:0000250|UniProtKB:P15328"
FT LIPID 234
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000250|UniProtKB:P15328"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.3"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.3"
FT DISULFID 36..64
FT /evidence="ECO:0000250|UniProtKB:P15328"
FT DISULFID 56..104
FT /evidence="ECO:0000250|UniProtKB:P15328"
FT DISULFID 65..108
FT /evidence="ECO:0000250|UniProtKB:P15328"
FT DISULFID 88..174
FT /evidence="ECO:0000250|UniProtKB:P15328"
FT DISULFID 95..145
FT /evidence="ECO:0000250|UniProtKB:P15328"
FT DISULFID 134..208
FT /evidence="ECO:0000250|UniProtKB:P15328"
FT DISULFID 138..188
FT /evidence="ECO:0000250|UniProtKB:P15328"
FT DISULFID 151..168
FT /evidence="ECO:0000250|UniProtKB:P15328"
FT CONFLICT 174..175
FT /note="CH -> HC (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ 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
