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P35846 (FOLR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Folate receptor alpha

Short name=FR-alpha
Alternative name(s):
Folate receptor 1
Folate-binding protein 1
Gene names
Name:Folr1
Synonyms:Fbp1, Folbp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor. Secreted By similarity. Cytoplasmic vesicle By similarity. Cytoplasmic vesicleclathrin-coated vesicle By similarity. Endosome By similarity. Apical cell membrane. Note: Endocytosed into cytoplasmic vesicles and then recycled to the cell membrane By similarity. Detected at proximal tubule apical membranes. Ref.1 Ref.10

Tissue specificity

Detected in kidney proximal tubules (at protein level). Ref.10

Post-translational modification

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 By similarity.

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Sequence similarities

Belongs to the folate receptor family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 232208Folate receptor alpha
PRO_0000008804
Propeptide233 – 25523Removed in mature form By similarity
PRO_0000008805

Regions

Region122 – 1265Folate binding By similarity
Region155 – 1606Folate binding By similarity

Sites

Binding site1011Folate By similarity
Binding site1051Folate By similarity
Binding site1941Folate By similarity

Amino acid modifications

Lipidation2321GPI-anchor amidated serine By similarity
Glycosylation671N-linked (GlcNAc...) Potential
Glycosylation1591N-linked (GlcNAc...) Potential
Glycosylation1991N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 63 By similarity
Disulfide bond55 ↔ 103 By similarity
Disulfide bond64 ↔ 107 By similarity
Disulfide bond87 ↔ 173 By similarity
Disulfide bond94 ↔ 144 By similarity
Disulfide bond133 ↔ 207 By similarity
Disulfide bond137 ↔ 187 By similarity
Disulfide bond150 ↔ 167 By similarity

Experimental info

Sequence conflict2361F → L in AAA37595. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P35846 [UniParc].

Last modified December 11, 2013. Version 2.
Checksum: A12ACA978BC8E134

FASTA25529,449
        10         20         30         40         50         60 
MAHLMTVQLL LLVMWMAECA QSRATRARTE LLNVCMDAKH HKEKPGPEDN LHDQCSPWKT 

        70         80         90        100        110        120 
NSCCSTNTSQ EAHKDISYLY RFNWNHCGTM TSECKRHFIQ DTCLYECSPN LGPWIQQVDQ 

       130        140        150        160        170        180 
SWRKERILDV PLCKEDCQQW WEDCQSSFTC KSNWHKGWNW SSGHNECPVG ASCHPFTFYF 

       190        200        210        220        230        240 
PTSAALCEEI WSHSYKLSNY SRGSGRCIQM WFDPAQGNPN EEVARFYAEA MSGAGFHGTW 

       250 
PLLCSLSLVL LWVIS 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of two cDNAs encoding folate-binding proteins from L1210 murine leukemia cells. Increased expression associated with a genomic rearrangement."
Brigle K.E., Westin E.H., Houghton M.T., Goldman I.D.
J. Biol. Chem. 266:17243-17249(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
[2]"Retinoic acid-dependent upregulation of mouse folate receptor-alpha expression in embryonic stem cells, and conservation of alternative splicing patterns."
Bolton J.A., Wood S.A., Kennedy D., Don R.H., Mattick J.S.
Gene 230:215-224(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
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. expand/collapse author list , 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.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[6]"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."
Brigle K.E., Westin E.H., Houghton M.T., Goldman I.D.
J. Biol. Chem. 267:22351-22355(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
[7]"Mice lacking the folic acid-binding protein Folbp1 are defective in early embryonic development."
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.
Nat. Genet. 23:228-232(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[8]"Neural and orofacial defects in Folp1 knockout mice."
Tang L.S., Finnell R.H.
Birth Defects Res. A Clin. Mol. Teratol. 67:209-218(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[9]"Developmental consequences of abnormal folate transport during murine heart morphogenesis."
Tang L.S., Wlodarczyk B.J., Santillano D.R., Miranda R.C., Finnell R.H.
Birth Defects Res. A Clin. Mol. Teratol. 70:449-458(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[10]"Renal tubular reabsorption of folate mediated by folate binding protein 1."
Birn H., Spiegelstein O., Christensen E.I., Finnell R.H.
J. Am. Soc. Nephrol. 16:608-615(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[11]"Cardiovascular abnormalities in Folr1 knockout mice and folate rescue."
Zhu H., Wlodarczyk B.J., Scott M., Yu W., Merriweather M., Gelineau-van Waes J., Schwartz R.J., Finnell R.H.
Birth Defects Res. A Clin. Mol. Teratol. 79:257-268(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64782 mRNA. Translation: AAA37595.1.
AF096319 mRNA. Translation: AAD19353.1.
AC167240 Genomic DNA. No translation available.
CH466531 Genomic DNA. Translation: EDL16530.1.
CH466531 Genomic DNA. Translation: EDL16532.1.
CH466531 Genomic DNA. Translation: EDL16533.1.
CH466531 Genomic DNA. Translation: EDL16534.1.
CH466531 Genomic DNA. Translation: EDL16535.1.
CH466531 Genomic DNA. Translation: EDL16536.1.
CH466531 Genomic DNA. Translation: EDL16537.1.
CH466531 Genomic DNA. Translation: EDL16538.1.
BC138781 mRNA. Translation: AAI38782.1.
BC138795 mRNA. Translation: AAI38796.1.
BC145414 mRNA. Translation: AAI45415.1.
M97700 Genomic DNA. Translation: AAA37596.1.
M97701 Genomic DNA. Translation: AAA37598.1.
CCDSCCDS21517.1.
PIRA40969.
RefSeqNP_001239481.1. NM_001252552.1.
NP_001239482.1. NM_001252553.1.
NP_001239483.1. NM_001252554.1.
NP_032060.2. NM_008034.3.
XP_006507423.1. XM_006507360.1.
XP_006507424.1. XM_006507361.1.
XP_006507425.1. XM_006507362.1.
XP_006507426.1. XM_006507363.1.
XP_006507427.1. XM_006507364.1.
XP_006507428.1. XM_006507365.1.
XP_006507429.1. XM_006507366.1.
XP_006507430.1. XM_006507367.1.
XP_006507431.1. XM_006507368.1.
XP_006507432.1. XM_006507369.1.
XP_006507433.1. XM_006507370.1.
UniGeneMm.2135.
Mm.490265.

3D structure databases

ProteinModelPortalP35846.
SMRP35846. Positions 28-233.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP35846. 1 interaction.
MINTMINT-4130923.

Proteomic databases

PaxDbP35846.
PRIDEP35846.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000001882; ENSMUSP00000001882; ENSMUSG00000001827.
ENSMUST00000106981; ENSMUSP00000102594; ENSMUSG00000001827.
ENSMUST00000106982; ENSMUSP00000102595; ENSMUSG00000001827.
ENSMUST00000106983; ENSMUSP00000102596; ENSMUSG00000001827.
ENSMUST00000106985; ENSMUSP00000102598; ENSMUSG00000001827.
ENSMUST00000106986; ENSMUSP00000102599; ENSMUSG00000001827.
ENSMUST00000123321; ENSMUSP00000114167; ENSMUSG00000001827.
ENSMUST00000123630; ENSMUSP00000121947; ENSMUSG00000001827.
GeneID14275.
KEGGmmu:14275.
UCSCuc009ipm.1. mouse.

Organism-specific databases

CTD2348.
MGIMGI:95568. Folr1.

Phylogenomic databases

eggNOGNOG26606.
GeneTreeENSGT00390000010470.
HOGENOMHOG000006539.
HOVERGENHBG039612.
InParanoidP35846.
KOK13649.
OMANWTSGFN.
OrthoDBEOG7K6PW3.
TreeFamTF328532.

Gene expression databases

BgeeP35846.
CleanExMM_FBP1.
MM_FOLR1.
GenevestigatorP35846.

Family and domain databases

InterProIPR004269. Folate_rcpt.
IPR018143. Folate_rcpt-like.
[Graphical view]
PANTHERPTHR10517. PTHR10517. 1 hit.
PfamPF03024. Folate_rec. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285649.
PROP35846.
SOURCESearch...

Entry information

Entry nameFOLR1_MOUSE
AccessionPrimary (citable) accession number: P35846
Secondary accession number(s): Q9R222
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 11, 2013
Last modified: July 9, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot