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P35846

- FOLR1_MOUSE

UniProt

P35846 - FOLR1_MOUSE

Protein

Folate receptor alpha

Gene

Folr1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 2 (11 Dec 2013)
      Previous versions | rss
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    Functioni

    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.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei101 – 1011FolateBy similarity
    Binding sitei105 – 1051FolateBy similarity
    Binding sitei194 – 1941FolateBy similarity

    GO - Molecular functioni

    1. folic acid binding Source: UniProtKB
    2. folic acid transporter activity Source: UniProtKB
    3. receptor activity Source: MGI

    GO - Biological processi

    1. folic acid metabolic process Source: MGI
    2. folic acid transport Source: UniProtKB
    3. posttranslational protein targeting to membrane Source: MGI

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Folate-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Folate receptor alpha
    Short name:
    FR-alpha
    Alternative name(s):
    Folate receptor 1
    Folate-binding protein 1
    Gene namesi
    Name:Folr1
    Synonyms:Fbp1, Folbp1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:95568. Folr1.

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. anchored component of external side of plasma membrane Source: UniProtKB
    2. apical plasma membrane Source: UniProtKB-SubCell
    3. clathrin-coated vesicle Source: UniProtKB-SubCell
    4. endosome Source: UniProtKB-SubCell
    5. extracellular region Source: UniProtKB-SubCell
    6. membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Endosome, Membrane, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    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.5 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 232208Folate receptor alphaPRO_0000008804Add
    BLAST
    Propeptidei233 – 25523Removed in mature formBy similarityPRO_0000008805Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi35 ↔ 63By similarity
    Disulfide bondi55 ↔ 103By similarity
    Disulfide bondi64 ↔ 107By similarity
    Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi87 ↔ 173By similarity
    Disulfide bondi94 ↔ 144By similarity
    Disulfide bondi133 ↔ 207By similarity
    Disulfide bondi137 ↔ 187By similarity
    Disulfide bondi150 ↔ 167By similarity
    Glycosylationi159 – 1591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi199 – 1991N-linked (GlcNAc...)Sequence Analysis
    Lipidationi232 – 2321GPI-anchor amidated serineBy similarity

    Post-translational modificationi

    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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    PaxDbiP35846.
    PRIDEiP35846.

    Expressioni

    Tissue specificityi

    Detected in kidney proximal tubules (at protein level).1 Publication

    Gene expression databases

    BgeeiP35846.
    CleanExiMM_FBP1.
    MM_FOLR1.
    GenevestigatoriP35846.

    Interactioni

    Protein-protein interaction databases

    IntActiP35846. 1 interaction.
    MINTiMINT-4130923.

    Structurei

    3D structure databases

    ProteinModelPortaliP35846.
    SMRiP35846. Positions 28-233.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni122 – 1265Folate bindingBy similarity
    Regioni155 – 1606Folate bindingBy similarity

    Sequence similaritiesi

    Belongs to the folate receptor family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG26606.
    GeneTreeiENSGT00390000010470.
    HOGENOMiHOG000006539.
    HOVERGENiHBG039612.
    InParanoidiP35846.
    KOiK13649.
    OMAiNWTSGFN.
    OrthoDBiEOG7K6PW3.
    TreeFamiTF328532.

    Family and domain databases

    InterProiIPR004269. Folate_rcpt.
    IPR018143. Folate_rcpt-like.
    [Graphical view]
    PANTHERiPTHR10517. PTHR10517. 1 hit.
    PfamiPF03024. Folate_rec. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P35846-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAHLMTVQLL LLVMWMAECA QSRATRARTE LLNVCMDAKH HKEKPGPEDN    50
    LHDQCSPWKT NSCCSTNTSQ EAHKDISYLY RFNWNHCGTM TSECKRHFIQ 100
    DTCLYECSPN LGPWIQQVDQ SWRKERILDV PLCKEDCQQW WEDCQSSFTC 150
    KSNWHKGWNW SSGHNECPVG ASCHPFTFYF PTSAALCEEI WSHSYKLSNY 200
    SRGSGRCIQM WFDPAQGNPN EEVARFYAEA MSGAGFHGTW PLLCSLSLVL 250
    LWVIS 255
    Length:255
    Mass (Da):29,449
    Last modified:December 11, 2013 - v2
    Checksum:iA12ACA978BC8E134
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti236 – 2361F → L in AAA37595. (PubMed:1894617)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS21517.1.
    PIRiA40969.
    RefSeqiNP_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.
    UniGeneiMm.2135.
    Mm.490265.

    Genome annotation databases

    EnsembliENSMUST00000001882; ENSMUSP00000001882; ENSMUSG00000001827.
    ENSMUST00000106981; ENSMUSP00000102594; ENSMUSG00000001827.
    ENSMUST00000106982; ENSMUSP00000102595; ENSMUSG00000001827.
    ENSMUST00000106983; ENSMUSP00000102596; ENSMUSG00000001827.
    ENSMUST00000106985; ENSMUSP00000102598; ENSMUSG00000001827.
    ENSMUST00000106986; ENSMUSP00000102599; ENSMUSG00000001827.
    ENSMUST00000123321; ENSMUSP00000114167; ENSMUSG00000001827.
    ENSMUST00000123630; ENSMUSP00000121947; ENSMUSG00000001827.
    GeneIDi14275.
    KEGGimmu:14275.
    UCSCiuc009ipm.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS21517.1.
    PIRi A40969.
    RefSeqi NP_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.
    UniGenei Mm.2135.
    Mm.490265.

    3D structure databases

    ProteinModelPortali P35846.
    SMRi P35846. Positions 28-233.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P35846. 1 interaction.
    MINTi MINT-4130923.

    Proteomic databases

    PaxDbi P35846.
    PRIDEi P35846.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000001882 ; ENSMUSP00000001882 ; ENSMUSG00000001827 .
    ENSMUST00000106981 ; ENSMUSP00000102594 ; ENSMUSG00000001827 .
    ENSMUST00000106982 ; ENSMUSP00000102595 ; ENSMUSG00000001827 .
    ENSMUST00000106983 ; ENSMUSP00000102596 ; ENSMUSG00000001827 .
    ENSMUST00000106985 ; ENSMUSP00000102598 ; ENSMUSG00000001827 .
    ENSMUST00000106986 ; ENSMUSP00000102599 ; ENSMUSG00000001827 .
    ENSMUST00000123321 ; ENSMUSP00000114167 ; ENSMUSG00000001827 .
    ENSMUST00000123630 ; ENSMUSP00000121947 ; ENSMUSG00000001827 .
    GeneIDi 14275.
    KEGGi mmu:14275.
    UCSCi uc009ipm.1. mouse.

    Organism-specific databases

    CTDi 2348.
    MGIi MGI:95568. Folr1.

    Phylogenomic databases

    eggNOGi NOG26606.
    GeneTreei ENSGT00390000010470.
    HOGENOMi HOG000006539.
    HOVERGENi HBG039612.
    InParanoidi P35846.
    KOi K13649.
    OMAi NWTSGFN.
    OrthoDBi EOG7K6PW3.
    TreeFami TF328532.

    Miscellaneous databases

    NextBioi 285649.
    PROi P35846.
    SOURCEi Search...

    Gene expression databases

    Bgeei P35846.
    CleanExi MM_FBP1.
    MM_FOLR1.
    Genevestigatori P35846.

    Family and domain databases

    InterProi IPR004269. Folate_rcpt.
    IPR018143. Folate_rcpt-like.
    [Graphical view ]
    PANTHERi PTHR10517. PTHR10517. 1 hit.
    Pfami PF03024. Folate_rec. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. Cited for: DISRUPTION PHENOTYPE, FUNCTION.

    Entry informationi

    Entry nameiFOLR1_MOUSE
    AccessioniPrimary (citable) accession number: P35846
    Secondary accession number(s): Q9R222
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: December 11, 2013
    Last modified: October 1, 2014
    This is version 95 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3