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Protein

Folate receptor beta

Gene

Folr2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei95 – 951FolateBy similarity
Binding sitei99 – 991FolateBy similarity
Binding sitei188 – 1881FolateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transport

Keywords - Ligandi

Folate-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Folate receptor beta
Short name:
FR-beta
Alternative name(s):
Folate receptor 2
Folate-binding protein 2
Gene namesi
Name:Folr2
Synonyms:Fbp2, Folbp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:95569. Folr2.

Subcellular locationi

GO - Cellular componenti

  • anchored component of external side of plasma membrane Source: UniProtKB
  • cell surface Source: MGI
  • intracellular Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 227207Folate receptor betaPRO_0000008808Add
BLAST
Propeptidei228 – 25124Removed in mature formSequence analysisPRO_0000008809Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 58By similarity
Disulfide bondi50 ↔ 97By similarity
Disulfide bondi59 ↔ 101By similarity
Glycosylationi62 – 621N-linked (GlcNAc...)Sequence analysis
Disulfide bondi81 ↔ 167By similarity
Disulfide bondi88 ↔ 138By similarity
Disulfide bondi127 ↔ 201By similarity
Disulfide bondi131 ↔ 181By similarity
Disulfide bondi144 ↔ 161By similarity
Glycosylationi193 – 1931N-linked (GlcNAc...)Sequence analysis
Lipidationi227 – 2271GPI-anchor amidated serineSequence analysisBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

EPDiQ05685.
MaxQBiQ05685.
PaxDbiQ05685.
PRIDEiQ05685.

PTM databases

PhosphoSiteiQ05685.

Expressioni

Gene expression databases

BgeeiQ05685.
CleanExiMM_FBP2.
MM_FOLR2.
GenevisibleiQ05685. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000091692.

Structurei

3D structure databases

ProteinModelPortaliQ05685.
SMRiQ05685. Positions 23-225.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni116 – 1205Folate bindingBy similarity
Regioni149 – 1546Folate bindingBy similarity

Sequence similaritiesi

Belongs to the folate receptor family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IFFP. Eukaryota.
ENOG4111IU4. LUCA.
GeneTreeiENSGT00390000010470.
HOGENOMiHOG000006539.
HOVERGENiHBG039612.
InParanoidiQ05685.
KOiK13649.
OMAiPVALCEG.
OrthoDBiEOG7K6PW3.
PhylomeDBiQ05685.
TreeFamiTF328532.

Family and domain databases

InterProiIPR004269. Folate_rcpt.
IPR018143. Folate_rcpt-like.
IPR032937. FOLR2.
[Graphical view]
PANTHERiPTHR10517. PTHR10517. 1 hit.
PTHR10517:SF8. PTHR10517:SF8. 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.

Q05685-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWKQTPLLL LVYMVTTGSG RDRTDLLNVC MDAKHHKTKP GPEDKLHDQC
60 70 80 90 100
SPWKKNACCS VNTSQELHKA DSRLYFNWDH CGKMEPACKS HFIQDSCLYE
110 120 130 140 150
CSPNLGPWIQ QVDQSWRKER FLDVPLCKED CHQWWEACRT SFTCKRDWHK
160 170 180 190 200
GWDWSSGINK CPNTAPCHTF EYYFPTPASL CEGLWSHSYK VSNYSRGSGR
210 220 230 240 250
CIQMWFDSTQ GNPNEDVVKF YASFMTSGTV PHAAVLLVPS LAPVLSLWLP

G
Length:251
Mass (Da):28,821
Last modified:June 1, 1994 - v1
Checksum:i8404EACEB1BFECC7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64817 mRNA. Translation: AAA37599.1.
BC022108 mRNA. Translation: AAH22108.1.
L25338 Genomic DNA. Translation: AAA37594.1.
CCDSiCCDS21516.1.
PIRiB40969.
RefSeqiNP_001290160.1. NM_001303231.1.
NP_001290168.1. NM_001303239.1.
NP_032061.1. NM_008035.2.
UniGeneiMm.439666.

Genome annotation databases

EnsembliENSMUST00000094141; ENSMUSP00000091692; ENSMUSG00000032725.
GeneIDi14276.
KEGGimmu:14276.
UCSCiuc009ipk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64817 mRNA. Translation: AAA37599.1.
BC022108 mRNA. Translation: AAH22108.1.
L25338 Genomic DNA. Translation: AAA37594.1.
CCDSiCCDS21516.1.
PIRiB40969.
RefSeqiNP_001290160.1. NM_001303231.1.
NP_001290168.1. NM_001303239.1.
NP_032061.1. NM_008035.2.
UniGeneiMm.439666.

3D structure databases

ProteinModelPortaliQ05685.
SMRiQ05685. Positions 23-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000091692.

PTM databases

PhosphoSiteiQ05685.

Proteomic databases

EPDiQ05685.
MaxQBiQ05685.
PaxDbiQ05685.
PRIDEiQ05685.

Protocols and materials databases

DNASUi14276.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000094141; ENSMUSP00000091692; ENSMUSG00000032725.
GeneIDi14276.
KEGGimmu:14276.
UCSCiuc009ipk.2. mouse.

Organism-specific databases

CTDi2350.
MGIiMGI:95569. Folr2.

Phylogenomic databases

eggNOGiENOG410IFFP. Eukaryota.
ENOG4111IU4. LUCA.
GeneTreeiENSGT00390000010470.
HOGENOMiHOG000006539.
HOVERGENiHBG039612.
InParanoidiQ05685.
KOiK13649.
OMAiPVALCEG.
OrthoDBiEOG7K6PW3.
PhylomeDBiQ05685.
TreeFamiTF328532.

Miscellaneous databases

PROiQ05685.
SOURCEiSearch...

Gene expression databases

BgeeiQ05685.
CleanExiMM_FBP2.
MM_FOLR2.
GenevisibleiQ05685. MM.

Family and domain databases

InterProiIPR004269. Folate_rcpt.
IPR018143. Folate_rcpt-like.
IPR032937. FOLR2.
[Graphical view]
PANTHERiPTHR10517. PTHR10517. 1 hit.
PTHR10517:SF8. PTHR10517:SF8. 1 hit.
PfamiPF03024. Folate_rec. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
  2. "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].
    Strain: FVB/N.
    Tissue: Liver.
  3. "Increased expression and genomic organization of a folate-binding protein homologous to the human placental isoform in L1210 murine leukemia cell lines with a defective reduced folate carrier."
    Brigle K.E., Seither R.L., Westin E.H., Goldman I.D.
    J. Biol. Chem. 269:4267-4272(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
  4. "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.
  5. "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.

Entry informationi

Entry nameiFOLR2_MOUSE
AccessioniPrimary (citable) accession number: Q05685
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 8, 2016
This is version 111 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.