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Folate receptor alpha (FR-alpha) (Adult folate-binding protein) (FBP) (Folate receptor 1) (Folate receptor, adult) (KB cells FBP) (Ovarian tumor-associated antigen MOv18)

 FOLR1_HUMAN             Reviewed;         257 AA.
P15328; Q53EW2; Q6FGT8; Q6LC90; Q9UCT2;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 3.
10-OCT-2018, entry version 171.
RecName: Full=Folate receptor alpha;
Short=FR-alpha;
AltName: Full=Adult folate-binding protein;
Short=FBP;
AltName: Full=Folate receptor 1;
AltName: Full=Folate receptor, adult;
AltName: Full=KB cells FBP;
AltName: Full=Ovarian tumor-associated antigen MOv18;
Flags: Precursor;
Name=FOLR1; Synonyms=FOLR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR
LOCATION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
PubMed=2768245;
Elwood P.C.;
"Molecular cloning and characterization of the human folate-binding
protein cDNA from placenta and malignant tissue culture (KB) cells.";
J. Biol. Chem. 264:14893-14901(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=2527252; DOI=10.1172/JCI114220;
Lacey S.W., Sanders J.M., Rothberg K.G., Anderson R.G.W., Kamen B.A.;
"Complementary DNA for the folate binding protein correctly predicts
anchoring to the membrane by glycosyl-phosphatidylinositol.";
J. Clin. Invest. 84:715-720(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Ovary;
PubMed=1717147;
Campbell I.G., Jones T.A., Foulkes W.D., Trowsdale J.;
"Folate-binding protein is a marker for ovarian cancer.";
Cancer Res. 51:5329-5338(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 31-56.
TISSUE=Ovarian carcinoma;
PubMed=1840502;
Coney L.R., Tomassetti A., Carayannopoulos L., Frasca V., Kamen B.A.,
Colnaghi M.I., Zurawski V.R. Jr.;
"Cloning of a tumor-associated antigen: MOv18 and MOv19 antibodies
recognize a folate-binding protein.";
Cancer Res. 51:6125-6132(1991).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1581364; DOI=10.1016/0167-4781(92)90103-7;
Sadasivan E., Cedeno M., Rothenberg S.P.;
"Genomic organization of the gene and a related pseudogene for a human
folate binding protein.";
Biochim. Biophys. Acta 1131:91-94(1992).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] OF 1-56,
AND TISSUE SPECIFICITY.
TISSUE=Lymphocyte;
PubMed=9063895; DOI=10.1021/bi962070h;
Elwood P.C., Nachmanoff K., Saikawa Y., Page S.T., Pacheco P.,
Roberts S., Chung K.-N.;
"The divergent 5' termini of the alpha human folate receptor (hFR)
mRNAs originate from two tissue-specific promoters and alternative
splicing: characterization of the alpha hFR gene structure.";
Biochemistry 36:1467-1478(1997).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney proximal tubule;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 24-249.
PubMed=2538429;
Sadasivan E., Rothenberg S.P.;
"The complete amino acid sequence of a human folate binding protein
from KB cells determined from the cDNA.";
J. Biol. Chem. 264:5806-5811(1989).
[13]
PROTEIN SEQUENCE OF 26-43, AND SUBCELLULAR LOCATION.
PubMed=3476960; DOI=10.1073/pnas.84.18.6546;
Luhrs C.A., Pitiranggon P., da Costa M., Rothenberg S.P.,
Slomiany B.L., Brink L., Tous G.I., Stein S.;
"Purified membrane and soluble folate binding proteins from cultured
KB cells have similar amino acid compositions and molecular weights
but differ in fatty acid acylation.";
Proc. Natl. Acad. Sci. U.S.A. 84:6546-6549(1987).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8033114;
Orr R.B., Kamen B.A.;
"UMSCC38 cells amplified at 11q13 for the folate receptor synthesize a
mutant nonfunctional folate receptor.";
Cancer Res. 54:3905-3911(1994).
[15]
GPI-ANCHOR AT SER-234, AND SUBCELLULAR LOCATION.
PubMed=7578066; DOI=10.1021/bi00044a039;
Yan W., Ratnam M.;
"Preferred sites of glycosylphosphatidylinositol modification in
folate receptors and constraints in the primary structure of the
hydrophobic portion of the signal.";
Biochemistry 34:14594-14600(1995).
[16]
FUNCTION, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
PubMed=8567728; DOI=10.1083/jcb.132.1.35;
Rijnboutt S., Jansen G., Posthuma G., Hynes J.B., Schornagel J.H.,
Strous G.J.;
"Endocytosis of GPI-linked membrane folate receptor-alpha.";
J. Cell Biol. 132:35-47(1996).
[17]
GPI-ANCHOR AT SER-234, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17566972; DOI=10.1002/pmic.200700068;
Omaetxebarria M.J., Elortza F., Rodriguez-Suarez E., Aloria K.,
Arizmendi J.M., Jensen O.N., Matthiesen R.;
"Computational approach for identification and characterization of
GPI-anchored peptides in proteomics experiments.";
Proteomics 7:1951-1960(2007).
[18]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-161 AND ASN-201.
TISSUE=Milk;
PubMed=18780401; DOI=10.1002/pmic.200701057;
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
"Identification of N-linked glycoproteins in human milk by hydrophilic
interaction liquid chromatography and mass spectrometry.";
Proteomics 8:3833-3847(2008).
[19]
INVOLVEMENT IN NEURODEGENERATION DUE TO CEREBRAL FOLATE TRANSPORT
DEFICIENCY.
PubMed=19732866; DOI=10.1016/j.ajhg.2009.08.005;
Steinfeld R., Grapp M., Kraetzner R., Dreha-Kulaczewski S., Helms G.,
Dechent P., Wevers R., Grosso S., Gaertner J.;
"Folate receptor alpha defect causes cerebral folate transport
deficiency: a treatable neurodegenerative disorder associated with
disturbed myelin metabolism.";
Am. J. Hum. Genet. 85:354-363(2009).
[20]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-235 IN COMPLEX WITH
FOLATE, FUNCTION, MUTAGENESIS OF TYR-82; ASP-103; TYR-107; TRP-124;
ARG-125; ARG-128; HIS-157; TRP-162 AND SER-196, DISULFIDE BONDS, AND
GLYCOSYLATION AT ASN-69; ASN-161 AND ASN-201.
PubMed=23851396; DOI=10.1038/nature12327;
Chen C., Ke J., Zhou X.E., Yi W., Brunzelle J.S., Li J., Yong E.L.,
Xu H.E., Melcher K.;
"Structural basis for molecular recognition of folic acid by folate
receptors.";
Nature 500:486-489(2013).
[21]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 30-234, FUNCTION,
GLYCOSYLATION AT ASN-69; ASN-161 AND ASN-201, AND DISULFIDE BONDS.
PubMed=23934049; DOI=10.1073/pnas.1308827110;
Wibowo A.S., Singh M., Reeder K.M., Carter J.J., Kovach A.R., Meng W.,
Ratnam M., Zhang F., Dann C.E. III;
"Structures of human folate receptors reveal biological trafficking
states and diversity in folate and antifolate recognition.";
Proc. Natl. Acad. Sci. U.S.A. 110:15180-15188(2013).
-!- 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. {ECO:0000269|PubMed:23851396,
ECO:0000269|PubMed:23934049, ECO:0000269|PubMed:2527252,
ECO:0000269|PubMed:8033114, ECO:0000269|PubMed:8567728}.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
Secreted {ECO:0000305}. Cytoplasmic vesicle. Cytoplasmic vesicle,
clathrin-coated vesicle. Endosome. Apical cell membrane
{ECO:0000250}. Note=Endocytosed into cytoplasmic vesicles and then
recycled to the cell membrane.
-!- TISSUE SPECIFICITY: Primarily expressed in tissues of epithelial
origin. Expression is increased in malignant tissues. Expressed in
kidney, lung and cerebellum. Detected in placenta and thymus
epithelium. {ECO:0000269|PubMed:2527252,
ECO:0000269|PubMed:2768245, ECO:0000269|PubMed:9063895}.
-!- 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.
-!- DISEASE: Neurodegeneration due to cerebral folate transport
deficiency (NCFTD) [MIM:613068]: A neurodegenerative disorder
resulting from brain-specific folate deficiency early in life.
Onset is apparent in late infancy with severe developmental
regression, movement disturbances, epilepsy and leukodystrophy.
{ECO:0000269|PubMed:19732866}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the folate receptor family. {ECO:0000305}.
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EMBL; J05013; AAA35823.1; -; mRNA.
EMBL; M28099; AAA35822.1; -; mRNA.
EMBL; X62753; CAA44610.1; -; mRNA.
EMBL; U20391; AAB05827.1; -; Genomic_DNA.
EMBL; U78793; AAB39751.1; -; mRNA.
EMBL; U78794; AAB39752.1; -; mRNA.
EMBL; BT007158; AAP35822.1; -; mRNA.
EMBL; CR542019; CAG46816.1; -; mRNA.
EMBL; AK223527; BAD97247.1; -; mRNA.
EMBL; CH471076; EAW74848.1; -; Genomic_DNA.
EMBL; BC002947; AAH02947.1; -; mRNA.
EMBL; M25317; AAA74896.1; -; mRNA.
CCDS; CCDS8211.1; -.
PIR; A44904; A45753.
RefSeq; NP_000793.1; NM_000802.3.
RefSeq; NP_057936.1; NM_016724.2.
RefSeq; NP_057937.1; NM_016725.2.
RefSeq; NP_057941.1; NM_016729.2.
UniGene; Hs.73769; -.
PDB; 4KM6; X-ray; 1.55 A; A=30-234.
PDB; 4KM7; X-ray; 1.80 A; A/B=28-234.
PDB; 4KMX; X-ray; 2.20 A; A=28-234.
PDB; 4LRH; X-ray; 2.80 A; A/B/C/D/E/F/G/H=23-235.
PDB; 5IZQ; X-ray; 3.60 A; A/B/C/D/E/F/G/H=1-235.
PDBsum; 4KM6; -.
PDBsum; 4KM7; -.
PDBsum; 4KMX; -.
PDBsum; 4LRH; -.
PDBsum; 5IZQ; -.
ProteinModelPortal; P15328; -.
SMR; P15328; -.
BioGrid; 108631; 13.
IntAct; P15328; 13.
STRING; 9606.ENSP00000308137; -.
BindingDB; P15328; -.
ChEMBL; CHEMBL2121; -.
DrugBank; DB05168; EC145.
DrugBank; DB05595; Farletuzumab.
DrugBank; DB00563; Methotrexate.
TCDB; 9.B.92.1.1; the folate receptor (fr) family.
GlyConnect; 1248; -.
iPTMnet; P15328; -.
BioMuta; FOLR1; -.
DMDM; 544337; -.
EPD; P15328; -.
MaxQB; P15328; -.
PaxDb; P15328; -.
PeptideAtlas; P15328; -.
PRIDE; P15328; -.
ProteomicsDB; 53130; -.
DNASU; 2348; -.
Ensembl; ENST00000312293; ENSP00000308137; ENSG00000110195.
Ensembl; ENST00000393676; ENSP00000377281; ENSG00000110195.
Ensembl; ENST00000393679; ENSP00000377284; ENSG00000110195.
Ensembl; ENST00000393681; ENSP00000377286; ENSG00000110195.
GeneID; 2348; -.
KEGG; hsa:2348; -.
UCSC; uc001orz.3; human.
CTD; 2348; -.
DisGeNET; 2348; -.
EuPathDB; HostDB:ENSG00000110195.11; -.
GeneCards; FOLR1; -.
HGNC; HGNC:3791; FOLR1.
HPA; HPA077030; -.
MalaCards; FOLR1; -.
MIM; 136430; gene.
MIM; 613068; phenotype.
neXtProt; NX_P15328; -.
OpenTargets; ENSG00000110195; -.
Orphanet; 217382; Neurodegenerative syndrome due to cerebral folate transport deficiency.
PharmGKB; PA28207; -.
eggNOG; ENOG410IFFP; Eukaryota.
eggNOG; ENOG4111IU4; LUCA.
GeneTree; ENSGT00390000010470; -.
HOGENOM; HOG000006539; -.
HOVERGEN; HBG039612; -.
InParanoid; P15328; -.
KO; K13649; -.
OMA; WNWTSGF; -.
OrthoDB; EOG091G0GIA; -.
PhylomeDB; P15328; -.
TreeFam; TF328532; -.
Reactome; R-HSA-204005; COPII-mediated vesicle transport.
Reactome; R-HSA-5694530; Cargo concentration in the ER.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
GeneWiki; Folate_receptor_1; -.
GenomeRNAi; 2348; -.
PRO; PR:P15328; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110195; Expressed in 139 organ(s), highest expression level in right uterine tube.
CleanEx; HS_FOLR1; -.
ExpressionAtlas; P15328; baseline and differential.
Genevisible; P15328; HS.
GO; GO:0031362; C:anchored component of external side of plasma membrane; IDA:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IDA:BHF-UCL.
GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
GO; GO:0009986; C:cell surface; HDA:UniProtKB.
GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016020; C:membrane; TAS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:CACAO.
GO; GO:0005886; C:plasma membrane; NAS:UniProtKB.
GO; GO:0030133; C:transport vesicle; TAS:Reactome.
GO; GO:0008144; F:drug binding; IPI:BHF-UCL.
GO; GO:0005542; F:folic acid binding; IDA:UniProtKB.
GO; GO:0061714; F:folic acid receptor activity; IMP:UniProtKB.
GO; GO:0051870; F:methotrexate binding; IDA:BHF-UCL.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0061713; P:anterior neural tube closure; ISS:BHF-UCL.
GO; GO:0031103; P:axon regeneration; ISS:BHF-UCL.
GO; GO:0003253; P:cardiac neural crest cell migration involved in outflow tract morphogenesis; ISS:BHF-UCL.
GO; GO:0071231; P:cellular response to folic acid; IDA:BHF-UCL.
GO; GO:0048208; P:COPII vesicle coating; TAS:Reactome.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:1904447; P:folate import across plasma membrane; IEA:InterPro.
GO; GO:0046655; P:folic acid metabolic process; IEA:Ensembl.
GO; GO:0015884; P:folic acid transport; IMP:UniProtKB.
GO; GO:0001947; P:heart looping; ISS:BHF-UCL.
GO; GO:0003147; P:neural crest cell migration involved in heart formation; ISS:BHF-UCL.
GO; GO:0061626; P:pharyngeal arch artery morphogenesis; ISS:BHF-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:ProtInc.
GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISS:BHF-UCL.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISS:BHF-UCL.
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;
3D-structure; Cell membrane; Complete proteome; Cytoplasmic vesicle;
Direct protein sequencing; Disulfide bond; Endosome; Folate-binding;
Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Neurodegeneration;
Polymorphism; Receptor; Reference proteome; Secreted; Signal;
Transport.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 234 Folate receptor alpha.
/FTId=PRO_0000008802.
PROPEP 235 257 Removed in mature form.
/FTId=PRO_0000008803.
REGION 124 128 Folate binding.
{ECO:0000269|PubMed:23851396}.
REGION 157 162 Folate binding.
{ECO:0000269|PubMed:23851396}.
BINDING 103 103 Folate. {ECO:0000269|PubMed:23851396}.
BINDING 107 107 Folate. {ECO:0000269|PubMed:23851396}.
BINDING 196 196 Folate. {ECO:0000269|PubMed:23851396}.
LIPID 234 234 GPI-anchor amidated serine.
{ECO:0000269|PubMed:17566972,
ECO:0000269|PubMed:7578066}.
CARBOHYD 69 69 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23851396,
ECO:0000269|PubMed:23934049}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401,
ECO:0000269|PubMed:23851396,
ECO:0000269|PubMed:23934049}.
CARBOHYD 201 201 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401,
ECO:0000269|PubMed:23851396,
ECO:0000269|PubMed:23934049}.
DISULFID 37 65 {ECO:0000244|PDB:4KM6,
ECO:0000244|PDB:4KM7,
ECO:0000244|PDB:4KMX,
ECO:0000244|PDB:4LRH,
ECO:0000269|PubMed:23851396,
ECO:0000269|PubMed:23934049}.
DISULFID 57 105 {ECO:0000244|PDB:4KM6,
ECO:0000244|PDB:4KM7,
ECO:0000244|PDB:4KMX,
ECO:0000244|PDB:4LRH,
ECO:0000269|PubMed:23851396,
ECO:0000269|PubMed:23934049}.
DISULFID 66 109 {ECO:0000244|PDB:4KM6,
ECO:0000244|PDB:4KM7,
ECO:0000244|PDB:4KMX,
ECO:0000244|PDB:4LRH,
ECO:0000269|PubMed:23851396,
ECO:0000269|PubMed:23934049}.
DISULFID 89 175 {ECO:0000244|PDB:4KM6,
ECO:0000244|PDB:4KM7,
ECO:0000244|PDB:4KMX,
ECO:0000244|PDB:4LRH,
ECO:0000269|PubMed:23851396,
ECO:0000269|PubMed:23934049}.
DISULFID 96 146 {ECO:0000244|PDB:4KM6,
ECO:0000244|PDB:4KM7,
ECO:0000244|PDB:4KMX,
ECO:0000244|PDB:4LRH,
ECO:0000269|PubMed:23851396,
ECO:0000269|PubMed:23934049}.
DISULFID 135 209 {ECO:0000244|PDB:4KM6,
ECO:0000244|PDB:4KM7,
ECO:0000244|PDB:4KMX,
ECO:0000244|PDB:4LRH,
ECO:0000269|PubMed:23851396,
ECO:0000269|PubMed:23934049}.
DISULFID 139 189 {ECO:0000244|PDB:4KM6,
ECO:0000244|PDB:4KM7,
ECO:0000244|PDB:4KMX,
ECO:0000244|PDB:4LRH,
ECO:0000269|PubMed:23851396,
ECO:0000269|PubMed:23934049}.
DISULFID 152 169 {ECO:0000244|PDB:4KM6,
ECO:0000244|PDB:4KM7,
ECO:0000244|PDB:4KMX,
ECO:0000244|PDB:4LRH,
ECO:0000269|PubMed:23851396,
ECO:0000269|PubMed:23934049}.
VARIANT 28 28 W -> R (in dbSNP:rs7928649).
/FTId=VAR_059284.
VARIANT 160 160 W -> C (in dbSNP:rs1801932).
/FTId=VAR_011963.
MUTAGEN 82 82 Y->A: Slightly reduced affinity for
folate. {ECO:0000269|PubMed:23851396}.
MUTAGEN 103 103 D->A: Strongly reduced affinity for
folate. {ECO:0000269|PubMed:23851396}.
MUTAGEN 107 107 Y->A: Moderately reduced affinity for
folate. {ECO:0000269|PubMed:23851396}.
MUTAGEN 124 124 W->A: Moderately reduced affinity for
folate. {ECO:0000269|PubMed:23851396}.
MUTAGEN 125 125 R->A: Moderately reduced affinity for
folate. {ECO:0000269|PubMed:23851396}.
MUTAGEN 128 128 R->A: Moderately reduced affinity for
folate. {ECO:0000269|PubMed:23851396}.
MUTAGEN 157 157 H->A: Moderately reduced affinity for
folate. {ECO:0000269|PubMed:23851396}.
MUTAGEN 162 162 W->A: Moderately reduced affinity for
folate. {ECO:0000269|PubMed:23851396}.
MUTAGEN 196 196 S->A: Moderately reduced affinity for
folate. {ECO:0000269|PubMed:23851396}.
CONFLICT 180 180 F -> L (in Ref. 9; BAD97247).
{ECO:0000305}.
CONFLICT 184 184 T -> S (in Ref. 12; AAA74896).
{ECO:0000305}.
HELIX 31 33 {ECO:0000244|PDB:4KMX}.
STRAND 48 50 {ECO:0000244|PDB:4KM6}.
TURN 53 56 {ECO:0000244|PDB:4KM6}.
HELIX 58 60 {ECO:0000244|PDB:4KM6}.
STRAND 63 67 {ECO:0000244|PDB:4KM6}.
HELIX 68 73 {ECO:0000244|PDB:4LRH}.
TURN 81 83 {ECO:0000244|PDB:4KM6}.
TURN 86 89 {ECO:0000244|PDB:4KM6}.
HELIX 94 109 {ECO:0000244|PDB:4KM6}.
HELIX 114 116 {ECO:0000244|PDB:4KM6}.
STRAND 117 122 {ECO:0000244|PDB:4LRH}.
STRAND 124 126 {ECO:0000244|PDB:4KM6}.
HELIX 136 145 {ECO:0000244|PDB:4KM6}.
TURN 146 148 {ECO:0000244|PDB:4KM6}.
STRAND 150 152 {ECO:0000244|PDB:4KM6}.
STRAND 156 158 {ECO:0000244|PDB:4LRH}.
HELIX 172 174 {ECO:0000244|PDB:4LRH}.
HELIX 178 181 {ECO:0000244|PDB:4KM6}.
HELIX 185 191 {ECO:0000244|PDB:4KM6}.
TURN 192 195 {ECO:0000244|PDB:4KM6}.
STRAND 206 210 {ECO:0000244|PDB:4KM6}.
HELIX 216 218 {ECO:0000244|PDB:4KM6}.
HELIX 222 232 {ECO:0000244|PDB:4KM6}.
SEQUENCE 257 AA; 29819 MW; D458D8BB047C96A6 CRC64;
MAQRMTTQLL LLLVWVAVVG EAQTRIAWAR TELLNVCMNA KHHKEKPGPE DKLHEQCRPW
RKNACCSTNT SQEAHKDVSY LYRFNWNHCG EMAPACKRHF IQDTCLYECS PNLGPWIQQV
DQSWRKERVL NVPLCKEDCE QWWEDCRTSY TCKSNWHKGW NWTSGFNKCA VGAACQPFHF
YFPTPTVLCN EIWTHSYKVS NYSRGSGRCI QMWFDPAQGN PNEEVARFYA AAMSGAGPWA
AWPFLLSLAL MLLWLLS


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