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9.B.92.1.1
Folate binding receptor, FRα (Jones et al. 2017).

Accession Number:P15328
Protein Name:FRα or FOLR
Length:257
Molecular Weight:29819.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cell membrane1 / Lipid-anchor2
Substrate Unknown

Cross database links:

Genevestigator: P15328
HEGENOM: HBG447315
RefSeq: NP_000793.1    NP_057936.1    NP_057937.1    NP_057941.1   
Entrez Gene ID: 2348   
Pfam: PF03024   
OMIM: 136430  gene
KEGG: hsa:2348   

Gene Ontology

GO:0005576 C:extracellular region
GO:0005887 C:integral to plasma membrane
GO:0005624 C:membrane fraction
GO:0005542 F:folic acid binding
GO:0004872 F:receptor activity
GO:0015884 P:folic acid transport
GO:0006898 P:receptor-mediated endocytosis

References (14)

[1] “Molecular cloning and characterization of the human folate-binding protein cDNA from placenta and malignant tissue culture (KB) cells.”  Elwood P.C.et.al.   2768245
[2] “Complementary DNA for the folate binding protein correctly predicts anchoring to the membrane by glycosyl-phosphatidylinositol.”  Lacey S.W.et.al.   2527252
[3] “Folate-binding protein is a marker for ovarian cancer.”  Campbell I.G.et.al.   1717147
[4] “Cloning of a tumor-associated antigen: MOv18 and MOv19 antibodies recognize a folate-binding protein.”  Coney L.R.et.al.   1840502
[5] “Genomic organization of the gene and a related pseudogene for a human folate binding protein.”  Sadasivan E.et.al.   1581364
[6] “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.”  Elwood P.C.et.al.   9063895
[7] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[8] “The complete amino acid sequence of a human folate binding protein from KB cells determined from the cDNA.”  Sadasivan E.et.al.   2538429
[9] “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.”  Luhrs C.A.et.al.   3476960
[10] “Preferred sites of glycosylphosphatidylinositol modification in folate receptors and constraints in the primary structure of the hydrophobic portion of the signal.”  Yan W.et.al.   7578066
[11] “Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins.”  Elortza F.et.al.   14517339
[12] “Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment.”  Elortza F.et.al.   16602701
[13] “Computational approach for identification and characterization of GPI-anchored peptides in proteomics experiments.”  Omaetxebarria M.J.et.al.   17566972
[14] “Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.”  Picariello G.et.al.   18780401
Structure:
4KM6   4KM7   4KMX   4LRH     

External Searches:

  • Search: DB with
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  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MAQRMTTQLL LLLVWVAVVG EAQTRIAWAR TELLNVCMNA KHHKEKPGPE DKLHEQCRPW 
61:	RKNACCSTNT SQEAHKDVSY LYRFNWNHCG EMAPACKRHF IQDTCLYECS PNLGPWIQQV 
121:	DQSWRKERVL NVPLCKEDCE QWWEDCRTSY TCKSNWHKGW NWTSGFNKCA VGAACQPFHF 
181:	YFPTPTVLCN EIWTHSYKVS NYSRGSGRCI QMWFDPAQGN PNEEVARFYA AAMSGAGPWA 
241:	AWPFLLSLAL MLLWLLS