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| 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
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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
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| Structure: | |
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Analyze:
| Predict TMSs (Predict number of transmembrane segments) | ||||
| FASTA formatted sequence |
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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
