Full text data of TFRC
TFRC
[Confidence: low (only semi-automatic identification from reviews)]
Transferrin receptor protein 1; TR; TfR; TfR1; Trfr (T9; p90; CD71; Transferrin receptor protein 1, serum form; sTfR)
Transferrin receptor protein 1; TR; TfR; TfR1; Trfr (T9; p90; CD71; Transferrin receptor protein 1, serum form; sTfR)
UniProt
P02786
ID TFR1_HUMAN Reviewed; 760 AA.
AC P02786; D3DXB0; Q1HE24; Q59G55; Q9UCN0; Q9UCU5; Q9UDF9; Q9UK21;
read moreDT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 22-JAN-2014, entry version 176.
DE RecName: Full=Transferrin receptor protein 1;
DE Short=TR;
DE Short=TfR;
DE Short=TfR1;
DE Short=Trfr;
DE AltName: Full=T9;
DE AltName: Full=p90;
DE AltName: CD_antigen=CD71;
DE Contains:
DE RecName: Full=Transferrin receptor protein 1, serum form;
DE Short=sTfR;
GN Name=TFRC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-142.
RX PubMed=6090955; DOI=10.1038/311675b0;
RA Schneider C., Owen M.J., Banville D., Williams J.G.;
RT "Primary structure of human transferrin receptor deduced from the mRNA
RT sequence.";
RL Nature 311:675-678(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-142.
RX PubMed=6094009; DOI=10.1016/0092-8674(84)90004-7;
RA McClelland A., Kuhn L.C., Ruddle F.H.;
RT "The human transferrin receptor gene: genomic organization, and the
RT complete primary structure of the receptor deduced from a cDNA
RT sequence.";
RL Cell 39:267-274(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=9358047; DOI=10.1016/S0378-1119(97)00356-9;
RA Evans P., Kemp J.;
RT "Exon/intron structure of the human transferrin receptor gene.";
RL Gene 199:123-131(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RA Wheeler D.L.;
RT "Molecular and evolutionary studies of the transferrin receptor.";
RL Thesis (1999), University of Iowa, United States.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 101-119 (STFR).
RX PubMed=2229063;
RA Shih Y.J., Baynes R.D., Hudson B.G., Flowers C.H., Skikne B.S.,
RA Cook J.D.;
RT "Serum transferrin receptor is a truncated form of tissue receptor.";
RL J. Biol. Chem. 265:19077-19081(1990).
RN [10]
RP PROTEIN SEQUENCE OF 101-123 (STFR), AND CHARACTERIZATION.
RC TISSUE=Erythroleukemia;
RX PubMed=1871153;
RA Baynes R.D., Shih Y.J., Hudson B.G., Cook J.D.;
RT "Characterization of transferrin receptor released by K562
RT erythroleukemia cells.";
RL Proc. Soc. Exp. Biol. Med. 197:416-423(1991).
RN [11]
RP PROTEIN SEQUENCE OF 288-302; 694-708 AND 721-730.
RC TISSUE=Prostatic carcinoma;
RX PubMed=7864799;
RA Coppolino M., Migliorini M., Argraves W.S., Dedhar S.;
RT "Identification of a novel form of the alpha 3 integrin subunit:
RT covalent association with transferrin receptor.";
RL Biochem. J. 306:129-134(1995).
RN [12]
RP PROTEIN SEQUENCE OF 680-696.
RX PubMed=1380674; DOI=10.1038/358764a0;
RA Chicz R.M., Urban R.G., Lane W.S., Gorga J.C., Stern L.J.,
RA Vignali D.A.A., Strominger J.L.;
RT "Predominant naturally processed peptides bound to HLA-DR1 are derived
RT from MHC-related molecules and are heterogeneous in size.";
RL Nature 358:764-768(1992).
RN [13]
RP FUNCTION.
RX PubMed=3568132; DOI=10.1016/0092-8674(87)90295-9;
RA Rothenberger S., Iacopetta B.J., Kuhn L.C.;
RT "Endocytosis of the transferrin receptor requires the cytoplasmic
RT domain but not its phosphorylation site.";
RL Cell 49:423-431(1987).
RN [14]
RP PALMITOYLATION AT CYS-62.
RX PubMed=3582362;
RA Jing S., Trowbridge I.S.;
RT "Identification of the intermolecular disulfide bonds of the human
RT transferrin receptor and its lipid-attachment site.";
RL EMBO J. 6:327-331(1987).
RN [15]
RP MUTAGENESIS OF CYSTEINE RESIDUES INVOLVED IN INTERMOLECULAR BONDS.
RX PubMed=2507316;
RA Alvarez E., Girones N., Davis R.J.;
RT "Intermolecular disulfide bonds are not required for the expression of
RT the dimeric state and functional activity of the transferrin
RT receptor.";
RL EMBO J. 8:2231-2240(1989).
RN [16]
RP MUTAGENESIS OF TYR-20.
RX PubMed=2327986;
RA Alvarez E., Girones N., Davis R.J.;
RT "A point mutation in the cytoplasmic domain of the transferrin
RT receptor inhibits endocytosis.";
RL Biochem. J. 267:31-35(1990).
RN [17]
RP INTERNALIZATION SEQUENCE, AND MUTAGENESIS OF TYR-20.
RX PubMed=2298808; DOI=10.1083/jcb.110.2.283;
RA Jing S., Spencer T., Miller K., Hopkins C., Trowbridge I.S.;
RT "Role of the human transferrin receptor cytoplasmic domain in
RT endocytosis: localization of a specific signal sequence for
RT internalization.";
RL J. Cell Biol. 110:283-294(1990).
RN [18]
RP GLYCOSYLATION AT THR-104.
RX PubMed=1421756; DOI=10.1093/glycob/2.4.345;
RA Do S.-I., Cummings R.D.;
RT "Presence of O-linked oligosaccharide on a threonine residue in the
RT human transferrin receptor.";
RL Glycobiology 2:345-353(1992).
RN [19]
RP GLYCOSYLATION AT THR-104.
RX PubMed=1421757; DOI=10.1093/glycob/2.4.355;
RA Hayes G.R., Enns C.A., Lucas J.J.;
RT "Identification of the O-linked glycosylation site of the human
RT transferrin receptor.";
RL Glycobiology 2:355-359(1992).
RN [20]
RP MUTAGENESIS OF 20-TYR--PHE-23; TYR-20; THR-21 AND PHE-23.
RX PubMed=8408022;
RA Collawn J.F., Lai A., Domingo D.L., Fitch M., Hatton S.,
RA Trowbridge I.S.;
RT "YTRF is the conserved internalization signal of the transferrin
RT receptor, and a second YTRF signal at position 31-34 enhances
RT endocytosis.";
RL J. Biol. Chem. 268:21686-21692(1993).
RN [21]
RP STRUCTURE OF CARBOHYDRATES ON ASN-727.
RX PubMed=7780197; DOI=10.1093/glycob/5.2.227;
RA Hayes G.R., Williams A., Costello C.E., Enns C.A., Lucas J.J.;
RT "The critical glycosylation site of human transferrin receptor
RT contains a high-mannose oligosaccharide.";
RL Glycobiology 5:227-232(1995).
RN [22]
RP IDENTIFICATION OF LIGAND-BINDING DOMAIN.
RX PubMed=8631371; DOI=10.1111/j.1432-1033.1996.0009u.x;
RA Buchegger F., Trowbridge I.S., Liu L.F., White S., Collawn J.F.;
RT "Functional analysis of human/chicken transferrin receptor chimeras
RT indicates that the carboxy-terminal region is important for ligand
RT binding.";
RL Eur. J. Biochem. 235:9-17(1996).
RN [23]
RP MUTAGENESIS OF ARG-646; GLY-647 AND ASP-648.
RX PubMed=10377239; DOI=10.1042/0264-6021:3410011;
RA Dubljevic V., Sali A., Goding J.W.;
RT "A conserved RGD (Arg-Gly-Asp) motif in the transferrin receptor is
RT required for binding to transferrin.";
RL Biochem. J. 341:11-14(1999).
RN [24]
RP MUTAGENESIS.
RX PubMed=11800564; DOI=10.1006/jmbi.2001.5048;
RA West A.P. Jr., Giannetti A.M., Herr A.B., Bennett M.J., Nangiana J.S.,
RA Pierce J.R., Weiner L.P., Snow P.M., Bjorkman P.J.;
RT "Mutational analysis of the transferrin receptor reveals overlapping
RT HFE and transferrin binding sites.";
RL J. Mol. Biol. 313:385-397(2001).
RN [25]
RP INTERACTION WITH SH3BP4.
RX PubMed=16325581; DOI=10.1016/j.cell.2005.10.021;
RA Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P.,
RA Tacchetti C., Di Fiore P.P.;
RT "TTP specifically regulates the internalization of the transferrin
RT receptor.";
RL Cell 123:875-888(2005).
RN [26]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-251, AND MASS
RP SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [28]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [29]
RP INTERACTION WITH MACHUPO ARENAVIRUS PROTEIN GPC.
RX PubMed=17287727; DOI=10.1038/nature05539;
RA Radoshitzky S.R., Abraham J., Spiropoulou C.F., Kuhn J.H., Nguyen D.,
RA Li W., Nagel J., Schmidt P.J., Nunberg J.H., Andrews N.C., Farzan M.,
RA Choe H.;
RT "Transferrin receptor 1 is a cellular receptor for New World
RT haemorrhagic fever arenaviruses.";
RL Nature 446:92-96(2007).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [31]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-251 AND ASN-727, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [32]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-251, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-
RT linked cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [33]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [35]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [36]
RP ELECTRON MICROSCOPY.
RX PubMed=9782058; DOI=10.1016/S0969-2126(98)00124-5;
RA Fuchs H., Luecken W., Tauber R., Engel A.;
RT "Structural model of phospholipid-reconstituted human transferrin
RT receptor derived by electron microscopy.";
RL Structure 6:1235-1243(1998).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 121-760.
RX PubMed=10531064; DOI=10.1126/science.286.5440.779;
RA Lawrence C.M., Ray S., Babyonyshev M., Galluser R., Borhani D.W.,
RA Harrison S.C.;
RT "Crystal structure of the ectodomain of human transferrin receptor.";
RL Science 286:779-782(1999).
RN [38]
RP VARIANT SER-142.
RX PubMed=11702220; DOI=10.1007/s004390100599;
RA Douabin-Gicquel V., Soriano N., Ferran H., Wojcik F., Palierne E.,
RA Tamim S., Jovelin T., McKie A.T., Le Gall J.-Y., David V., Mosser J.;
RT "Identification of 96 single nucleotide polymorphisms in eight genes
RT involved in iron metabolism: efficiency of bioinformatic extraction
RT compared with a systematic sequencing approach.";
RL Hum. Genet. 109:393-401(2001).
CC -!- FUNCTION: Cellular uptake of iron occurs via receptor-mediated
CC endocytosis of ligand-occupied transferrin receptor into
CC specialized endosomes. Endosomal acidification leads to iron
CC release. The apotransferrin-receptor complex is then recycled to
CC the cell surface with a return to neutral pH and the concomitant
CC loss of affinity of apotransferrin for its receptor. Transferrin
CC receptor is necessary for development of erythrocytes and the
CC nervous system (By similarity). A second ligand, the heditary
CC hemochromatosis protein HFE, competes for binding with transferrin
CC for an overlapping C-terminal binding site.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Binds one transferrin or HFE
CC molecule per subunit. Binds the HLA class II histocompatibility
CC antigen, DR1. Interacts with SH3BP3. Interacts with Machupo
CC arenavirus GPC.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-355727, EBI-355727;
CC P02768:ALB; NbExp=2; IntAct=EBI-355727, EBI-714423;
CC Q9P0V3:SH3BP4; NbExp=6; IntAct=EBI-355727, EBI-1049513;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein. Melanosome. Note=Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV.
CC -!- SUBCELLULAR LOCATION: Transferrin receptor protein 1, serum form:
CC Secreted.
CC -!- INDUCTION: Regulated by cellular iron levels through binding of
CC the iron regulatory proteins, IRP1 and IRP2, to iron-responsive
CC elements in the 3'-UTR. Up-regulated upon mitogenic stimulation.
CC -!- PTM: N- and O-glycosylated, phosphorylated and palmitoylated. The
CC serum form is only glycosylated.
CC -!- PTM: Proteolytically cleaved on Arg-100 to produce the soluble
CC serum form (sTfR).
CC -!- PTM: Palmitoylated on both Cys-62 and Cys-67. Cys-62 seems to be
CC the major site of palmitoylation.
CC -!- MISCELLANEOUS: Serum transferrin receptor (sTfR) is used as a
CC means of detecting erythropoietin (EPO) misuse by athletes and as
CC a diagnostic test for anemia resulting from a number of conditions
CC including rheumatoid arthritis, pregnancy, irritable bowel
CC syndrome and in HIV patients.
CC -!- MISCELLANEOUS: Canine and feline parvoviruses bind human and
CC feline transferrin receptors and use these receptors to enter and
CC infect cells.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC -!- SIMILARITY: Contains 1 PA (protease associated) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92491.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TFRCID259ch3q29.html";
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DR EMBL; X01060; CAA25527.1; -; mRNA.
DR EMBL; M11507; AAA61153.1; -; mRNA.
DR EMBL; AF187320; AAF04564.1; -; Genomic_DNA.
DR EMBL; AB209254; BAD92491.1; ALT_INIT; mRNA.
DR EMBL; DQ496099; ABF47088.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53670.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53673.1; -; Genomic_DNA.
DR EMBL; BC001188; AAH01188.1; -; mRNA.
DR PIR; A93343; JXHU.
DR RefSeq; NP_001121620.1; NM_001128148.1.
DR RefSeq; NP_003225.2; NM_003234.2.
DR UniGene; Hs.529618; -.
DR PDB; 1CX8; X-ray; 3.20 A; A/B/C/D/E/F/G/H=122-760.
DR PDB; 1DE4; X-ray; 2.80 A; C/F/I=121-760.
DR PDB; 1SUV; EM; 7.50 A; A/B=122-760.
DR PDB; 2NSU; EM; 27.00 A; A/B=122-760.
DR PDB; 3KAS; X-ray; 2.40 A; A=121-760.
DR PDB; 3S9L; X-ray; 3.22 A; A/B=120-760.
DR PDB; 3S9M; X-ray; 3.32 A; A/B=120-760.
DR PDB; 3S9N; X-ray; 3.25 A; A/B=120-760.
DR PDBsum; 1CX8; -.
DR PDBsum; 1DE4; -.
DR PDBsum; 1SUV; -.
DR PDBsum; 2NSU; -.
DR PDBsum; 3KAS; -.
DR PDBsum; 3S9L; -.
DR PDBsum; 3S9M; -.
DR PDBsum; 3S9N; -.
DR ProteinModelPortal; P02786; -.
DR SMR; P02786; 122-756.
DR DIP; DIP-2736N; -.
DR IntAct; P02786; 23.
DR MINT; MINT-4999032; -.
DR STRING; 9606.ENSP00000353224; -.
DR MEROPS; M28.972; -.
DR PhosphoSite; P02786; -.
DR UniCarbKB; P02786; -.
DR DMDM; 108935939; -.
DR PaxDb; P02786; -.
DR PeptideAtlas; P02786; -.
DR PRIDE; P02786; -.
DR DNASU; 7037; -.
DR Ensembl; ENST00000360110; ENSP00000353224; ENSG00000072274.
DR Ensembl; ENST00000392396; ENSP00000376197; ENSG00000072274.
DR GeneID; 7037; -.
DR KEGG; hsa:7037; -.
DR UCSC; uc003fvz.4; human.
DR CTD; 7037; -.
DR GeneCards; GC03M195754; -.
DR HGNC; HGNC:11763; TFRC.
DR HPA; CAB000153; -.
DR HPA; HPA028598; -.
DR MIM; 190010; gene.
DR neXtProt; NX_P02786; -.
DR PharmGKB; PA36478; -.
DR eggNOG; COG2234; -.
DR HOVERGEN; HBG023177; -.
DR InParanoid; P02786; -.
DR KO; K06503; -.
DR OMA; DNSHVEM; -.
DR PhylomeDB; P02786; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR ChiTaRS; TFRC; human.
DR EvolutionaryTrace; P02786; -.
DR GeneWiki; TFRC; -.
DR GenomeRNAi; 7037; -.
DR NextBio; 27493; -.
DR PRO; PR:P02786; -.
DR ArrayExpress; P02786; -.
DR Bgee; P02786; -.
DR CleanEx; HS_TFRC; -.
DR Genevestigator; P02786; -.
DR GO; GO:0005905; C:coated pit; IDA:UniProtKB.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0004998; F:transferrin receptor activity; NAS:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; NAS:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR Gene3D; 1.20.930.40; -; 1.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR003137; Protease-assoc_domain.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF47672; SSF47672; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Endocytosis; Glycoprotein;
KW Host-virus interaction; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Polymorphism; Receptor; Reference proteome; Secreted;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1 760 Transferrin receptor protein 1.
FT /FTId=PRO_0000174132.
FT CHAIN 101 760 Transferrin receptor protein 1, serum
FT form.
FT /FTId=PRO_0000292265.
FT TOPO_DOM 1 67 Cytoplasmic (Potential).
FT TRANSMEM 68 88 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 89 760 Extracellular (Potential).
FT DOMAIN 223 313 PA.
FT REGION 1 67 Mediates interaction with SH3BP4.
FT REGION 569 760 Ligand-binding.
FT MOTIF 20 23 Endocytosis signal.
FT MOTIF 58 61 Stop-transfer sequence.
FT MOTIF 646 648 Cell attachment site; required for
FT binding to transferrin.
FT SITE 100 101 Cleavage; by trypsin; to produce soluble
FT form.
FT MOD_RES 20 20 Phosphotyrosine.
FT MOD_RES 21 21 Phosphothreonine.
FT MOD_RES 24 24 Phosphoserine.
FT LIPID 62 62 S-palmitoyl cysteine.
FT LIPID 67 67 S-palmitoyl cysteine.
FT CARBOHYD 104 104 O-linked (GalNAc...).
FT /FTId=CAR_000072.
FT CARBOHYD 251 251 N-linked (GlcNAc...).
FT CARBOHYD 317 317 N-linked (GlcNAc...).
FT CARBOHYD 727 727 N-linked (GlcNAc...).
FT /FTId=CAR_000173.
FT DISULFID 89 89 Interchain.
FT DISULFID 98 98 Interchain.
FT VARIANT 142 142 G -> S (rare polymorphism;
FT dbSNP:rs3817672).
FT /FTId=VAR_012737.
FT VARIANT 212 212 L -> V (in dbSNP:rs41301381).
FT /FTId=VAR_051806.
FT VARIANT 420 420 G -> S (in dbSNP:rs41295879).
FT /FTId=VAR_051807.
FT VARIANT 677 677 R -> H (in dbSNP:rs41298067).
FT /FTId=VAR_051808.
FT MUTAGEN 9 12 FSNL->YTRF: Only 80% as active as wild-
FT type receptor.
FT MUTAGEN 20 34 YTRFSLARQVDGDNS->PPGYSLARQVDYTRF: No
FT influence on endocytic uptake of the
FT receptor.
FT MUTAGEN 20 23 YTRF->PPGY: Only 16% as active as wild-
FT type receptor.
FT MUTAGEN 20 20 Y->C: Only 35% as active as wild-type
FT receptor.
FT MUTAGEN 20 20 Y->G: Only 20% as active as wild-type
FT receptor.
FT MUTAGEN 21 21 T->F: Only 88% as active as wild-type
FT receptor.
FT MUTAGEN 21 21 T->TA: Only 14% as active as wild-type
FT receptor.
FT MUTAGEN 21 21 T->TAA: Only 19% as active as wild-type
FT receptor.
FT MUTAGEN 23 23 F->Y: Only 48% as active as wild-type
FT receptor.
FT MUTAGEN 31 34 GDNS->YTRF: 2-fold increase of the
FT endocytic uptake of the receptor.
FT MUTAGEN 47 50 NADN->YTRF: 1.27-fold increase of the
FT endocytic uptake of the receptor.
FT MUTAGEN 619 619 L->A: 20-fold reduced affinity for
FT transferrin receptor. No binding to HFE.
FT MUTAGEN 622 622 V->A: No significant effect on binding to
FT transferrin nor HFE.
FT MUTAGEN 623 623 R->A: No significant effect on binding to
FT transferrin nor HFE.
FT MUTAGEN 629 629 R->A: >5-fold reduced affinity for
FT transferrin. >10-fold reduced affinity
FT for HFE.
FT MUTAGEN 640 640 Q->A: No effect on binding to
FT transferrin. >10-fold reduced affinity
FT for HFE.
FT MUTAGEN 641 641 W->A: No significant effect on binding to
FT transferrin nor HFE.
FT MUTAGEN 643 643 Y->A: 20-fold reduced affinity for
FT transferrin. No binding to HFE.
FT MUTAGEN 644 644 S->A: No significant effect on binding to
FT transferrin nor HFE.
FT MUTAGEN 646 646 R->A,H: No binding to transferrin.
FT MUTAGEN 646 646 R->K: 5% binding to transferrin.
FT MUTAGEN 647 647 G->A: Large effect on affinity for
FT transferrin. 4-fold reduced affinity for
FT HFE.
FT MUTAGEN 648 648 D->A: 16% binding to transferrin.
FT MUTAGEN 648 648 D->E: 57% binding to transferrin.
FT MUTAGEN 650 650 F->Q: >5-fold reduced affinity for
FT transferrin. >10-fold reduced affinity
FT for HFE.
FT CONFLICT 104 104 T -> K (in Ref. 10; AA sequence).
FT CONFLICT 109 109 R -> V (in Ref. 10; AA sequence).
FT CONFLICT 123 123 Y -> T (in Ref. 10; AA sequence).
FT HELIX 124 136
FT HELIX 140 146
FT TURN 150 152
FT HELIX 160 176
FT STRAND 179 192
FT STRAND 199 204
FT TURN 205 208
FT STRAND 209 214
FT STRAND 220 222
FT STRAND 226 230
FT STRAND 232 234
FT TURN 236 238
FT HELIX 240 244
FT STRAND 245 248
FT STRAND 253 259
FT HELIX 264 272
FT TURN 273 275
FT STRAND 277 282
FT TURN 285 287
FT STRAND 303 306
FT STRAND 308 310
FT STRAND 311 313
FT HELIX 317 319
FT STRAND 334 336
FT HELIX 339 346
FT STRAND 349 352
FT HELIX 355 357
FT STRAND 364 367
FT STRAND 371 377
FT STRAND 380 393
FT STRAND 396 408
FT STRAND 411 413
FT TURN 416 419
FT HELIX 420 438
FT STRAND 445 455
FT HELIX 456 458
FT HELIX 461 469
FT TURN 470 473
FT HELIX 474 476
FT STRAND 478 483
FT STRAND 491 498
FT HELIX 500 502
FT HELIX 503 510
FT TURN 516 518
FT STRAND 520 522
FT HELIX 528 531
FT HELIX 541 546
FT STRAND 552 558
FT TURN 564 567
FT HELIX 573 579
FT HELIX 583 603
FT STRAND 604 606
FT HELIX 613 625
FT HELIX 626 628
FT TURN 629 636
FT HELIX 640 662
FT HELIX 668 680
FT HELIX 682 685
FT STRAND 688 690
FT TURN 692 694
FT TURN 700 702
FT STRAND 705 708
FT HELIX 709 717
FT TURN 718 722
FT HELIX 728 749
FT HELIX 753 755
SQ SEQUENCE 760 AA; 84871 MW; C886F14000D90154 CRC64;
MMDQARSAFS NLFGGEPLSY TRFSLARQVD GDNSHVEMKL AVDEEENADN NTKANVTKPK
RCSGSICYGT IAVIVFFLIG FMIGYLGYCK GVEPKTECER LAGTESPVRE EPGEDFPAAR
RLYWDDLKRK LSEKLDSTDF TGTIKLLNEN SYVPREAGSQ KDENLALYVE NQFREFKLSK
VWRDQHFVKI QVKDSAQNSV IIVDKNGRLV YLVENPGGYV AYSKAATVTG KLVHANFGTK
KDFEDLYTPV NGSIVIVRAG KITFAEKVAN AESLNAIGVL IYMDQTKFPI VNAELSFFGH
AHLGTGDPYT PGFPSFNHTQ FPPSRSSGLP NIPVQTISRA AAEKLFGNME GDCPSDWKTD
STCRMVTSES KNVKLTVSNV LKEIKILNIF GVIKGFVEPD HYVVVGAQRD AWGPGAAKSG
VGTALLLKLA QMFSDMVLKD GFQPSRSIIF ASWSAGDFGS VGATEWLEGY LSSLHLKAFT
YINLDKAVLG TSNFKVSASP LLYTLIEKTM QNVKHPVTGQ FLYQDSNWAS KVEKLTLDNA
AFPFLAYSGI PAVSFCFCED TDYPYLGTTM DTYKELIERI PELNKVARAA AEVAGQFVIK
LTHDVELNLD YERYNSQLLS FVRDLNQYRA DIKEMGLSLQ WLYSARGDFF RATSRLTTDF
GNAEKTDRFV MKKLNDRVMR VEYHFLSPYV SPKESPFRHV FWGSGSHTLP ALLENLKLRK
QNNGAFNETL FRNQLALATW TIQGAANALS GDVWDIDNEF
//
ID TFR1_HUMAN Reviewed; 760 AA.
AC P02786; D3DXB0; Q1HE24; Q59G55; Q9UCN0; Q9UCU5; Q9UDF9; Q9UK21;
read moreDT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 22-JAN-2014, entry version 176.
DE RecName: Full=Transferrin receptor protein 1;
DE Short=TR;
DE Short=TfR;
DE Short=TfR1;
DE Short=Trfr;
DE AltName: Full=T9;
DE AltName: Full=p90;
DE AltName: CD_antigen=CD71;
DE Contains:
DE RecName: Full=Transferrin receptor protein 1, serum form;
DE Short=sTfR;
GN Name=TFRC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-142.
RX PubMed=6090955; DOI=10.1038/311675b0;
RA Schneider C., Owen M.J., Banville D., Williams J.G.;
RT "Primary structure of human transferrin receptor deduced from the mRNA
RT sequence.";
RL Nature 311:675-678(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-142.
RX PubMed=6094009; DOI=10.1016/0092-8674(84)90004-7;
RA McClelland A., Kuhn L.C., Ruddle F.H.;
RT "The human transferrin receptor gene: genomic organization, and the
RT complete primary structure of the receptor deduced from a cDNA
RT sequence.";
RL Cell 39:267-274(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=9358047; DOI=10.1016/S0378-1119(97)00356-9;
RA Evans P., Kemp J.;
RT "Exon/intron structure of the human transferrin receptor gene.";
RL Gene 199:123-131(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RA Wheeler D.L.;
RT "Molecular and evolutionary studies of the transferrin receptor.";
RL Thesis (1999), University of Iowa, United States.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 101-119 (STFR).
RX PubMed=2229063;
RA Shih Y.J., Baynes R.D., Hudson B.G., Flowers C.H., Skikne B.S.,
RA Cook J.D.;
RT "Serum transferrin receptor is a truncated form of tissue receptor.";
RL J. Biol. Chem. 265:19077-19081(1990).
RN [10]
RP PROTEIN SEQUENCE OF 101-123 (STFR), AND CHARACTERIZATION.
RC TISSUE=Erythroleukemia;
RX PubMed=1871153;
RA Baynes R.D., Shih Y.J., Hudson B.G., Cook J.D.;
RT "Characterization of transferrin receptor released by K562
RT erythroleukemia cells.";
RL Proc. Soc. Exp. Biol. Med. 197:416-423(1991).
RN [11]
RP PROTEIN SEQUENCE OF 288-302; 694-708 AND 721-730.
RC TISSUE=Prostatic carcinoma;
RX PubMed=7864799;
RA Coppolino M., Migliorini M., Argraves W.S., Dedhar S.;
RT "Identification of a novel form of the alpha 3 integrin subunit:
RT covalent association with transferrin receptor.";
RL Biochem. J. 306:129-134(1995).
RN [12]
RP PROTEIN SEQUENCE OF 680-696.
RX PubMed=1380674; DOI=10.1038/358764a0;
RA Chicz R.M., Urban R.G., Lane W.S., Gorga J.C., Stern L.J.,
RA Vignali D.A.A., Strominger J.L.;
RT "Predominant naturally processed peptides bound to HLA-DR1 are derived
RT from MHC-related molecules and are heterogeneous in size.";
RL Nature 358:764-768(1992).
RN [13]
RP FUNCTION.
RX PubMed=3568132; DOI=10.1016/0092-8674(87)90295-9;
RA Rothenberger S., Iacopetta B.J., Kuhn L.C.;
RT "Endocytosis of the transferrin receptor requires the cytoplasmic
RT domain but not its phosphorylation site.";
RL Cell 49:423-431(1987).
RN [14]
RP PALMITOYLATION AT CYS-62.
RX PubMed=3582362;
RA Jing S., Trowbridge I.S.;
RT "Identification of the intermolecular disulfide bonds of the human
RT transferrin receptor and its lipid-attachment site.";
RL EMBO J. 6:327-331(1987).
RN [15]
RP MUTAGENESIS OF CYSTEINE RESIDUES INVOLVED IN INTERMOLECULAR BONDS.
RX PubMed=2507316;
RA Alvarez E., Girones N., Davis R.J.;
RT "Intermolecular disulfide bonds are not required for the expression of
RT the dimeric state and functional activity of the transferrin
RT receptor.";
RL EMBO J. 8:2231-2240(1989).
RN [16]
RP MUTAGENESIS OF TYR-20.
RX PubMed=2327986;
RA Alvarez E., Girones N., Davis R.J.;
RT "A point mutation in the cytoplasmic domain of the transferrin
RT receptor inhibits endocytosis.";
RL Biochem. J. 267:31-35(1990).
RN [17]
RP INTERNALIZATION SEQUENCE, AND MUTAGENESIS OF TYR-20.
RX PubMed=2298808; DOI=10.1083/jcb.110.2.283;
RA Jing S., Spencer T., Miller K., Hopkins C., Trowbridge I.S.;
RT "Role of the human transferrin receptor cytoplasmic domain in
RT endocytosis: localization of a specific signal sequence for
RT internalization.";
RL J. Cell Biol. 110:283-294(1990).
RN [18]
RP GLYCOSYLATION AT THR-104.
RX PubMed=1421756; DOI=10.1093/glycob/2.4.345;
RA Do S.-I., Cummings R.D.;
RT "Presence of O-linked oligosaccharide on a threonine residue in the
RT human transferrin receptor.";
RL Glycobiology 2:345-353(1992).
RN [19]
RP GLYCOSYLATION AT THR-104.
RX PubMed=1421757; DOI=10.1093/glycob/2.4.355;
RA Hayes G.R., Enns C.A., Lucas J.J.;
RT "Identification of the O-linked glycosylation site of the human
RT transferrin receptor.";
RL Glycobiology 2:355-359(1992).
RN [20]
RP MUTAGENESIS OF 20-TYR--PHE-23; TYR-20; THR-21 AND PHE-23.
RX PubMed=8408022;
RA Collawn J.F., Lai A., Domingo D.L., Fitch M., Hatton S.,
RA Trowbridge I.S.;
RT "YTRF is the conserved internalization signal of the transferrin
RT receptor, and a second YTRF signal at position 31-34 enhances
RT endocytosis.";
RL J. Biol. Chem. 268:21686-21692(1993).
RN [21]
RP STRUCTURE OF CARBOHYDRATES ON ASN-727.
RX PubMed=7780197; DOI=10.1093/glycob/5.2.227;
RA Hayes G.R., Williams A., Costello C.E., Enns C.A., Lucas J.J.;
RT "The critical glycosylation site of human transferrin receptor
RT contains a high-mannose oligosaccharide.";
RL Glycobiology 5:227-232(1995).
RN [22]
RP IDENTIFICATION OF LIGAND-BINDING DOMAIN.
RX PubMed=8631371; DOI=10.1111/j.1432-1033.1996.0009u.x;
RA Buchegger F., Trowbridge I.S., Liu L.F., White S., Collawn J.F.;
RT "Functional analysis of human/chicken transferrin receptor chimeras
RT indicates that the carboxy-terminal region is important for ligand
RT binding.";
RL Eur. J. Biochem. 235:9-17(1996).
RN [23]
RP MUTAGENESIS OF ARG-646; GLY-647 AND ASP-648.
RX PubMed=10377239; DOI=10.1042/0264-6021:3410011;
RA Dubljevic V., Sali A., Goding J.W.;
RT "A conserved RGD (Arg-Gly-Asp) motif in the transferrin receptor is
RT required for binding to transferrin.";
RL Biochem. J. 341:11-14(1999).
RN [24]
RP MUTAGENESIS.
RX PubMed=11800564; DOI=10.1006/jmbi.2001.5048;
RA West A.P. Jr., Giannetti A.M., Herr A.B., Bennett M.J., Nangiana J.S.,
RA Pierce J.R., Weiner L.P., Snow P.M., Bjorkman P.J.;
RT "Mutational analysis of the transferrin receptor reveals overlapping
RT HFE and transferrin binding sites.";
RL J. Mol. Biol. 313:385-397(2001).
RN [25]
RP INTERACTION WITH SH3BP4.
RX PubMed=16325581; DOI=10.1016/j.cell.2005.10.021;
RA Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P.,
RA Tacchetti C., Di Fiore P.P.;
RT "TTP specifically regulates the internalization of the transferrin
RT receptor.";
RL Cell 123:875-888(2005).
RN [26]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-251, AND MASS
RP SPECTROMETRY.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
RA Moore R.J., Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [28]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [29]
RP INTERACTION WITH MACHUPO ARENAVIRUS PROTEIN GPC.
RX PubMed=17287727; DOI=10.1038/nature05539;
RA Radoshitzky S.R., Abraham J., Spiropoulou C.F., Kuhn J.H., Nguyen D.,
RA Li W., Nagel J., Schmidt P.J., Nunberg J.H., Andrews N.C., Farzan M.,
RA Choe H.;
RT "Transferrin receptor 1 is a cellular receptor for New World
RT haemorrhagic fever arenaviruses.";
RL Nature 446:92-96(2007).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [31]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-251 AND ASN-727, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [32]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-251, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-
RT linked cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [33]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [35]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [36]
RP ELECTRON MICROSCOPY.
RX PubMed=9782058; DOI=10.1016/S0969-2126(98)00124-5;
RA Fuchs H., Luecken W., Tauber R., Engel A.;
RT "Structural model of phospholipid-reconstituted human transferrin
RT receptor derived by electron microscopy.";
RL Structure 6:1235-1243(1998).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 121-760.
RX PubMed=10531064; DOI=10.1126/science.286.5440.779;
RA Lawrence C.M., Ray S., Babyonyshev M., Galluser R., Borhani D.W.,
RA Harrison S.C.;
RT "Crystal structure of the ectodomain of human transferrin receptor.";
RL Science 286:779-782(1999).
RN [38]
RP VARIANT SER-142.
RX PubMed=11702220; DOI=10.1007/s004390100599;
RA Douabin-Gicquel V., Soriano N., Ferran H., Wojcik F., Palierne E.,
RA Tamim S., Jovelin T., McKie A.T., Le Gall J.-Y., David V., Mosser J.;
RT "Identification of 96 single nucleotide polymorphisms in eight genes
RT involved in iron metabolism: efficiency of bioinformatic extraction
RT compared with a systematic sequencing approach.";
RL Hum. Genet. 109:393-401(2001).
CC -!- FUNCTION: Cellular uptake of iron occurs via receptor-mediated
CC endocytosis of ligand-occupied transferrin receptor into
CC specialized endosomes. Endosomal acidification leads to iron
CC release. The apotransferrin-receptor complex is then recycled to
CC the cell surface with a return to neutral pH and the concomitant
CC loss of affinity of apotransferrin for its receptor. Transferrin
CC receptor is necessary for development of erythrocytes and the
CC nervous system (By similarity). A second ligand, the heditary
CC hemochromatosis protein HFE, competes for binding with transferrin
CC for an overlapping C-terminal binding site.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Binds one transferrin or HFE
CC molecule per subunit. Binds the HLA class II histocompatibility
CC antigen, DR1. Interacts with SH3BP3. Interacts with Machupo
CC arenavirus GPC.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-355727, EBI-355727;
CC P02768:ALB; NbExp=2; IntAct=EBI-355727, EBI-714423;
CC Q9P0V3:SH3BP4; NbExp=6; IntAct=EBI-355727, EBI-1049513;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein. Melanosome. Note=Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV.
CC -!- SUBCELLULAR LOCATION: Transferrin receptor protein 1, serum form:
CC Secreted.
CC -!- INDUCTION: Regulated by cellular iron levels through binding of
CC the iron regulatory proteins, IRP1 and IRP2, to iron-responsive
CC elements in the 3'-UTR. Up-regulated upon mitogenic stimulation.
CC -!- PTM: N- and O-glycosylated, phosphorylated and palmitoylated. The
CC serum form is only glycosylated.
CC -!- PTM: Proteolytically cleaved on Arg-100 to produce the soluble
CC serum form (sTfR).
CC -!- PTM: Palmitoylated on both Cys-62 and Cys-67. Cys-62 seems to be
CC the major site of palmitoylation.
CC -!- MISCELLANEOUS: Serum transferrin receptor (sTfR) is used as a
CC means of detecting erythropoietin (EPO) misuse by athletes and as
CC a diagnostic test for anemia resulting from a number of conditions
CC including rheumatoid arthritis, pregnancy, irritable bowel
CC syndrome and in HIV patients.
CC -!- MISCELLANEOUS: Canine and feline parvoviruses bind human and
CC feline transferrin receptors and use these receptors to enter and
CC infect cells.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
CC -!- SIMILARITY: Contains 1 PA (protease associated) domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92491.1; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TFRCID259ch3q29.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; X01060; CAA25527.1; -; mRNA.
DR EMBL; M11507; AAA61153.1; -; mRNA.
DR EMBL; AF187320; AAF04564.1; -; Genomic_DNA.
DR EMBL; AB209254; BAD92491.1; ALT_INIT; mRNA.
DR EMBL; DQ496099; ABF47088.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53670.1; -; Genomic_DNA.
DR EMBL; CH471191; EAW53673.1; -; Genomic_DNA.
DR EMBL; BC001188; AAH01188.1; -; mRNA.
DR PIR; A93343; JXHU.
DR RefSeq; NP_001121620.1; NM_001128148.1.
DR RefSeq; NP_003225.2; NM_003234.2.
DR UniGene; Hs.529618; -.
DR PDB; 1CX8; X-ray; 3.20 A; A/B/C/D/E/F/G/H=122-760.
DR PDB; 1DE4; X-ray; 2.80 A; C/F/I=121-760.
DR PDB; 1SUV; EM; 7.50 A; A/B=122-760.
DR PDB; 2NSU; EM; 27.00 A; A/B=122-760.
DR PDB; 3KAS; X-ray; 2.40 A; A=121-760.
DR PDB; 3S9L; X-ray; 3.22 A; A/B=120-760.
DR PDB; 3S9M; X-ray; 3.32 A; A/B=120-760.
DR PDB; 3S9N; X-ray; 3.25 A; A/B=120-760.
DR PDBsum; 1CX8; -.
DR PDBsum; 1DE4; -.
DR PDBsum; 1SUV; -.
DR PDBsum; 2NSU; -.
DR PDBsum; 3KAS; -.
DR PDBsum; 3S9L; -.
DR PDBsum; 3S9M; -.
DR PDBsum; 3S9N; -.
DR ProteinModelPortal; P02786; -.
DR SMR; P02786; 122-756.
DR DIP; DIP-2736N; -.
DR IntAct; P02786; 23.
DR MINT; MINT-4999032; -.
DR STRING; 9606.ENSP00000353224; -.
DR MEROPS; M28.972; -.
DR PhosphoSite; P02786; -.
DR UniCarbKB; P02786; -.
DR DMDM; 108935939; -.
DR PaxDb; P02786; -.
DR PeptideAtlas; P02786; -.
DR PRIDE; P02786; -.
DR DNASU; 7037; -.
DR Ensembl; ENST00000360110; ENSP00000353224; ENSG00000072274.
DR Ensembl; ENST00000392396; ENSP00000376197; ENSG00000072274.
DR GeneID; 7037; -.
DR KEGG; hsa:7037; -.
DR UCSC; uc003fvz.4; human.
DR CTD; 7037; -.
DR GeneCards; GC03M195754; -.
DR HGNC; HGNC:11763; TFRC.
DR HPA; CAB000153; -.
DR HPA; HPA028598; -.
DR MIM; 190010; gene.
DR neXtProt; NX_P02786; -.
DR PharmGKB; PA36478; -.
DR eggNOG; COG2234; -.
DR HOVERGEN; HBG023177; -.
DR InParanoid; P02786; -.
DR KO; K06503; -.
DR OMA; DNSHVEM; -.
DR PhylomeDB; P02786; -.
DR Reactome; REACT_11123; Membrane Trafficking.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR ChiTaRS; TFRC; human.
DR EvolutionaryTrace; P02786; -.
DR GeneWiki; TFRC; -.
DR GenomeRNAi; 7037; -.
DR NextBio; 27493; -.
DR PRO; PR:P02786; -.
DR ArrayExpress; P02786; -.
DR Bgee; P02786; -.
DR CleanEx; HS_TFRC; -.
DR Genevestigator; P02786; -.
DR GO; GO:0005905; C:coated pit; IDA:UniProtKB.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0004998; F:transferrin receptor activity; NAS:UniProtKB.
DR GO; GO:0006879; P:cellular iron ion homeostasis; NAS:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0033572; P:transferrin transport; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR Gene3D; 1.20.930.40; -; 1.
DR InterPro; IPR007484; Peptidase_M28.
DR InterPro; IPR003137; Protease-assoc_domain.
DR InterPro; IPR007365; TFR-like_dimer_dom.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
DR Pfam; PF04253; TFR_dimer; 1.
DR SUPFAM; SSF47672; SSF47672; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Endocytosis; Glycoprotein;
KW Host-virus interaction; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Polymorphism; Receptor; Reference proteome; Secreted;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1 760 Transferrin receptor protein 1.
FT /FTId=PRO_0000174132.
FT CHAIN 101 760 Transferrin receptor protein 1, serum
FT form.
FT /FTId=PRO_0000292265.
FT TOPO_DOM 1 67 Cytoplasmic (Potential).
FT TRANSMEM 68 88 Helical; Signal-anchor for type II
FT membrane protein; (Potential).
FT TOPO_DOM 89 760 Extracellular (Potential).
FT DOMAIN 223 313 PA.
FT REGION 1 67 Mediates interaction with SH3BP4.
FT REGION 569 760 Ligand-binding.
FT MOTIF 20 23 Endocytosis signal.
FT MOTIF 58 61 Stop-transfer sequence.
FT MOTIF 646 648 Cell attachment site; required for
FT binding to transferrin.
FT SITE 100 101 Cleavage; by trypsin; to produce soluble
FT form.
FT MOD_RES 20 20 Phosphotyrosine.
FT MOD_RES 21 21 Phosphothreonine.
FT MOD_RES 24 24 Phosphoserine.
FT LIPID 62 62 S-palmitoyl cysteine.
FT LIPID 67 67 S-palmitoyl cysteine.
FT CARBOHYD 104 104 O-linked (GalNAc...).
FT /FTId=CAR_000072.
FT CARBOHYD 251 251 N-linked (GlcNAc...).
FT CARBOHYD 317 317 N-linked (GlcNAc...).
FT CARBOHYD 727 727 N-linked (GlcNAc...).
FT /FTId=CAR_000173.
FT DISULFID 89 89 Interchain.
FT DISULFID 98 98 Interchain.
FT VARIANT 142 142 G -> S (rare polymorphism;
FT dbSNP:rs3817672).
FT /FTId=VAR_012737.
FT VARIANT 212 212 L -> V (in dbSNP:rs41301381).
FT /FTId=VAR_051806.
FT VARIANT 420 420 G -> S (in dbSNP:rs41295879).
FT /FTId=VAR_051807.
FT VARIANT 677 677 R -> H (in dbSNP:rs41298067).
FT /FTId=VAR_051808.
FT MUTAGEN 9 12 FSNL->YTRF: Only 80% as active as wild-
FT type receptor.
FT MUTAGEN 20 34 YTRFSLARQVDGDNS->PPGYSLARQVDYTRF: No
FT influence on endocytic uptake of the
FT receptor.
FT MUTAGEN 20 23 YTRF->PPGY: Only 16% as active as wild-
FT type receptor.
FT MUTAGEN 20 20 Y->C: Only 35% as active as wild-type
FT receptor.
FT MUTAGEN 20 20 Y->G: Only 20% as active as wild-type
FT receptor.
FT MUTAGEN 21 21 T->F: Only 88% as active as wild-type
FT receptor.
FT MUTAGEN 21 21 T->TA: Only 14% as active as wild-type
FT receptor.
FT MUTAGEN 21 21 T->TAA: Only 19% as active as wild-type
FT receptor.
FT MUTAGEN 23 23 F->Y: Only 48% as active as wild-type
FT receptor.
FT MUTAGEN 31 34 GDNS->YTRF: 2-fold increase of the
FT endocytic uptake of the receptor.
FT MUTAGEN 47 50 NADN->YTRF: 1.27-fold increase of the
FT endocytic uptake of the receptor.
FT MUTAGEN 619 619 L->A: 20-fold reduced affinity for
FT transferrin receptor. No binding to HFE.
FT MUTAGEN 622 622 V->A: No significant effect on binding to
FT transferrin nor HFE.
FT MUTAGEN 623 623 R->A: No significant effect on binding to
FT transferrin nor HFE.
FT MUTAGEN 629 629 R->A: >5-fold reduced affinity for
FT transferrin. >10-fold reduced affinity
FT for HFE.
FT MUTAGEN 640 640 Q->A: No effect on binding to
FT transferrin. >10-fold reduced affinity
FT for HFE.
FT MUTAGEN 641 641 W->A: No significant effect on binding to
FT transferrin nor HFE.
FT MUTAGEN 643 643 Y->A: 20-fold reduced affinity for
FT transferrin. No binding to HFE.
FT MUTAGEN 644 644 S->A: No significant effect on binding to
FT transferrin nor HFE.
FT MUTAGEN 646 646 R->A,H: No binding to transferrin.
FT MUTAGEN 646 646 R->K: 5% binding to transferrin.
FT MUTAGEN 647 647 G->A: Large effect on affinity for
FT transferrin. 4-fold reduced affinity for
FT HFE.
FT MUTAGEN 648 648 D->A: 16% binding to transferrin.
FT MUTAGEN 648 648 D->E: 57% binding to transferrin.
FT MUTAGEN 650 650 F->Q: >5-fold reduced affinity for
FT transferrin. >10-fold reduced affinity
FT for HFE.
FT CONFLICT 104 104 T -> K (in Ref. 10; AA sequence).
FT CONFLICT 109 109 R -> V (in Ref. 10; AA sequence).
FT CONFLICT 123 123 Y -> T (in Ref. 10; AA sequence).
FT HELIX 124 136
FT HELIX 140 146
FT TURN 150 152
FT HELIX 160 176
FT STRAND 179 192
FT STRAND 199 204
FT TURN 205 208
FT STRAND 209 214
FT STRAND 220 222
FT STRAND 226 230
FT STRAND 232 234
FT TURN 236 238
FT HELIX 240 244
FT STRAND 245 248
FT STRAND 253 259
FT HELIX 264 272
FT TURN 273 275
FT STRAND 277 282
FT TURN 285 287
FT STRAND 303 306
FT STRAND 308 310
FT STRAND 311 313
FT HELIX 317 319
FT STRAND 334 336
FT HELIX 339 346
FT STRAND 349 352
FT HELIX 355 357
FT STRAND 364 367
FT STRAND 371 377
FT STRAND 380 393
FT STRAND 396 408
FT STRAND 411 413
FT TURN 416 419
FT HELIX 420 438
FT STRAND 445 455
FT HELIX 456 458
FT HELIX 461 469
FT TURN 470 473
FT HELIX 474 476
FT STRAND 478 483
FT STRAND 491 498
FT HELIX 500 502
FT HELIX 503 510
FT TURN 516 518
FT STRAND 520 522
FT HELIX 528 531
FT HELIX 541 546
FT STRAND 552 558
FT TURN 564 567
FT HELIX 573 579
FT HELIX 583 603
FT STRAND 604 606
FT HELIX 613 625
FT HELIX 626 628
FT TURN 629 636
FT HELIX 640 662
FT HELIX 668 680
FT HELIX 682 685
FT STRAND 688 690
FT TURN 692 694
FT TURN 700 702
FT STRAND 705 708
FT HELIX 709 717
FT TURN 718 722
FT HELIX 728 749
FT HELIX 753 755
SQ SEQUENCE 760 AA; 84871 MW; C886F14000D90154 CRC64;
MMDQARSAFS NLFGGEPLSY TRFSLARQVD GDNSHVEMKL AVDEEENADN NTKANVTKPK
RCSGSICYGT IAVIVFFLIG FMIGYLGYCK GVEPKTECER LAGTESPVRE EPGEDFPAAR
RLYWDDLKRK LSEKLDSTDF TGTIKLLNEN SYVPREAGSQ KDENLALYVE NQFREFKLSK
VWRDQHFVKI QVKDSAQNSV IIVDKNGRLV YLVENPGGYV AYSKAATVTG KLVHANFGTK
KDFEDLYTPV NGSIVIVRAG KITFAEKVAN AESLNAIGVL IYMDQTKFPI VNAELSFFGH
AHLGTGDPYT PGFPSFNHTQ FPPSRSSGLP NIPVQTISRA AAEKLFGNME GDCPSDWKTD
STCRMVTSES KNVKLTVSNV LKEIKILNIF GVIKGFVEPD HYVVVGAQRD AWGPGAAKSG
VGTALLLKLA QMFSDMVLKD GFQPSRSIIF ASWSAGDFGS VGATEWLEGY LSSLHLKAFT
YINLDKAVLG TSNFKVSASP LLYTLIEKTM QNVKHPVTGQ FLYQDSNWAS KVEKLTLDNA
AFPFLAYSGI PAVSFCFCED TDYPYLGTTM DTYKELIERI PELNKVARAA AEVAGQFVIK
LTHDVELNLD YERYNSQLLS FVRDLNQYRA DIKEMGLSLQ WLYSARGDFF RATSRLTTDF
GNAEKTDRFV MKKLNDRVMR VEYHFLSPYV SPKESPFRHV FWGSGSHTLP ALLENLKLRK
QNNGAFNETL FRNQLALATW TIQGAANALS GDVWDIDNEF
//
MIM
190010
*RECORD*
*FIELD* NO
190010
*FIELD* TI
*190010 TRANSFERRIN RECEPTOR; TFRC
;;TRANSFERRIN RECEPTOR 1; TFR1;;
TFR;;
TRFR;;
CD71
read more*FIELD* TX
CLONING
A monoclonal antibody, OKT-9, recognizes an antigen ubiquitously
distributed on the cell surface of actively growing human cells. It is a
glycoprotein composed of disulfide-linked polypeptide chains, each of
90,000 daltons molecular weight. Immunoprecipitation of the OKT-9
antigen in the presence of labeled transferrin results in specific
precipitation of transferrin (Sutherland et al., 1981); thus, the OKT-9
antigen is presumably transferrin receptor. Nikinmaa and Schroder (1987)
concluded that p90 and TFRC are the same protein: studies using
monoclonal antibodies indicated that exhaustive precipitation of
radioactively labeled lysates with one antibody removed all activity of
lysates with the other. Peptide maps of antigens recognized with both
antibodies showed great similarity and indicated that both antibodies
react with the same antigen, the human transferrin receptor, but with
different antigenic sites of the molecule.
GENE FUNCTION
Casey et al. (1988) analyzed the regulation by iron of the TFRC gene by
examining mouse cells transformed with chimeric constructs containing
the human transferrin receptor gene's promoter and either the structural
gene for bacterial chloramphenicol acetyltransferase or the human TFRC
cDNA. They concluded that at least 2 genetic elements, one 5-prime and
one 3-prime to the gene, are involved in the regulation of the TFRC gene
by iron.
Radoshitzky et al. (2007) demonstrated a specific high-affinity
association between TFR1 and the entry glycoprotein of Machupo virus (a
New World arenavirus). Expression of human TFR1, but not human TFR2
(604720), in hamster cell lines markedly enhanced the infection of
viruses pseudotyped with the glycoprotein of Machupo, Guanarito, and
Junin viruses, but not with those of Lassa or lymphocytic
choriomeningitis viruses. An anti-TFR1 antibody efficiently inhibited
the replication of Machupo, Guanarito, Junin, and Sabia viruses, but not
that of Lassa virus. Iron depletion of culture medium enhanced, and iron
supplementation decreased, the efficiency of infection by Junin and
Machupo but not Lassa pseudoviruses. Radoshitzky et al. (2007) concluded
that TFR1 is a cellular receptor for New World hemorrhagic fever
arenaviruses.
Ishii et al. (2009) found that knockdown of Ppargc1b (608886) in primary
mouse osteoclasts impaired their differentiation and mitochondrial
biogenesis. Transferrin receptor expression was induced in osteoclasts
via iron regulatory protein-2 (IREB2; 147582), and Tfrc-mediated iron
uptake promoted osteoclast differentiation and bone-resorbing activity,
which was associated with the induction of mitochondrial respiration,
production of reactive oxygen species, and accelerated Ppargc1b
transcription. Iron chelation inhibited osteoclastic bone resorption and
protected female mice against bone loss following estrogen deficiency
resulting from ovariectomy. Ishii et al. (2009) concluded that
mitochondrial biogenesis, which is induced by PPARGC1B and supported by
TFRC-mediated iron uptake for utilization by mitochondrial respiratory
proteins, is fundamental to osteoclast activation and bone metabolism.
Elahi et al. (2013) showed that physiologically enriched CD71+ erythroid
cells in neonatal mice and human cord blood have distinctive
immunosuppressive properties. The production of innate immune protective
cytokines by adult cells is diminished after transfer to neonatal mice
or after coculture with neonatal splenocytes. Neonatal CD71+ cells
express the enzyme arginase-2 (ARG2; 107830), and arginase activity is
essential for the immunosuppressive properties of these cells because
molecular inhibition of this enzyme or supplementation with L-arginine
overrides immunosuppression. In addition, the ablation of CD71+ cells in
neonatal mice, or the decline in number of these cells as postnatal
development progresses, parallels the loss of suppression and restored
resistance to the perinatal pathogens Listeria monocytogenes and E.
coli. However, CD71+ cell-mediated susceptibility to infection is
counterbalanced by CD71+ cell-mediated protection against aberrant
immune cell activation in the intestine, where colonization with
commensal microorganisms occurs swiftly after parturition. Conversely,
circumventing such colonization by using antimicrobials or gnotobiotic
germ-free mice overrides these protective benefits. Elahi et al. (2013)
thus concluded that CD71+ cells quench the excessive inflammation
induced by abrupt colonization with commensal microorganisms after
parturition. The authors further suggested that this finding challenged
the idea that the susceptibility of neonates to infection reflects
immune cell-intrinsic defects and instead highlights processes that are
developmentally more essential and that inadvertently mitigate innate
immune protection.
MAPPING
By somatic cell hybrid studies, Goodfellow et al. (1982) assigned the
TFR locus to chromosome 3. Miller et al. (1983) confirmed the assignment
to chromosome 3, specifically 3q22-qter. By in situ hybridization, Rabin
et al. (1985) narrowed the assignment to 3q26.2-qter. Adriaansen et al.
(1990) confirmed the assignment to chromosome 3 by study of somatic cell
hybrids. Using linkage analysis, somatic cell hybrid and radiation
hybrid mapping panels, and fluorescence in situ hybridization, Kashuba
et al. (1997) refined the localization of the TFRC gene to 3q29.
Valenzuela et al. (1991) found highly significant association between Rh
(111700) phenotypes and total iron binding capacity, i.e., transferrin.
Children with the C Rh specificity had higher values than non-C or c
individuals. Valenzuela et al. (1991) suggested that this finding may be
significant in relation to maintenance of the Rh polymorphism and
fetomaternal incompatibility.
BIOCHEMICAL FEATURES
Athletes such as racing cyclists sometimes use erythropoietin, which has
been officially included in the International Olympic Committee list of
banned substances since 1990, as a booster drug. Gareau et al. (1994)
presented evidence that the level of transferrin receptor in the blood
can be used as a means of detecting Epo misuse.
ANIMAL MODEL
Levy et al. (1999) disrupted the transferrin receptor gene, which they
termed Trfr, in mice. Homozygous mutant mice were not viable beyond
embryonic day 12.5 and had severe anemia with hydrops as well as diffuse
neurologic abnormalities. There was some variation of onset of severe
anemia, and in nonanemic embryos without tissue edema and necrosis
(E9.5), both stressed erythropoiesis and neurologic abnormalities were
apparent. The authors concluded that inadequate iron led to neuronal
apoptosis, but that tissues other than erythrocytes and neurons can
obtain sufficient iron for growth and development through mechanisms
independent of the transferrin cycle. Haploinsufficiency for the
transferrin receptor resulted in microcytic, hypochromic erythrocytes;
normal hemoglobin and hematocrit values were due to compensatory
increase in red cell numbers. Although iron saturation of serum
transferrin was indistinguishable from that of wildtype, heterozygotes
had significantly less tissue iron.
*FIELD* SA
Enns et al. (1982); Larrick and Hyman (1984); Newman et al. (1982);
Omary and Trowbridge (1981); Schneider et al. (1983); Schneider et
al. (1984); Vodinelich et al. (1983)
*FIELD* RF
1. Adriaansen, H. J.; Geurts Van Kessel, A. H. M.; Wijdenes-De Bresser,
J. H. F. M.; Van Drunen-Schoenmaker, E.; Van Dongen, J. J. M.: Expression
of the myeloid differentiation antigen CD33 depends on the presence
of human chromosome 19 in human-mouse hybrids. Ann. Hum. Genet. 54:
115-119, 1990.
2. Casey, J. L.; Di Jeso, B.; Rao, K.; Klausner, R. D.; Harford, J.
B.: Two genetic loci participate in the regulation by iron of the
gene for the human transferrin receptor. Proc. Nat. Acad. Sci. 85:
1787-1791, 1988.
3. Elahi, S.; Ertelt, J. M.; Kinder, J. M.; Jiang, T. T.; Zhang, X.;
Xin, L.; Chaturvedi, V.; Strong, B. S.; Qualls, J. E.; Steinbrecher,
K. A.; Kalfa, T. A.; Shaaban, A. F.; Way, S. S.: Immunosuppressive
CD71+ erythroid cells compromise neonatal host defence against infection. Nature 504:
158-162, 2013.
4. Enns, C. A.; Suomalainen, H. A.; Gebhardt, J. E.; Schroder, J.;
Sussman, H. H.: Human transferrin receptor: expression of the receptor
is assigned to chromosome 3. Proc. Nat. Acad. Sci. 79: 3241-3245,
1982.
5. Gareau, R.; Gagnon, M. G.; Thellend, C.; Chenard, C.; Audran, M.;
Chanal, J.-L.; Ayotte, C.; Brisson, G. R.: Transferrin soluble receptor:
a possible probe for detection of erythropoietin abuse by athletes. Horm.
Metab. Res. 26: 311-312, 1994.
6. Goodfellow, P. N.; Banting, G.; Sutherland, R.; Greaves, M.; Solomon,
E.; Povey, S.: Expression of human transferrin receptor is controlled
by a gene on chromosome 3: assignment using species specificity of
a monoclonal antibody. Somat. Cell Genet. 8: 197-206, 1982.
7. Ishii, K.; Fumoto, T.; Iwai, K.; Takeshita, S.; Ito, M.; Shimohata,
N.; Aburatani, H.; Taketani, S.; Lelliott, C. J.; Vidal-Puig, A.;
Ikeda, K.: Coordination of PGC-1-beta and iron uptake in mitochondrial
biogenesis and osteoclast activation. Nature Med. 15: 259-266, 2009.
8. Kashuba, V. I.; Gizatullin, R. Z.; Protopopov, A. I.; Allikmets,
R.; Korolev, S.; Li, J.; Boldog, F.; Tory, K.; Zabarovska, V.; Marcsek,
Z.; Sumegi, J.; Klein, G.; Zabarovsky, E. R.; Kisselev, L.: NotI
linking/jumping clones of human chromosome 3: mapping of the TFRC,
RAB7 and HAUSP genes to regions rearranged in leukemia and deleted
in solid tumors. FEBS Lett. 419: 181-185, 1997.
9. Larrick, J. W.; Hyman, E. S.: Acquired iron-deficiency anemia
caused by an antibody against the transferrin receptor. New Eng.
J. Med. 311: 214-218, 1984.
10. Levy, J. E.; Jin, O.; Fujiwara, Y.; Kuo, F.; Andrews, N. C.:
Transferrin receptor is necessary for development of erythrocytes
and the nervous system. Nature Genet. 21: 396-399, 1999.
11. Miller, Y. E.; Jones, C.; Scoggin, C.; Morse, H.; Seligman, P.
: Chromosome 3q (22-ter) encodes the human transferrin receptor. Am.
J. Hum. Genet. 35: 573-583, 1983.
12. Newman, R.; Schneider, C.; Sutherland, R.; Vodinelich, L.; Greaves,
M.: The transferrin receptor. Trends Biochem. Sci. 7: 397-400,
1982.
13. Nikinmaa, B.; Schroder, J.: Two antigens, the transferrin receptor
and p90 assigned to human chromosome 3, are probably the same protein. Hereditas 107:
55-58, 1987.
14. Omary, M. B.; Trowbridge, I. S.: Biosynthesis of the human transferrin
receptor in cultured cells. J. Biol. Chem. 256: 12888-12892, 1981.
15. Rabin, M.; McClelland, A.; Kuhn, L.; Ruddle, F. H.: Regional
localization of the human transferrin receptor gene to 3q26.2-qter. Am.
J. Hum. Genet. 37: 1112-1116, 1985.
16. Radoshitzky, S. R.; Abraham, J.; Spiropoulou, C. F.; Kuhn, J.
H.; Nguyen, D.; Li, W.; Nagel, J.; Schmidt, P. J.; Nunberg, J. H.;
Andrews, N. C.; Farzan, M.; Choe, H.: Transferrin receptor 1 is a
cellular receptor for New World haemorrhagic fever arenaviruses. Nature 446:
92-96, 2007.
17. Schneider, C.; Kurkinen, M.; Greaves, M.: Isolation of cDNA clones
for the human transferrin receptor. EMBO J. 2: 2259-2263, 1983.
18. Schneider, C.; Owen, M. J.; Banville, D.; Williams, J. G.: Primary
structure of human transferrin receptor deduced from the mRNA sequence. Nature 311:
675-678, 1984.
19. Sutherland, R.; Delia, D.; Schneider, C.; Newman, R.; Kemshead,
J.; Greaves, M.: Ubiquitous cell-surface glycoprotein on tumor cells
is proliferation-associated receptor for transferrin. Proc. Nat.
Acad. Sci. 78: 4515-4519, 1981.
20. Valenzuela, C. Y.; Avendano, A.; Harb, Z.: Association between
Rh and plasma iron binding (transferrin). Hum. Genet. 87: 438-440,
1991.
21. Vodinelich, L.; Sutherland, R.; Schneider, C.; Newman, R.; Greaves,
M.: Receptor for transferrin may be a 'target' structure for natural
killer cells. Proc. Nat. Acad. Sci. 80: 835-839, 1983.
*FIELD* CN
Ada Hamosh - updated: 02/05/2014
Patricia A. Hartz - updated: 6/8/2009
Ada Hamosh - updated: 6/20/2007
Ada Hamosh - updated: 3/30/1999
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
alopez: 02/05/2014
wwang: 6/11/2009
terry: 6/8/2009
carol: 4/23/2008
alopez: 6/27/2007
terry: 6/20/2007
joanna: 3/14/2007
alopez: 3/30/1999
terry: 6/5/1998
dholmes: 4/14/1998
alopez: 2/26/1998
carol: 9/20/1994
supermim: 3/16/1992
carol: 2/22/1992
carol: 10/18/1991
carol: 10/16/1991
carol: 10/5/1990
*RECORD*
*FIELD* NO
190010
*FIELD* TI
*190010 TRANSFERRIN RECEPTOR; TFRC
;;TRANSFERRIN RECEPTOR 1; TFR1;;
TFR;;
TRFR;;
CD71
read more*FIELD* TX
CLONING
A monoclonal antibody, OKT-9, recognizes an antigen ubiquitously
distributed on the cell surface of actively growing human cells. It is a
glycoprotein composed of disulfide-linked polypeptide chains, each of
90,000 daltons molecular weight. Immunoprecipitation of the OKT-9
antigen in the presence of labeled transferrin results in specific
precipitation of transferrin (Sutherland et al., 1981); thus, the OKT-9
antigen is presumably transferrin receptor. Nikinmaa and Schroder (1987)
concluded that p90 and TFRC are the same protein: studies using
monoclonal antibodies indicated that exhaustive precipitation of
radioactively labeled lysates with one antibody removed all activity of
lysates with the other. Peptide maps of antigens recognized with both
antibodies showed great similarity and indicated that both antibodies
react with the same antigen, the human transferrin receptor, but with
different antigenic sites of the molecule.
GENE FUNCTION
Casey et al. (1988) analyzed the regulation by iron of the TFRC gene by
examining mouse cells transformed with chimeric constructs containing
the human transferrin receptor gene's promoter and either the structural
gene for bacterial chloramphenicol acetyltransferase or the human TFRC
cDNA. They concluded that at least 2 genetic elements, one 5-prime and
one 3-prime to the gene, are involved in the regulation of the TFRC gene
by iron.
Radoshitzky et al. (2007) demonstrated a specific high-affinity
association between TFR1 and the entry glycoprotein of Machupo virus (a
New World arenavirus). Expression of human TFR1, but not human TFR2
(604720), in hamster cell lines markedly enhanced the infection of
viruses pseudotyped with the glycoprotein of Machupo, Guanarito, and
Junin viruses, but not with those of Lassa or lymphocytic
choriomeningitis viruses. An anti-TFR1 antibody efficiently inhibited
the replication of Machupo, Guanarito, Junin, and Sabia viruses, but not
that of Lassa virus. Iron depletion of culture medium enhanced, and iron
supplementation decreased, the efficiency of infection by Junin and
Machupo but not Lassa pseudoviruses. Radoshitzky et al. (2007) concluded
that TFR1 is a cellular receptor for New World hemorrhagic fever
arenaviruses.
Ishii et al. (2009) found that knockdown of Ppargc1b (608886) in primary
mouse osteoclasts impaired their differentiation and mitochondrial
biogenesis. Transferrin receptor expression was induced in osteoclasts
via iron regulatory protein-2 (IREB2; 147582), and Tfrc-mediated iron
uptake promoted osteoclast differentiation and bone-resorbing activity,
which was associated with the induction of mitochondrial respiration,
production of reactive oxygen species, and accelerated Ppargc1b
transcription. Iron chelation inhibited osteoclastic bone resorption and
protected female mice against bone loss following estrogen deficiency
resulting from ovariectomy. Ishii et al. (2009) concluded that
mitochondrial biogenesis, which is induced by PPARGC1B and supported by
TFRC-mediated iron uptake for utilization by mitochondrial respiratory
proteins, is fundamental to osteoclast activation and bone metabolism.
Elahi et al. (2013) showed that physiologically enriched CD71+ erythroid
cells in neonatal mice and human cord blood have distinctive
immunosuppressive properties. The production of innate immune protective
cytokines by adult cells is diminished after transfer to neonatal mice
or after coculture with neonatal splenocytes. Neonatal CD71+ cells
express the enzyme arginase-2 (ARG2; 107830), and arginase activity is
essential for the immunosuppressive properties of these cells because
molecular inhibition of this enzyme or supplementation with L-arginine
overrides immunosuppression. In addition, the ablation of CD71+ cells in
neonatal mice, or the decline in number of these cells as postnatal
development progresses, parallels the loss of suppression and restored
resistance to the perinatal pathogens Listeria monocytogenes and E.
coli. However, CD71+ cell-mediated susceptibility to infection is
counterbalanced by CD71+ cell-mediated protection against aberrant
immune cell activation in the intestine, where colonization with
commensal microorganisms occurs swiftly after parturition. Conversely,
circumventing such colonization by using antimicrobials or gnotobiotic
germ-free mice overrides these protective benefits. Elahi et al. (2013)
thus concluded that CD71+ cells quench the excessive inflammation
induced by abrupt colonization with commensal microorganisms after
parturition. The authors further suggested that this finding challenged
the idea that the susceptibility of neonates to infection reflects
immune cell-intrinsic defects and instead highlights processes that are
developmentally more essential and that inadvertently mitigate innate
immune protection.
MAPPING
By somatic cell hybrid studies, Goodfellow et al. (1982) assigned the
TFR locus to chromosome 3. Miller et al. (1983) confirmed the assignment
to chromosome 3, specifically 3q22-qter. By in situ hybridization, Rabin
et al. (1985) narrowed the assignment to 3q26.2-qter. Adriaansen et al.
(1990) confirmed the assignment to chromosome 3 by study of somatic cell
hybrids. Using linkage analysis, somatic cell hybrid and radiation
hybrid mapping panels, and fluorescence in situ hybridization, Kashuba
et al. (1997) refined the localization of the TFRC gene to 3q29.
Valenzuela et al. (1991) found highly significant association between Rh
(111700) phenotypes and total iron binding capacity, i.e., transferrin.
Children with the C Rh specificity had higher values than non-C or c
individuals. Valenzuela et al. (1991) suggested that this finding may be
significant in relation to maintenance of the Rh polymorphism and
fetomaternal incompatibility.
BIOCHEMICAL FEATURES
Athletes such as racing cyclists sometimes use erythropoietin, which has
been officially included in the International Olympic Committee list of
banned substances since 1990, as a booster drug. Gareau et al. (1994)
presented evidence that the level of transferrin receptor in the blood
can be used as a means of detecting Epo misuse.
ANIMAL MODEL
Levy et al. (1999) disrupted the transferrin receptor gene, which they
termed Trfr, in mice. Homozygous mutant mice were not viable beyond
embryonic day 12.5 and had severe anemia with hydrops as well as diffuse
neurologic abnormalities. There was some variation of onset of severe
anemia, and in nonanemic embryos without tissue edema and necrosis
(E9.5), both stressed erythropoiesis and neurologic abnormalities were
apparent. The authors concluded that inadequate iron led to neuronal
apoptosis, but that tissues other than erythrocytes and neurons can
obtain sufficient iron for growth and development through mechanisms
independent of the transferrin cycle. Haploinsufficiency for the
transferrin receptor resulted in microcytic, hypochromic erythrocytes;
normal hemoglobin and hematocrit values were due to compensatory
increase in red cell numbers. Although iron saturation of serum
transferrin was indistinguishable from that of wildtype, heterozygotes
had significantly less tissue iron.
*FIELD* SA
Enns et al. (1982); Larrick and Hyman (1984); Newman et al. (1982);
Omary and Trowbridge (1981); Schneider et al. (1983); Schneider et
al. (1984); Vodinelich et al. (1983)
*FIELD* RF
1. Adriaansen, H. J.; Geurts Van Kessel, A. H. M.; Wijdenes-De Bresser,
J. H. F. M.; Van Drunen-Schoenmaker, E.; Van Dongen, J. J. M.: Expression
of the myeloid differentiation antigen CD33 depends on the presence
of human chromosome 19 in human-mouse hybrids. Ann. Hum. Genet. 54:
115-119, 1990.
2. Casey, J. L.; Di Jeso, B.; Rao, K.; Klausner, R. D.; Harford, J.
B.: Two genetic loci participate in the regulation by iron of the
gene for the human transferrin receptor. Proc. Nat. Acad. Sci. 85:
1787-1791, 1988.
3. Elahi, S.; Ertelt, J. M.; Kinder, J. M.; Jiang, T. T.; Zhang, X.;
Xin, L.; Chaturvedi, V.; Strong, B. S.; Qualls, J. E.; Steinbrecher,
K. A.; Kalfa, T. A.; Shaaban, A. F.; Way, S. S.: Immunosuppressive
CD71+ erythroid cells compromise neonatal host defence against infection. Nature 504:
158-162, 2013.
4. Enns, C. A.; Suomalainen, H. A.; Gebhardt, J. E.; Schroder, J.;
Sussman, H. H.: Human transferrin receptor: expression of the receptor
is assigned to chromosome 3. Proc. Nat. Acad. Sci. 79: 3241-3245,
1982.
5. Gareau, R.; Gagnon, M. G.; Thellend, C.; Chenard, C.; Audran, M.;
Chanal, J.-L.; Ayotte, C.; Brisson, G. R.: Transferrin soluble receptor:
a possible probe for detection of erythropoietin abuse by athletes. Horm.
Metab. Res. 26: 311-312, 1994.
6. Goodfellow, P. N.; Banting, G.; Sutherland, R.; Greaves, M.; Solomon,
E.; Povey, S.: Expression of human transferrin receptor is controlled
by a gene on chromosome 3: assignment using species specificity of
a monoclonal antibody. Somat. Cell Genet. 8: 197-206, 1982.
7. Ishii, K.; Fumoto, T.; Iwai, K.; Takeshita, S.; Ito, M.; Shimohata,
N.; Aburatani, H.; Taketani, S.; Lelliott, C. J.; Vidal-Puig, A.;
Ikeda, K.: Coordination of PGC-1-beta and iron uptake in mitochondrial
biogenesis and osteoclast activation. Nature Med. 15: 259-266, 2009.
8. Kashuba, V. I.; Gizatullin, R. Z.; Protopopov, A. I.; Allikmets,
R.; Korolev, S.; Li, J.; Boldog, F.; Tory, K.; Zabarovska, V.; Marcsek,
Z.; Sumegi, J.; Klein, G.; Zabarovsky, E. R.; Kisselev, L.: NotI
linking/jumping clones of human chromosome 3: mapping of the TFRC,
RAB7 and HAUSP genes to regions rearranged in leukemia and deleted
in solid tumors. FEBS Lett. 419: 181-185, 1997.
9. Larrick, J. W.; Hyman, E. S.: Acquired iron-deficiency anemia
caused by an antibody against the transferrin receptor. New Eng.
J. Med. 311: 214-218, 1984.
10. Levy, J. E.; Jin, O.; Fujiwara, Y.; Kuo, F.; Andrews, N. C.:
Transferrin receptor is necessary for development of erythrocytes
and the nervous system. Nature Genet. 21: 396-399, 1999.
11. Miller, Y. E.; Jones, C.; Scoggin, C.; Morse, H.; Seligman, P.
: Chromosome 3q (22-ter) encodes the human transferrin receptor. Am.
J. Hum. Genet. 35: 573-583, 1983.
12. Newman, R.; Schneider, C.; Sutherland, R.; Vodinelich, L.; Greaves,
M.: The transferrin receptor. Trends Biochem. Sci. 7: 397-400,
1982.
13. Nikinmaa, B.; Schroder, J.: Two antigens, the transferrin receptor
and p90 assigned to human chromosome 3, are probably the same protein. Hereditas 107:
55-58, 1987.
14. Omary, M. B.; Trowbridge, I. S.: Biosynthesis of the human transferrin
receptor in cultured cells. J. Biol. Chem. 256: 12888-12892, 1981.
15. Rabin, M.; McClelland, A.; Kuhn, L.; Ruddle, F. H.: Regional
localization of the human transferrin receptor gene to 3q26.2-qter. Am.
J. Hum. Genet. 37: 1112-1116, 1985.
16. Radoshitzky, S. R.; Abraham, J.; Spiropoulou, C. F.; Kuhn, J.
H.; Nguyen, D.; Li, W.; Nagel, J.; Schmidt, P. J.; Nunberg, J. H.;
Andrews, N. C.; Farzan, M.; Choe, H.: Transferrin receptor 1 is a
cellular receptor for New World haemorrhagic fever arenaviruses. Nature 446:
92-96, 2007.
17. Schneider, C.; Kurkinen, M.; Greaves, M.: Isolation of cDNA clones
for the human transferrin receptor. EMBO J. 2: 2259-2263, 1983.
18. Schneider, C.; Owen, M. J.; Banville, D.; Williams, J. G.: Primary
structure of human transferrin receptor deduced from the mRNA sequence. Nature 311:
675-678, 1984.
19. Sutherland, R.; Delia, D.; Schneider, C.; Newman, R.; Kemshead,
J.; Greaves, M.: Ubiquitous cell-surface glycoprotein on tumor cells
is proliferation-associated receptor for transferrin. Proc. Nat.
Acad. Sci. 78: 4515-4519, 1981.
20. Valenzuela, C. Y.; Avendano, A.; Harb, Z.: Association between
Rh and plasma iron binding (transferrin). Hum. Genet. 87: 438-440,
1991.
21. Vodinelich, L.; Sutherland, R.; Schneider, C.; Newman, R.; Greaves,
M.: Receptor for transferrin may be a 'target' structure for natural
killer cells. Proc. Nat. Acad. Sci. 80: 835-839, 1983.
*FIELD* CN
Ada Hamosh - updated: 02/05/2014
Patricia A. Hartz - updated: 6/8/2009
Ada Hamosh - updated: 6/20/2007
Ada Hamosh - updated: 3/30/1999
*FIELD* CD
Victor A. McKusick: 6/2/1986
*FIELD* ED
alopez: 02/05/2014
wwang: 6/11/2009
terry: 6/8/2009
carol: 4/23/2008
alopez: 6/27/2007
terry: 6/20/2007
joanna: 3/14/2007
alopez: 3/30/1999
terry: 6/5/1998
dholmes: 4/14/1998
alopez: 2/26/1998
carol: 9/20/1994
supermim: 3/16/1992
carol: 2/22/1992
carol: 10/18/1991
carol: 10/16/1991
carol: 10/5/1990