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Transferrin receptor protein 1 (TR) (TfR) (TfR1) (Trfr) (T9) (p90) (CD antigen CD71) [Cleaved into: Transferrin receptor protein 1, serum form (sTfR)]

 TFR1_HUMAN              Reviewed;         760 AA.
P02786; D3DXB0; Q1HE24; Q59G55; Q9UCN0; Q9UCU5; Q9UDF9; Q9UK21;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
30-MAY-2006, sequence version 2.
22-NOV-2017, entry version 217.
RecName: Full=Transferrin receptor protein 1;
Short=TR;
Short=TfR;
Short=TfR1;
Short=Trfr;
AltName: Full=T9;
AltName: Full=p90;
AltName: CD_antigen=CD71;
Contains:
RecName: Full=Transferrin receptor protein 1, serum form;
Short=sTfR;
Name=TFRC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-142.
PubMed=6090955; DOI=10.1038/311675b0;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-142.
PubMed=6094009; DOI=10.1016/0092-8674(84)90004-7;
McClelland A., Kuhn L.C., Ruddle F.H.;
"The human transferrin receptor gene: genomic organization, and the
complete primary structure of the receptor deduced from a cDNA
sequence.";
Cell 39:267-274(1984).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=9358047; DOI=10.1016/S0378-1119(97)00356-9;
Evans P., Kemp J.;
"Exon/intron structure of the human transferrin receptor gene.";
Gene 199:123-131(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
Wheeler D.L.;
"Molecular and evolutionary studies of the transferrin receptor.";
Thesis (1999), University of Iowa, United States.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye;
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).
[9]
PROTEIN SEQUENCE OF 101-119 (STFR).
PubMed=2229063;
Shih Y.J., Baynes R.D., Hudson B.G., Flowers C.H., Skikne B.S.,
Cook J.D.;
"Serum transferrin receptor is a truncated form of tissue receptor.";
J. Biol. Chem. 265:19077-19081(1990).
[10]
PROTEIN SEQUENCE OF 101-123 (STFR), AND CHARACTERIZATION.
TISSUE=Erythroleukemia;
PubMed=1871153; DOI=10.3181/00379727-197-43276;
Baynes R.D., Shih Y.J., Hudson B.G., Cook J.D.;
"Characterization of transferrin receptor released by K562
erythroleukemia cells.";
Proc. Soc. Exp. Biol. Med. 197:416-423(1991).
[11]
PROTEIN SEQUENCE OF 288-302; 694-708 AND 721-730.
TISSUE=Prostatic carcinoma;
PubMed=7864799; DOI=10.1042/bj3060129;
Coppolino M., Migliorini M., Argraves W.S., Dedhar S.;
"Identification of a novel form of the alpha 3 integrin subunit:
covalent association with transferrin receptor.";
Biochem. J. 306:129-134(1995).
[12]
PROTEIN SEQUENCE OF 680-696.
PubMed=1380674; DOI=10.1038/358764a0;
Chicz R.M., Urban R.G., Lane W.S., Gorga J.C., Stern L.J.,
Vignali D.A.A., Strominger J.L.;
"Predominant naturally processed peptides bound to HLA-DR1 are derived
from MHC-related molecules and are heterogeneous in size.";
Nature 358:764-768(1992).
[13]
FUNCTION.
PubMed=3568132; DOI=10.1016/0092-8674(87)90295-9;
Rothenberger S., Iacopetta B.J., Kuhn L.C.;
"Endocytosis of the transferrin receptor requires the cytoplasmic
domain but not its phosphorylation site.";
Cell 49:423-431(1987).
[14]
PALMITOYLATION AT CYS-62 AND CYS-67.
PubMed=3582362;
Jing S., Trowbridge I.S.;
"Identification of the intermolecular disulfide bonds of the human
transferrin receptor and its lipid-attachment site.";
EMBO J. 6:327-331(1987).
[15]
MUTAGENESIS OF CYSTEINE RESIDUES INVOLVED IN INTERMOLECULAR BONDS.
PubMed=2507316;
Alvarez E., Girones N., Davis R.J.;
"Intermolecular disulfide bonds are not required for the expression of
the dimeric state and functional activity of the transferrin
receptor.";
EMBO J. 8:2231-2240(1989).
[16]
MUTAGENESIS OF TYR-20.
PubMed=2327986; DOI=10.1042/bj2670031;
Alvarez E., Girones N., Davis R.J.;
"A point mutation in the cytoplasmic domain of the transferrin
receptor inhibits endocytosis.";
Biochem. J. 267:31-35(1990).
[17]
INTERNALIZATION SEQUENCE, AND MUTAGENESIS OF TYR-20.
PubMed=2298808; DOI=10.1083/jcb.110.2.283;
Jing S., Spencer T., Miller K., Hopkins C., Trowbridge I.S.;
"Role of the human transferrin receptor cytoplasmic domain in
endocytosis: localization of a specific signal sequence for
internalization.";
J. Cell Biol. 110:283-294(1990).
[18]
GLYCOSYLATION AT THR-104.
PubMed=1421756; DOI=10.1093/glycob/2.4.345;
Do S.-I., Cummings R.D.;
"Presence of O-linked oligosaccharide on a threonine residue in the
human transferrin receptor.";
Glycobiology 2:345-353(1992).
[19]
GLYCOSYLATION AT THR-104.
PubMed=1421757; DOI=10.1093/glycob/2.4.355;
Hayes G.R., Enns C.A., Lucas J.J.;
"Identification of the O-linked glycosylation site of the human
transferrin receptor.";
Glycobiology 2:355-359(1992).
[20]
MUTAGENESIS OF 20-TYR--PHE-23; TYR-20; THR-21 AND PHE-23.
PubMed=8408022;
Collawn J.F., Lai A., Domingo D.L., Fitch M., Hatton S.,
Trowbridge I.S.;
"YTRF is the conserved internalization signal of the transferrin
receptor, and a second YTRF signal at position 31-34 enhances
endocytosis.";
J. Biol. Chem. 268:21686-21692(1993).
[21]
STRUCTURE OF CARBOHYDRATES ON ASN-727.
PubMed=7780197; DOI=10.1093/glycob/5.2.227;
Hayes G.R., Williams A., Costello C.E., Enns C.A., Lucas J.J.;
"The critical glycosylation site of human transferrin receptor
contains a high-mannose oligosaccharide.";
Glycobiology 5:227-232(1995).
[22]
IDENTIFICATION OF LIGAND-BINDING DOMAIN.
PubMed=8631371; DOI=10.1111/j.1432-1033.1996.0009u.x;
Buchegger F., Trowbridge I.S., Liu L.F., White S., Collawn J.F.;
"Functional analysis of human/chicken transferrin receptor chimeras
indicates that the carboxy-terminal region is important for ligand
binding.";
Eur. J. Biochem. 235:9-17(1996).
[23]
MUTAGENESIS OF ARG-646; GLY-647 AND ASP-648.
PubMed=10377239; DOI=10.1042/bj3410011;
Dubljevic V., Sali A., Goding J.W.;
"A conserved RGD (Arg-Gly-Asp) motif in the transferrin receptor is
required for binding to transferrin.";
Biochem. J. 341:11-14(1999).
[24]
MUTAGENESIS.
PubMed=11800564; DOI=10.1006/jmbi.2001.5048;
West A.P. Jr., Giannetti A.M., Herr A.B., Bennett M.J., Nangiana J.S.,
Pierce J.R., Weiner L.P., Snow P.M., Bjorkman P.J.;
"Mutational analysis of the transferrin receptor reveals overlapping
HFE and transferrin binding sites.";
J. Mol. Biol. 313:385-397(2001).
[25]
INTERACTION WITH SH3BP4.
PubMed=16325581; DOI=10.1016/j.cell.2005.10.021;
Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P.,
Tacchetti C., Di Fiore P.P.;
"TTP specifically regulates the internalization of the transferrin
receptor.";
Cell 123:875-888(2005).
[26]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-251.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[28]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[29]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH MACHUPO VIRUS
PROTEIN GLYCOPROTEIN COMPLEX.
PubMed=17287727; DOI=10.1038/nature05539;
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).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[31]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH GUANARITO VIRUS
GLYCOPROTEIN COMPLEX, INTERACTION WITH JUNIN VIRUS GLYCOPROTEIN
COMPLEX, AND INTERACTION WITH MACHUPO VIRUS GLYCOPROTEIN COMPLEX.
PubMed=18268337; DOI=10.1073/pnas.0709254105;
Radoshitzky S.R., Kuhn J.H., Spiropoulou C.F., Albarino C.G.,
Nguyen D.P., Salazar-Bravo J., Dorfman T., Lee A.S., Wang E.,
Ross S.R., Choe H., Farzan M.;
"Receptor determinants of zoonotic transmission of New World
hemorrhagic fever arenaviruses.";
Proc. Natl. Acad. Sci. U.S.A. 105:2664-2669(2008).
[32]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-251 AND ASN-727.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[33]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-251.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[39]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[40]
ELECTRON MICROSCOPY, AND PHOSPHORYLATION AT SER-24.
PubMed=9782058; DOI=10.1016/S0969-2126(98)00124-5;
Fuchs H., Luecken W., Tauber R., Engel A.;
"Structural model of phospholipid-reconstituted human transferrin
receptor derived by electron microscopy.";
Structure 6:1235-1243(1998).
[41]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 121-760.
PubMed=10531064; DOI=10.1126/science.286.5440.779;
Lawrence C.M., Ray S., Babyonyshev M., Galluser R., Borhani D.W.,
Harrison S.C.;
"Crystal structure of the ectodomain of human transferrin receptor.";
Science 286:779-782(1999).
[42]
VARIANT SER-142.
PubMed=11702220; DOI=10.1007/s004390100599;
Douabin-Gicquel V., Soriano N., Ferran H., Wojcik F., Palierne E.,
Tamim S., Jovelin T., McKie A.T., Le Gall J.-Y., David V., Mosser J.;
"Identification of 96 single nucleotide polymorphisms in eight genes
involved in iron metabolism: efficiency of bioinformatic extraction
compared with a systematic sequencing approach.";
Hum. Genet. 109:393-401(2001).
[43]
INVOLVEMENT IN IMD46, VARIANT IMD46 HIS-20, CHARACTERIZATION OF
VARIANT IMD46 HIS-20, FUNCTION, AND INTERACTION WITH STEAP3.
PubMed=26642240; DOI=10.1038/ng.3465;
Jabara H.H., Boyden S.E., Chou J., Ramesh N., Massaad M.J., Benson H.,
Bainter W., Fraulino D., Rahimov F., Sieff C., Liu Z.J.,
Alshemmari S.H., Al-Ramadi B.K., Al-Dhekri H., Arnaout R.,
Abu-Shukair M., Vatsayan A., Silver E., Ahuja S., Davies E.G.,
Sola-Visner M., Ohsumi T.K., Andrews N.C., Notarangelo L.D.,
Fleming M.D., Al-Herz W., Kunkel L.M., Geha R.S.;
"A missense mutation in TFRC, encoding transferrin receptor 1, causes
combined immunodeficiency.";
Nat. Genet. 48:74-78(2016).
-!- FUNCTION: Cellular uptake of iron occurs via receptor-mediated
endocytosis of ligand-occupied transferrin receptor into
specialized endosomes. Endosomal acidification leads to iron
release. The apotransferrin-receptor complex is then recycled to
the cell surface with a return to neutral pH and the concomitant
loss of affinity of apotransferrin for its receptor. Transferrin
receptor is necessary for development of erythrocytes and the
nervous system (By similarity). A second ligand, the heditary
hemochromatosis protein HFE, competes for binding with transferrin
for an overlapping C-terminal binding site. Positively regulates T
and B cell proliferation through iron uptake (PubMed:26642240).
{ECO:0000250, ECO:0000269|PubMed:26642240,
ECO:0000269|PubMed:3568132}.
-!- FUNCTION: (Microbial infection) Acts as a receptor for new-world
arenaviruses: Guanarito, Junin and Machupo virus.
{ECO:0000269|PubMed:17287727, ECO:0000269|PubMed:18268337}.
-!- SUBUNIT: Homodimer; disulfide-linked. Binds one transferrin or HFE
molecule per subunit. Binds the HLA class II histocompatibility
antigen, DR1. Interacts with SH3BP3. Interacts with STEAP3;
facilitates TFRC endocytosis in erythroid precursor cells
(PubMed:26642240). {ECO:0000269|PubMed:16325581,
ECO:0000269|PubMed:26642240}.
-!- SUBUNIT: (Microbial infection) Interacts with Guanarito, Junin and
Machupo arenavirus glycoprotein complex (PubMed:17287727,
PubMed:18268337). {ECO:0000269|PubMed:17287727,
ECO:0000269|PubMed:18268337}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-355727, EBI-355727;
P02768:ALB; NbExp=2; IntAct=EBI-355727, EBI-714423;
Q96BA8:CREB3L1; NbExp=4; IntAct=EBI-355727, EBI-6942903;
P02794:FTH1; NbExp=2; IntAct=EBI-355727, EBI-713259;
Q30201:HFE; NbExp=3; IntAct=EBI-355727, EBI-1028850;
Q30201-1:HFE; NbExp=3; IntAct=EBI-355727, EBI-15489346;
O43765:SGTA; NbExp=5; IntAct=EBI-355727, EBI-347996;
Q9P0V3:SH3BP4; NbExp=6; IntAct=EBI-355727, EBI-1049513;
P02787:TF; NbExp=9; IntAct=EBI-355727, EBI-714319;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17081065};
Single-pass type II membrane protein
{ECO:0000269|PubMed:17081065}. Melanosome
{ECO:0000269|PubMed:17081065}. Note=Identified by mass
spectrometry in melanosome fractions from stage I to stage IV.
{ECO:0000269|PubMed:17081065}.
-!- SUBCELLULAR LOCATION: Transferrin receptor protein 1, serum form:
Secreted {ECO:0000269|PubMed:17081065}.
-!- INDUCTION: Regulated by cellular iron levels through binding of
the iron regulatory proteins, IRP1 and IRP2, to iron-responsive
elements in the 3'-UTR. Up-regulated upon mitogenic stimulation.
-!- PTM: N- and O-glycosylated, phosphorylated and palmitoylated. The
serum form is only glycosylated. {ECO:0000269|PubMed:1421756,
ECO:0000269|PubMed:1421757, ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:3582362}.
-!- PTM: Proteolytically cleaved on Arg-100 to produce the soluble
serum form (sTfR).
-!- PTM: Palmitoylated on both Cys-62 and Cys-67. Cys-62 seems to be
the major site of palmitoylation. {ECO:0000269|PubMed:3582362}.
-!- DISEASE: Immunodeficiency 46 (IMD46) [MIM:616740]: An autosomal
recessive primary immunodeficiency disorder characterized by
early-onset chronic diarrhea, recurrent infections, hypo- or
agammaglobulinemia, normal lymphocyte counts, intermittent
neutropenia, and intermittent thrombocytopenia.
{ECO:0000269|PubMed:26642240}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Serum transferrin receptor (sTfR) is used as a
means of detecting erythropoietin (EPO) misuse by athletes and as
a diagnostic test for anemia resulting from a number of conditions
including rheumatoid arthritis, pregnancy, irritable bowel
syndrome and in HIV patients.
-!- MISCELLANEOUS: Canine and feline parvoviruses bind human and
feline transferrin receptors and use these receptors to enter and
infect cells.
-!- SIMILARITY: Belongs to the peptidase M28 family. M28B subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD92491.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TFRCID259ch3q29.html";
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EMBL; X01060; CAA25527.1; -; mRNA.
EMBL; M11507; AAA61153.1; -; mRNA.
EMBL; AF187320; AAF04564.1; -; Genomic_DNA.
EMBL; AB209254; BAD92491.1; ALT_INIT; mRNA.
EMBL; DQ496099; ABF47088.1; -; Genomic_DNA.
EMBL; CH471191; EAW53670.1; -; Genomic_DNA.
EMBL; CH471191; EAW53673.1; -; Genomic_DNA.
EMBL; BC001188; AAH01188.1; -; mRNA.
CCDS; CCDS3312.1; -.
PIR; A93343; JXHU.
RefSeq; NP_001121620.1; NM_001128148.2.
RefSeq; NP_001300894.1; NM_001313965.1.
RefSeq; NP_001300895.1; NM_001313966.1.
RefSeq; NP_003225.2; NM_003234.3.
UniGene; Hs.529618; -.
PDB; 1CX8; X-ray; 3.20 A; A/B/C/D/E/F/G/H=122-760.
PDB; 1DE4; X-ray; 2.80 A; C/F/I=121-760.
PDB; 1SUV; EM; 7.50 A; A/B=122-760.
PDB; 2NSU; EM; 27.00 A; A/B=122-760.
PDB; 3KAS; X-ray; 2.40 A; A=121-760.
PDB; 3S9L; X-ray; 3.22 A; A/B=120-760.
PDB; 3S9M; X-ray; 3.32 A; A/B=120-760.
PDB; 3S9N; X-ray; 3.25 A; A/B=120-760.
PDBsum; 1CX8; -.
PDBsum; 1DE4; -.
PDBsum; 1SUV; -.
PDBsum; 2NSU; -.
PDBsum; 3KAS; -.
PDBsum; 3S9L; -.
PDBsum; 3S9M; -.
PDBsum; 3S9N; -.
ProteinModelPortal; P02786; -.
SMR; P02786; -.
BioGrid; 112895; 84.
CORUM; P02786; -.
DIP; DIP-2736N; -.
ELM; P02786; -.
IntAct; P02786; 71.
MINT; MINT-4999032; -.
STRING; 9606.ENSP00000353224; -.
DrugBank; DB09412; Gallium citrate Ga-67.
DrugBank; DB05260; Gallium nitrate.
MEROPS; M28.972; -.
iPTMnet; P02786; -.
PhosphoSitePlus; P02786; -.
SwissPalm; P02786; -.
UniCarbKB; P02786; -.
BioMuta; TFRC; -.
DMDM; 108935939; -.
EPD; P02786; -.
MaxQB; P02786; -.
PaxDb; P02786; -.
PeptideAtlas; P02786; -.
PRIDE; P02786; -.
DNASU; 7037; -.
Ensembl; ENST00000360110; ENSP00000353224; ENSG00000072274.
Ensembl; ENST00000392396; ENSP00000376197; ENSG00000072274.
GeneID; 7037; -.
KEGG; hsa:7037; -.
UCSC; uc003fvz.5; human.
CTD; 7037; -.
DisGeNET; 7037; -.
EuPathDB; HostDB:ENSG00000072274.12; -.
GeneCards; TFRC; -.
HGNC; HGNC:11763; TFRC.
HPA; CAB000153; -.
HPA; HPA028598; -.
MalaCards; TFRC; -.
MIM; 190010; gene.
MIM; 616740; phenotype.
neXtProt; NX_P02786; -.
OpenTargets; ENSG00000072274; -.
PharmGKB; PA36478; -.
eggNOG; KOG2195; Eukaryota.
eggNOG; COG2234; LUCA.
GeneTree; ENSGT00550000074421; -.
HOVERGEN; HBG023177; -.
InParanoid; P02786; -.
KO; K06503; -.
OMA; DNSHVEM; -.
OrthoDB; EOG091G02ZM; -.
PhylomeDB; P02786; -.
TreeFam; TF312981; -.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
SIGNOR; P02786; -.
ChiTaRS; TFRC; human.
EvolutionaryTrace; P02786; -.
GeneWiki; TFRC; -.
GenomeRNAi; 7037; -.
PRO; PR:P02786; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000072274; -.
CleanEx; HS_TFRC; -.
ExpressionAtlas; P02786; baseline and differential.
Genevisible; P02786; HS.
GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; IDA:UniProtKB.
GO; GO:0030665; C:clathrin-coated vesicle membrane; TAS:Reactome.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0010008; C:endosome membrane; IDA:CAFA.
GO; GO:0009897; C:external side of plasma membrane; IGI:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:1990712; C:HFE-transferrin receptor complex; IDA:BHF-UCL.
GO; GO:0005887; C:integral component of plasma membrane; IGI:BHF-UCL.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; NAS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:CAFA.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0004998; F:transferrin receptor activity; TAS:ProtInc.
GO; GO:0033570; F:transferrin transmembrane transporter activity; IDA:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:ProtInc.
GO; GO:0035690; P:cellular response to drug; IDA:MGI.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0097286; P:iron ion import; IDA:UniProtKB.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:UniProtKB.
GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
GO; GO:0045830; P:positive regulation of isotype switching; IDA:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:UniProtKB.
GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
GO; GO:0033572; P:transferrin transport; IDA:UniProtKB.
Gene3D; 1.20.930.40; -; 1.
InterPro; IPR003137; PA_domain.
InterPro; IPR007484; Peptidase_M28.
InterPro; IPR029513; TfR.
InterPro; IPR007365; TFR-like_dimer_dom.
InterPro; IPR036757; TFR-like_dimer_dom_sf.
PANTHER; PTHR10404:SF26; PTHR10404:SF26; 1.
Pfam; PF02225; PA; 1.
Pfam; PF04389; Peptidase_M28; 1.
Pfam; PF04253; TFR_dimer; 1.
SUPFAM; SSF47672; SSF47672; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Endocytosis; Glycoprotein; Host cell receptor for virus entry;
Host-virus interaction; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Secreted;
Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1 760 Transferrin receptor protein 1.
/FTId=PRO_0000174132.
CHAIN 101 760 Transferrin receptor protein 1, serum
form.
/FTId=PRO_0000292265.
TOPO_DOM 1 67 Cytoplasmic. {ECO:0000255}.
TRANSMEM 68 88 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 89 760 Extracellular. {ECO:0000255}.
DOMAIN 223 313 PA.
REGION 1 67 Mediates interaction with SH3BP4.
{ECO:0000269|PubMed:16325581}.
REGION 569 760 Ligand-binding.
MOTIF 20 23 Endocytosis signal.
MOTIF 58 61 Stop-transfer sequence.
MOTIF 646 648 Cell attachment site; required for
binding to transferrin.
SITE 100 101 Cleavage; by trypsin; to produce soluble
form.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000250|UniProtKB:Q62351}.
MOD_RES 20 20 Phosphotyrosine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 21 21 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000269|PubMed:9782058}.
LIPID 62 62 S-palmitoyl cysteine.
{ECO:0000269|PubMed:3582362}.
LIPID 67 67 S-palmitoyl cysteine.
{ECO:0000305|PubMed:3582362}.
CARBOHYD 104 104 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:1421756,
ECO:0000269|PubMed:1421757}.
/FTId=CAR_000072.
CARBOHYD 251 251 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1CX8,
ECO:0000244|PDB:3KAS,
ECO:0000269|PubMed:10531064,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 317 317 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1CX8,
ECO:0000244|PDB:1DE4,
ECO:0000244|PDB:3S9L,
ECO:0000244|PDB:3S9M,
ECO:0000244|PDB:3S9N,
ECO:0000269|PubMed:10531064}.
CARBOHYD 727 727 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:1CX8,
ECO:0000244|PDB:3KAS,
ECO:0000269|PubMed:10531064,
ECO:0000269|PubMed:19159218}.
/FTId=CAR_000173.
DISULFID 89 89 Interchain.
DISULFID 98 98 Interchain.
VARIANT 20 20 Y -> H (in IMD46; increases protein
expression; increases cell surface
expression on T and B cells; increases
soluble form level; impairs receptor
internalization; impairs transferrin
transport; impairs T and B cell
proliferation as well as B cell class-
switching; interacts with STEAP3; doesn't
affect receptor internalization in
erythroid precursor cells;
dbSNP:rs863225436).
{ECO:0000269|PubMed:26642240}.
/FTId=VAR_076365.
VARIANT 142 142 G -> S (rare polymorphism;
dbSNP:rs3817672).
{ECO:0000269|PubMed:11702220,
ECO:0000269|PubMed:6090955,
ECO:0000269|PubMed:6094009}.
/FTId=VAR_012737.
VARIANT 212 212 L -> V (in dbSNP:rs41301381).
/FTId=VAR_051806.
VARIANT 420 420 G -> S (in dbSNP:rs41295879).
/FTId=VAR_051807.
VARIANT 677 677 R -> H (in dbSNP:rs41298067).
/FTId=VAR_051808.
MUTAGEN 9 12 FSNL->YTRF: Only 80% as active as wild-
type receptor.
MUTAGEN 20 34 YTRFSLARQVDGDNS->PPGYSLARQVDYTRF: No
influence on endocytic uptake of the
receptor.
MUTAGEN 20 23 YTRF->PPGY: Only 16% as active as wild-
type receptor.
{ECO:0000269|PubMed:8408022}.
MUTAGEN 20 20 Y->C: Only 35% as active as wild-type
receptor. {ECO:0000269|PubMed:2298808,
ECO:0000269|PubMed:2327986,
ECO:0000269|PubMed:8408022}.
MUTAGEN 20 20 Y->G: Only 20% as active as wild-type
receptor. {ECO:0000269|PubMed:2298808,
ECO:0000269|PubMed:2327986,
ECO:0000269|PubMed:8408022}.
MUTAGEN 21 21 T->F: Only 88% as active as wild-type
receptor. {ECO:0000269|PubMed:8408022}.
MUTAGEN 21 21 T->TA: Only 14% as active as wild-type
receptor. {ECO:0000269|PubMed:8408022}.
MUTAGEN 21 21 T->TAA: Only 19% as active as wild-type
receptor. {ECO:0000269|PubMed:8408022}.
MUTAGEN 23 23 F->Y: Only 48% as active as wild-type
receptor. {ECO:0000269|PubMed:8408022}.
MUTAGEN 31 34 GDNS->YTRF: 2-fold increase of the
endocytic uptake of the receptor.
MUTAGEN 47 50 NADN->YTRF: 1.27-fold increase of the
endocytic uptake of the receptor.
MUTAGEN 619 619 L->A: 20-fold reduced affinity for
transferrin receptor. No binding to HFE.
MUTAGEN 622 622 V->A: No significant effect on binding to
transferrin nor HFE.
MUTAGEN 623 623 R->A: No significant effect on binding to
transferrin nor HFE.
MUTAGEN 629 629 R->A: >5-fold reduced affinity for
transferrin. >10-fold reduced affinity
for HFE.
MUTAGEN 640 640 Q->A: No effect on binding to
transferrin. >10-fold reduced affinity
for HFE.
MUTAGEN 641 641 W->A: No significant effect on binding to
transferrin nor HFE.
MUTAGEN 643 643 Y->A: 20-fold reduced affinity for
transferrin. No binding to HFE.
MUTAGEN 644 644 S->A: No significant effect on binding to
transferrin nor HFE.
MUTAGEN 646 646 R->A,H: No binding to transferrin.
{ECO:0000269|PubMed:10377239}.
MUTAGEN 646 646 R->K: 5% binding to transferrin.
{ECO:0000269|PubMed:10377239}.
MUTAGEN 647 647 G->A: Large effect on affinity for
transferrin. 4-fold reduced affinity for
HFE. {ECO:0000269|PubMed:10377239}.
MUTAGEN 648 648 D->A: 16% binding to transferrin.
{ECO:0000269|PubMed:10377239}.
MUTAGEN 648 648 D->E: 57% binding to transferrin.
{ECO:0000269|PubMed:10377239}.
MUTAGEN 650 650 F->Q: >5-fold reduced affinity for
transferrin. >10-fold reduced affinity
for HFE.
CONFLICT 104 104 T -> K (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 109 109 R -> V (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 123 123 Y -> T (in Ref. 10; AA sequence).
{ECO:0000305}.
HELIX 124 136 {ECO:0000244|PDB:3KAS}.
HELIX 140 146 {ECO:0000244|PDB:3KAS}.
TURN 150 152 {ECO:0000244|PDB:3KAS}.
HELIX 160 176 {ECO:0000244|PDB:3KAS}.
STRAND 179 192 {ECO:0000244|PDB:3KAS}.
STRAND 199 204 {ECO:0000244|PDB:3KAS}.
TURN 205 208 {ECO:0000244|PDB:3KAS}.
STRAND 209 214 {ECO:0000244|PDB:3KAS}.
STRAND 220 222 {ECO:0000244|PDB:3S9L}.
STRAND 226 230 {ECO:0000244|PDB:3KAS}.
STRAND 232 234 {ECO:0000244|PDB:3KAS}.
TURN 236 238 {ECO:0000244|PDB:1CX8}.
HELIX 240 244 {ECO:0000244|PDB:3KAS}.
STRAND 245 248 {ECO:0000244|PDB:1CX8}.
STRAND 253 259 {ECO:0000244|PDB:3KAS}.
HELIX 264 272 {ECO:0000244|PDB:3KAS}.
TURN 273 275 {ECO:0000244|PDB:3KAS}.
STRAND 277 282 {ECO:0000244|PDB:3KAS}.
TURN 285 287 {ECO:0000244|PDB:3KAS}.
STRAND 303 306 {ECO:0000244|PDB:3KAS}.
STRAND 308 310 {ECO:0000244|PDB:3S9L}.
STRAND 311 313 {ECO:0000244|PDB:1CX8}.
HELIX 317 319 {ECO:0000244|PDB:1DE4}.
STRAND 334 336 {ECO:0000244|PDB:3KAS}.
HELIX 339 346 {ECO:0000244|PDB:3KAS}.
STRAND 349 352 {ECO:0000244|PDB:3KAS}.
HELIX 355 357 {ECO:0000244|PDB:3KAS}.
STRAND 364 367 {ECO:0000244|PDB:3KAS}.
STRAND 371 377 {ECO:0000244|PDB:3KAS}.
STRAND 380 393 {ECO:0000244|PDB:3KAS}.
STRAND 396 408 {ECO:0000244|PDB:3KAS}.
STRAND 411 413 {ECO:0000244|PDB:3S9N}.
TURN 416 419 {ECO:0000244|PDB:3KAS}.
HELIX 420 438 {ECO:0000244|PDB:3KAS}.
STRAND 445 455 {ECO:0000244|PDB:3KAS}.
HELIX 456 458 {ECO:0000244|PDB:3KAS}.
HELIX 461 469 {ECO:0000244|PDB:3KAS}.
TURN 470 473 {ECO:0000244|PDB:3KAS}.
HELIX 474 476 {ECO:0000244|PDB:3KAS}.
STRAND 478 483 {ECO:0000244|PDB:3KAS}.
STRAND 491 498 {ECO:0000244|PDB:3KAS}.
HELIX 500 502 {ECO:0000244|PDB:3KAS}.
HELIX 503 510 {ECO:0000244|PDB:3KAS}.
TURN 516 518 {ECO:0000244|PDB:3KAS}.
STRAND 520 522 {ECO:0000244|PDB:3KAS}.
HELIX 528 531 {ECO:0000244|PDB:3KAS}.
HELIX 541 546 {ECO:0000244|PDB:3KAS}.
STRAND 552 558 {ECO:0000244|PDB:3KAS}.
TURN 564 567 {ECO:0000244|PDB:3KAS}.
HELIX 573 579 {ECO:0000244|PDB:3KAS}.
HELIX 583 603 {ECO:0000244|PDB:3KAS}.
STRAND 604 606 {ECO:0000244|PDB:3KAS}.
HELIX 613 625 {ECO:0000244|PDB:3KAS}.
HELIX 626 628 {ECO:0000244|PDB:3KAS}.
TURN 629 636 {ECO:0000244|PDB:3KAS}.
HELIX 640 662 {ECO:0000244|PDB:3KAS}.
HELIX 668 680 {ECO:0000244|PDB:3KAS}.
HELIX 682 685 {ECO:0000244|PDB:3KAS}.
STRAND 688 690 {ECO:0000244|PDB:3S9L}.
TURN 692 694 {ECO:0000244|PDB:3KAS}.
TURN 700 702 {ECO:0000244|PDB:3KAS}.
STRAND 705 708 {ECO:0000244|PDB:3S9M}.
HELIX 709 717 {ECO:0000244|PDB:3KAS}.
TURN 718 722 {ECO:0000244|PDB:3S9L}.
HELIX 728 749 {ECO:0000244|PDB:3KAS}.
HELIX 753 755 {ECO:0000244|PDB:1DE4}.
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


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