Transferrin receptor 1

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Transferrin receptor
Protein TFRC PDB 1cx8.png
PDB rendering based on 1cx8.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols TFRC ; CD71; T9; TFR; TFR1; TR; TRFR; p90
External IDs OMIM190010 MGI98822 HomoloGene2429 GeneCards: TFRC Gene
RNA expression pattern
PBB GE TFRC 208691 at tn.png
PBB GE TFRC 207332 s at tn.png
More reference expression data
Species Human Mouse
Entrez 7037 22042
Ensembl ENSG00000072274 ENSMUSG00000022797
UniProt P02786 Q62351
RefSeq (mRNA) NM_001128148 NM_011638
RefSeq (protein) NP_001121620 NP_035768
Location (UCSC) Chr 3:
196.03 – 196.08 Mb
Chr 16:
32.61 – 32.63 Mb
PubMed search [1] [2]

Transferrin receptor protein 1 (TfR1), also known as Cluster of Differentiation 71 (CD71), is a protein that in humans is encoded by the TFRC gene.[1][2] TfR1 is required for iron import from transferrin into cells by endocytosis.[3][4]

Structure and function[edit]

TfR1 is a transmembrane glycoprotein composed of two disulfide-linked monomers joined by two disulfide bonds. Each monomer binds one holo-transferrin molecule creating an iron-Tf-TfR complex which enters the cell by endocytosis.[5]

Clinical significance[edit]

TfR1 as a potential new target in cases of human leukemia & lymphoma. InatherYs, in Évry, France, developed a candidate drug, INA01 antibody (anti-CD71) that showed efficacy in pre-clinical studies in the therapy of two incurable orphan oncohematological diseases: the adult T cell leukemia (ATLL) caused by HTLV-1 and the Mantle cell lymphoma (MCL).[citation needed]


TfR1 has been shown to interact with GABARAP[6] and HFE.[7][8]

See also[edit]


  1. ^ Sutherland R, Delia D, Schneider C, Newman R, Kemshead J, Greaves M (July 1981). "Ubiquitous cell-surface glycoprotein on tumor cells is proliferation-associated receptor for transferrin". Proc. Natl. Acad. Sci. U.S.A. 78 (7): 4515–9. doi:10.1073/pnas.78.7.4515. PMC 319822. PMID 6270680. 
  2. ^ Rabin M, McClelland A, Kühn L, Ruddle FH (November 1985). "Regional localization of the human transferrin receptor gene to 3q26.2----qter". Am. J. Hum. Genet. 37 (6): 1112–6. PMC 1684729. PMID 3002171. 
  3. ^ Aisen P (November 2004). "Transferrin receptor 1". Int. J. Biochem. Cell Biol. 36 (11): 2137–43. doi:10.1016/j.biocel.2004.02.007. PMID 15313461. 
  4. ^ Moos T (November 2002). "Brain iron homeostasis". Danish Medical Bulletin 49 (4): 279–301. PMID 12553165. 
  5. ^ Speeckaert MM, Speeckaert R, Delanghe JR (December 2010). "Biological and clinical aspects of soluble transferrin receptor". Critical Reviews in Clinical Laboratory Sciences 47 (5-6): 213–228. doi:10.3109/10408363.2010.550461. PMID 21391831. 
  6. ^ Green F, O'Hare T, Blackwell A, Enns CA (May 2002). "Association of human transferrin receptor with GABARAP". FEBS Lett. 518 (1–3): 101–6. doi:10.1016/S0014-5793(02)02655-8. PMID 11997026. 
  7. ^ Feder JN, Penny DM, Irrinki A, Lee VK, Lebrón JA, Watson N, Tsuchihashi Z, Sigal E, Bjorkman PJ, Schatzman RC (February 1998). "The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding". Proc. Natl. Acad. Sci. U.S.A. 95 (4): 1472–7. doi:10.1073/pnas.95.4.1472. PMC 19050. PMID 9465039. 
  8. ^ West AP, Bennett MJ, Sellers VM, Andrews NC, Enns CA, Bjorkman PJ (December 2000). "Comparison of the interactions of transferrin receptor and transferrin receptor 2 with transferrin and the hereditary hemochromatosis protein HFE". J. Biol. Chem. 275 (49): 38135–8. doi:10.1074/jbc.C000664200. PMID 11027676.