Transferrin receptor 1

TFRC
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1CX8, 1DE4, 1SUV, 2NSU, 3KAS, 3S9L, 3S9M, 3S9N
Identifiers
Aliases	TFRC, CD71, T9, TFR, TFR1, TR, TRFR, p90, IMD46, transferrin receptor
External IDs	MGI: 98822 HomoloGene: 2429 GeneCards: TFRC
Gene location (Human)
Chr.	Chromosome 3 (human)[1]
End	196,082,189 bp[1]
Gene location (Mouse)
Chr.	Chromosome 16 (mouse)[2]
End	32,632,794 bp[2]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• protein homodimerization activity; • virus receptor activity; • transferrin receptor activity; • identical protein binding; • double-stranded RNA binding; • transferrin transmembrane transporter activity; • RNA binding; • protein binding;
Cellular component	• extracellular vesicle; • integral component of membrane; • recycling endosome; • HFE-transferrin receptor complex; • endosome; • blood microparticle; • membrane; • melanosome; • plasma membrane; • integral component of plasma membrane; • extracellular region; • cell surface; • basolateral plasma membrane; • perinuclear region of cytoplasm; • clathrin-coated pit; • extracellular exosome; • external side of plasma membrane; • extracellular space; • clathrin-coated vesicle membrane; • cytoplasmic vesicle; • endosome membrane; • early endosome;
Biological process	• endocytosis; • osteoclast differentiation; • positive regulation of bone resorption; • receptor-mediated endocytosis; • iron ion import; • cellular response to drug; • regulation of cell proliferation; • regulation of cell growth; • Viral entry; • viral process; • cellular iron ion homeostasis; • positive regulation of isotype switching; • receptor internalization; • transferrin transport; • positive regulation of B cell proliferation; • positive regulation of T cell proliferation; • membrane organization; • cellular response to leukemia inhibitory factor;
	Sources:Amigo / QuickGO
Orthologs
	7037
	22042
	ENSG00000072274
	ENSMUSG00000022797
	P02786
	Q62351
	NM_001313965; NM_001313966; NM_001128148; NM_003234
	NM_011638; NM_001357298
	NP_001121620; NP_001300894; NP_001300895; NP_003225
	NP_035768; NP_001344227
	Wikidata
View/Edit Human	View/Edit Mouse

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.^[5]^[6] TfR1 is required for iron import from transferrin into cells by endocytosis.^[7]^[8]

Structure and function

TfR1 = transferrin receptor 1 in Human iron metabolism.

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.^[9]

Clinical significance

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).

Interactions

TfR1 has been shown to interact with GABARAP^[10] and HFE.^[11]^[12]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000072274 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000022797 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
↑ 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.
↑ 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.
↑ Moos T (November 2002). "Brain iron homeostasis". Danish Medical Bulletin. 49 (4): 279–301. PMID 12553165.
↑ 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.
↑ 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.
↑ 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.
↑ 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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000072274 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000022797 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid6270680-5] 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.

[pmid3002171-6] 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.

[pmid15313461-7] 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.

[pmid12553165-8] Moos T (November 2002). "Brain iron homeostasis". Danish Medical Bulletin. 49 (4): 279–301. PMID 12553165.

[9] 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.

[pmid11997026-10] 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.

[pmid9465039-11] 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.

[pmid11027676-12] 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.

Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1-50	CD1 a-c 1A 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51-100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 - CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101-150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151-200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201-250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 - CD248 CD249
251-300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301-350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

Transferrin receptor 1

Structure and function

Clinical significance

Interactions

See also

References