DMT1

From Wikipedia, the free encyclopedia

Solute carrier family 11 (proton-coupled divalent metal ion transporters), member 2

Identifiers

SLC11A2; DMT1; DCT1; FLJ37416; NRAMP2

External IDs

OMIM: 600523 MGI: 1345279 HomoloGene: 55471

Gene ontology
Molecular Function:	• transporter activity • iron ion transmembrane transporter activity • iron ion binding • cobalt ion transmembrane transporter activity
Cellular Component:	• endosome • plasma membrane • integral to plasma membrane • endosome membrane • endomembrane system • membrane
Biological Process:	• transport • ion transport • cobalt ion transport • iron ion transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_000617 (mRNA)
NP_000608 (protein)

NM_008732 (mRNA)
NP_032758 (protein)

Location

Chr 12: 49.66 - 49.71 Mb

Chr 15: 100.22 - 100.25 Mb

Pubmed search

[1]

[2]

DMT1 ("divalent metal transporter 1") is a transporter involved in human iron metabolism. It is located on the apical membrane of duodenal enterocytes and transports Fe²⁺ from the intestinal lumen to the cytosol.

Dietary iron must be reduced from Fe³⁺ to Fe²⁺ before being transported by DMT1. This is accomplished by Duodenal cytochrome B.

[edit] Further reading

Vidal S, Belouchi AM, Cellier M, et al. (1995). "Cloning and characterization of a second human NRAMP gene on chromosome 12q13.". Mamm. Genome 6 (4): 224–30. PMID 7613023.
Fleming MD, Trenor CC, Su MA, et al. (1997). "Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene.". Nat. Genet. 16 (4): 383–6. doi:10.1038/ng0897-383. PMID 9241278.
Kishi F, Tabuchi M (1998). "Complete nucleotide sequence of human NRAMP2 cDNA.". Mol. Immunol. 34 (12-13): 839–42. PMID 9464519.
Lee PL, Gelbart T, West C, et al. (1998). "The human Nramp2 gene: characterization of the gene structure, alternative splicing, promoter region and polymorphisms.". Blood Cells Mol. Dis. 24 (2): 199–215. doi:10.1006/bcmd.1998.0186. PMID 9642100.
Kishi F, Tabuchi M (1998). "Human natural resistance-associated macrophage protein 2: gene cloning and protein identification.". Biochem. Biophys. Res. Commun. 251 (3): 775–83. doi:10.1006/bbrc.1998.9415. PMID 9790986.
Tabuchi M, Yoshimori T, Yamaguchi K, et al. (2000). "Human NRAMP2/DMT1, which mediates iron transport across endosomal membranes, is localized to late endosomes and lysosomes in HEp-2 cells.". J. Biol. Chem. 275 (29): 22220–8. doi:10.1074/jbc.M001478200. PMID 10751401.
Griffiths WJ, Kelly AL, Smith SJ, Cox TM (2000). "Localization of iron transport and regulatory proteins in human cells.". QJM : monthly journal of the Association of Physicians 93 (9): 575–87. PMID 10984552.
Georgieff MK, Wobken JK, Welle J, et al. (2001). "Identification and localization of divalent metal transporter-1 (DMT-1) in term human placenta.". Placenta 21 (8): 799–804. doi:10.1053/plac.2000.0566. PMID 11095929.
Tallkvist J, Bowlus CL, Lönnerdal B (2001). "DMT1 gene expression and cadmium absorption in human absorptive enterocytes.". Toxicol. Lett. 122 (2): 171–7. PMID 11439223.
Sharp P, Tandy S, Yamaji S, et al. (2002). "Rapid regulation of divalent metal transporter (DMT1) protein but not mRNA expression by non-haem iron in human intestinal Caco-2 cells.". FEBS Lett. 510 (1-2): 71–6. PMID 11755534.
Umbreit JN, Conrad ME, Hainsworth LN, Simovich M (2002). "The ferrireductase paraferritin contains divalent metal transporter as well as mobilferrin.". Am. J. Physiol. Gastrointest. Liver Physiol. 282 (3): G534–9. doi:10.1152/ajpgi.00199.2001. PMID 11842004.
Simovich MJ, Conrad ME, Umbreit JN, et al. (2002). "Cellular location of proteins related to iron absorption and transport.". Am. J. Hematol. 69 (3): 164–70. PMID 11891802.
Rolfs A, Bonkovsky HL, Kohlroser JG, et al. (2002). "Intestinal expression of genes involved in iron absorption in humans.". Am. J. Physiol. Gastrointest. Liver Physiol. 282 (4): G598–607. doi:10.1152/ajpgi.00371.2001. PMID 11897618.
Wang X, Ghio AJ, Yang F, et al. (2002). "Iron uptake and Nramp2/DMT1/DCT1 in human bronchial epithelial cells.". Am. J. Physiol. Lung Cell Mol. Physiol. 282 (5): L987–95. doi:10.1152/ajplung.00253.2001. PMID 11943663.
I Bannon D, Portnoy ME, Olivi L, et al. (2002). "Uptake of lead and iron by divalent metal transporter 1 in yeast and mammalian cells.". Biochem. Biophys. Res. Commun. 295 (4): 978–84. PMID 12127992.
Zoller H, Decristoforo C, Weiss G (2002). "Erythroid 5-aminolevulinate synthase, ferrochelatase and DMT1 expression in erythroid progenitors: differential pathways for erythropoietin and iron-dependent regulation.". Br. J. Haematol. 118 (2): 619–26. PMID 12139757.
Hubert N, Hentze MW (2002). "Previously uncharacterized isoforms of divalent metal transporter (DMT)-1: implications for regulation and cellular function.". Proc. Natl. Acad. Sci. U.S.A. 99 (19): 12345–50. doi:10.1073/pnas.192423399. PMID 12209011.
Tabuchi M, Tanaka N, Nishida-Kitayama J, et al. (2003). "Alternative splicing regulates the subcellular localization of divalent metal transporter 1 isoforms.". Mol. Biol. Cell 13 (12): 4371–87. doi:10.1091/mbc.E02-03-0165. PMID 12475959.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Okubo M, Yamada K, Hosoyamada M, et al. (2003). "Cadmium transport by human Nramp 2 expressed in Xenopus laevis oocytes.". Toxicol. Appl. Pharmacol. 187 (3): 162–7. PMID 12662899.

[edit] External links

MeSH DMT1+protein+(iron+transporter)

This membrane protein-related article is a stub. You can help Wikipedia by expanding it.

v • d • e Membrane proteins, carrier proteins: membrane transport proteins

ABC-transporter	A1, A2, A3, A4, A7, A8, A12, B1 B2-3, B2, B3, B4, B5, B6, B7, B9, B11 C1, C2, C3, C4, C5, C6, C8, C8-9, C10, C13, C11 D1, D2, D3, D4, E1, F1, F2 G1, G2, G4, Sterolin (G5, G8)

Solute carrier	1A1-7, 1A1, 1A2, 1A3, 1A4, 1A5, 2A1, 2A2, 2A3, 2A4, 2A5, 2A6, 2A8, 2A9, 2A10, 2A12, 3A1, 3A2, 4A1, 4A2, 4A3, 4A4, 4A5, 4A7, 4A8, 4A11, 5A1-2, 5A1, 5A3, 5A5, 5A8, 6A1, 6A2, 6A3, 6A4, 6A5, 6A8, 6A9, 6A19, 7A1, 7A2, 7A3, 7A4, 7A5, 7A7, 7A8, 7A9, 7A11, 8A1-3, 9A1, 9A2, 9A3, 9A3R1, 9A3R2, 9A5, 9A6, 9A8, 10A1, 10A2, 10A3, 10A7, 11A1, 11A2, 11A3, 12A1-2, 12A3, 12A4, 12A5, 12A6, 12A7, 14A1, 13A3, 14A2, 15A1, 15A2, 16A1, 16A2, 16A3, 16A4, 17A1, 17A5, 17A6-8, 17A7, 18A1, 18A2, 18A3, 19A1, 19A2, 19A3, 20A1, 20A2, 22A1, 22A2, 22A3, 22A4, 22A5, 22A6, 22A7, 22A9, 22A11, 22A12, 22A18, 23A1, 23A2, 24A1-2, 24A5, 25A1, 25A3, 25A4, 25A4-6, 25A8, 25A10, 25A11, 25A12, 25A13, 25A14, 25A15, 25A17, 25A19, 25A20, 25A27, 25A31, 25A37, 25A39, 26A2, 26A3, 26A4, 26A5, 26A6, 26A7, 26A8, 27A1, 27A2, 27A3, 27A4, 28A1, 28A2, 29A1, 29A2, 29A4, 30A4, 30A7, 30A8, 31A1, 31A2, 32A1, 34A1, 34A2, 34A3, 35A1, 35A2, 35B2, 35B4, 35C1, 36A1, 37A4, 38A2, 38A3, 39A1, 39A2, 39A3, 39A4, 39A6, 39A7, 40A1, 43A1 44A1, 44A2, 44A4, 45A2, O1A2, O1B1, O1B3, O2B1, O431, O4A1

Monosaccharide	GLUT1, GLUT2, GLUT3, GLUT4, GLUT5, GLUT6, GLUT8, GLUT9

Other	Amino acid (CD98) - Fatty acid (CD36) - Ion channels - Ion pumps - Mitochondrial membrane transport protein - Neurotransmitter transport proteins - Nuclear (Importin, Karyopherin)

v • d • e Metabolism: Iron metabolism (including iron-binding proteins)

Absorption in duodenum	Iron(II) oxide: DMT1 (SLC11A2) - Ferritin - Hephaestin/Ferroportin (SLC11A3/SLC40A1) - Transferrin to Transferrin receptor (TFRC, TFR2) Iron(III) oxide: Duodenal cytochrome B - Integrin - Calreticulin/mobilferrin - Ferritin

Other	Hepcidin/HAMP - Hemojuvelin - Iron-responsive element binding protein (Aconitase) - Ceruloplasmin - HFE - Hemosiderin - Lactoferrin