DMT1

Solute carrier family 11 (proton-coupled divalent metal ion transporters), member 2
Available structures PDB [1]
Identifiers
Symbols	SLC11A2; DCT1; DMT1; FLJ37416; NRAMP2
External IDs	OMIM: 600523 MGI: 1345279 HomoloGene: 55471 GeneCards: SLC11A2 Gene
Gene Ontology Molecular function • transporter activity • copper ion transmembrane transporter activity • iron ion transmembrane transporter activity • manganese ion transmembrane transporter activity • zinc ion transmembrane transporter activity • zinc ion transmembrane transporter activity • iron ion binding • copper ion binding • protein binding • zinc ion binding • hydrogen ion transmembrane transporter activity • calcium ion transmembrane transporter activity • cadmium ion transmembrane transporter activity • cobalt ion transmembrane transporter activity • cobalt ion transmembrane transporter activity • ferrous iron transmembrane transporter activity • lead ion transmembrane transporter activity • nickel ion transmembrane transporter activity • nickel ion transmembrane transporter activity • vanadium ion transmembrane transporter activity • solute:hydrogen symporter activity • nickel ion binding • inorganic cation transmembrane transporter activity • manganese ion binding • cadmium ion binding • cobalt ion binding • chromium ion transmembrane transporter activity Cellular component • nucleus • cytoplasm • lysosome • lysosomal membrane • early endosome • late endosome • vacuole • trans-Golgi network • plasma membrane • plasma membrane • plasma membrane • integral to plasma membrane • brush border • cell surface • endomembrane system • apical plasma membrane • cytoplasmic vesicle • late endosome membrane • apical part of cell • basal part of cell • perinuclear region of cytoplasm • recycling endosome • paraferritin complex Biological process • response to hypoxia • detection of oxygen • detection of oxygen • heme biosynthetic process • ion transport • cobalt ion transport • copper ion transport • manganese ion transport • cellular iron ion homeostasis • activation of caspase activity • learning or memory • response to iron ion • response to iron ion • response to manganese ion • response to lead ion • nickel ion transport • vanadium ion transport • ferrous iron transport • lead ion transport • proton transport • cellular response to oxidative stress • iron ion transmembrane transport • copper ion transmembrane transport • nickel ion transmembrane transport • response to cadmium ion • dendrite morphogenesis • erythrocyte development • transmembrane transport • multicellular organismal iron ion homeostasis • cadmium ion transmembrane transport • ferrous iron import • manganese ion transmembrane transport • zinc ion transmembrane transport Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	4891	18174
Ensembl	ENSG00000110911	ENSMUSG00000023030
UniProt	P49281	Q3UFV5
RefSeq (mRNA)	NM_000617	NM_008732
RefSeq (protein)	NP_000608	NP_032758
Location (UCSC)	Chr 12: 51.37 – 51.42 Mb	Chr 15: 100.22 – 100.26 Mb
PubMed search	[2]	[3]

DMT1 has two forms in the brain + ire and -ire. There is differential expression after injury or aging. Appears to be important in the accumulation of iron in the brain in Parkinson's Disease 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.

Further reading

• Vidal S, Belouchi AM, Cellier M (1995). "Cloning and characterization of a second human NRAMP gene on chromosome 12q13.". Mamm. Genome 6 (4): 224–30. doi:10.1007/BF00352405. PMID 7613023. 
• Fleming MD, Trenor CC, Su MA (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. doi:10.1016/S0161-5890(97)00110-7. PMID 9464519. 
• Lee PL, Gelbart T, West C (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 (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. doi:10.1093/qjmed/93.9.575. PMID 10984552. 
• Georgieff MK, Wobken JK, Welle J (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. doi:10.1016/S0378-4274(01)00363-0. PMID 11439223. 
• Sharp P, Tandy S, Yamaji S (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. doi:10.1016/S0014-5793(01)03225-2. 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 (2002). "Cellular location of proteins related to iron absorption and transport". Am. J. Hematol. 69 (3): 164–70. doi:10.1002/ajh.10052. PMID 11891802. 
• Rolfs A, Bonkovsky HL, Kohlroser JG (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 (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 (2002). "Uptake of lead and iron by divalent metal transporter 1 in yeast and mammalian cells". Biochem. Biophys. Res. Commun. 295 (4): 978–84. doi:10.1016/S0006-291X(02)00756-8. 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. doi:10.1046/j.1365-2141.2002.03626.x. 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. PMC 129447. PMID 12209011. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=129447. 
• Tabuchi M, Tanaka N, Nishida-Kitayama J (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. PMC 138640. PMID 12475959. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=138640. 
• Strausberg RL, Feingold EA, Grouse LH (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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Okubo M, Yamada K, Hosoyamada M (2003). "Cadmium transport by human Nramp 2 expressed in Xenopus laevis oocytes". Toxicol. Appl. Pharmacol. 187 (3): 162–7. doi:10.1016/S0041-008X(02)00078-9. PMID 12662899. 

External links

• MeSH DMT1+protein+(iron+transporter)

SLC11–20
(11) proton coupled metal ion transporter (SLC11A1, SLC11A2) 11A3 (12) electroneutral cation-Cl cotransporter (SLC12A1, SLC12A1, SLC12A2, SLC12A3, SLC12A4, SLC12A5, SLC12A6, SLC12A7, SLC12A8, SLC12A9) (13) human Na+-sulfate/carboxylate cotransporter (SLC13A1, SLC13A2, SLC13A3, SLC13A4, SLC13A5) (14) urea transporter (SLC14A1, SLC14A2) (15) proton oligopeptide cotransporter (SLC15A1, SLC15A2, SLC15A3, SLC15A4) (16) monocarboxylate transporter (SLC16A1, SLC16A2, SLC16A3, SLC16A4, SLC16A5, SLC16A6, SLC16A7, SLC16A8, SLC16A9, SLC16A10, SLC16A11, SLC16A12, SLC16A13, SLC16A14) (17) vesicular glutamate transporter (SLC17A1, SLC17A2, SLC17A3, SLC17A4, SLC17A5, SLC17A6, SLC17A7, SLC17A8, SLC17A9) (18) vesicular amine transporter (SLC18A1, SLC18A2, SLC18A3) (19) folate/thiamine transporter (SLC19A1, SLC19A2, SLC19A3) (20) type III Na+-phosphate cotransporter (SLC20A1, SLC20A2)

SLC21–30
(21) organic anion transporting (SLCO1A2, SLCO1B1, SLCO1B3, SLCO1B4, SLCO1C1) (SLCO2A1, SLCO2B1) (SLCO3A1) (SLCO4A1, SLCO4C1) (SLCO5A1) (SLCO6A1) (22) organic cation/anion/zwitterion transporter (SLC22A1, SLC22A2, SLC22A3, SLC22A4, SLC22A5, SLC22A6, SLC22A7, SLC22A8, SLC22A9, SLC22A10, SLC22A11, SLC22A12, SLC22A13, SLC22A14, SLC22A15, SLC22A16, SLC22A17, SLC22A18, SLC22A19, SLC22A20) (23) Na+-dependent ascorbic acid transporter (SLC23A1, SLC23A2, SLC23A3, SLC23A4) (24) Na+/(Ca2+-K+) exchanger (SLC24A1, SLC24A2, SLC24A3, SLC24A4, SLC24A5, SLC24A6) (25) mitochondrial carrier (SLC25A1, SLC25A2, SLC25A3, SLC25A4, SLC25A5, SLC25A6, SLC25A7, SLC25A8, SLC25A9, SLC25A10, SLC25A11, SLC25A12, SLC25A13, SLC25A14, SLC25A15, SLC25A16, SLC25A17, SLC25A18, SLC25A19, SLC25A20, SLC25A21, SLC25A22, SLC25A23, SLC25A24, SLC25A25, SLC25A26, SLC25A27, SLC25A28, SLC25A29, SLC25A30, SLC25A31, SLC25A32, SLC25A33, SLC25A34, SLC25A35, SLC25A36, SLC25A37, SLC25A38, SLC25A39, SLC25A40, SLC25A41, SLC25A42, SLC25A43, SLC25A44, SLC25A45, SLC25A46) (26) multifunctional anion exchanger (SLC26A1, SLC26A2, SLC26A3, SLC26A4, SLC26A5, SLC26A6, SLC26A7, SLC26A8, SLC26A9, SLC26A10, SLC26A11) (27) fatty acid transport proteins (SLC27A1, SLC27A2, SLC27A3, SLC27A4, SLC27A5, SLC27A6) (28) Na+-coupled nucleoside transport (SLC28A1, SLC28A2, SLC28A3 (29) facilitative nucleoside transporter (SLC29A1, SLC29A2, SLC29A3, SLC29A4) (30) zinc efflux (SLC30A1, SLC30A2, SLC30A3, SLC30A4, SLC30A5, SLC30A6, SLC30A7, SLC30A8, SLC30A9, SLC30A10)

SLC31–40
(31) copper transporter (SLC31A1) (32) vesicular inhibitory amino-acid transporter (SLC32A1) (33) Acetyl-CoA transporter (SLC33A1) (34) type II Na+-phosphate cotransporter (SLC34A1, SLC34A2, SLC34A3) (35) nucleoside-sugar transporter (SLC35A1, SLC35A2, SLC35A3, SLC35A4, SLC35A5) (SLC35B1, SLC35B2, SLC35B3, SLC35B4) (SLC35C1, SLC35C2) (SLC35D1, SLC35D2, SLC35D3) (SLC35E1, SLC35E2, SLC35E3, SLC35E4) (36) proton-coupled amino-acid transporter (SLC36A1, SLC36A2, SLC36A3, SLC36A4)36A2 · (37) sugar-phosphate/phosphate exchanger (SLC37A1, SLC37A2, SLC37A3, SLC37A4) (38) System A & N, sodium-coupled neutral amino-acid transporter (SLC38A1, SLC38A2, SLC38A3, SLC38A4, SLC38A5, SLC38A6, SLC38A10) (39) metal ion transporter (SLC39A1, SLC39A2, SLC39A3, SLC39A4, SLC39A5, SLC39A6, SLC39A7, SLC39A8, SLC39A9, SLC39A10, SLC39A11, SLC39A12, SLC39A13, SLC39A14) (40) basolateral iron transporter (SLC40A1)

SLC41–48
(41) MgtE-like magnesium transporter (SLC41A1, SLC41A2, SLC41A3) (42) Ammonia transporter (RhAG, RhBG, RhCG) (43) Na+-independent, system-L like amino-acid transporter (SLC43A1, SLC43A2, SLC43A3) (44) Choline-like transporter (SLC44A1, SLC44A2, SLC44A3, SLC44A4, SLC44A5) (45) Putative sugar transporter (SLC45A1, SLC45A2, SLC54A3, SLC45A4) (46) Folate transporter (SLC46A1, SLC46A2) (47) multidrug and toxin extrusion (SLC47A1, SLC47A2) (48) Heme transporter

SLCO1–4
O1A2 · O1B1 · O1B3 · O2B1 · O431 · O4A1

Ion pumps
Symporter, Cotransporter Na+/K+/2Cl- - Na/Pi3 - Na+/Cl- - Na/glucose - Na+/I- - Cl-/K+ (4, 5) Antiporter (exchanger) Na+/H+ - Na+/Ca2+ (Na+/(Ca2+-K+)) - Cl-/HCO3- (Band 3) - Cl-formate exchanger - Cl-oxalate exchanger

see also solute carrier disorders
B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othr