A 22aa Peptide sequence located at the predicted cytoplasmic loop near the C-terminus of rat NRAMP2, without IRE .||Natural resistance to infection with unrelated intracellular parasite such as Mycobacteria, Salmonella, and Leishmania is controlled by a single gene that encodes a macrophage-specific membrane protein designated as Natural Resistance-Associated Macrophage Protein (Nramp1). Recently a second member of NRAMP family, termed NRAMP2/DMT/DCT1 (Divalent Metal ion Transporter 1 or Divalent Cation Transporter 1), has been identified (human, rat and mouse 568 aa, ~65% identity with NRAMP1). Unlike NRAMP1, NRAMP2 expression is more ubiquitous and has been detected in most tissues. It is dramatically up-regulated by iron starvation in the intestine. NRAMP2 gene produces two alternatively spliced transcripts generated by alternative use of two 3' exons encoding distinct C-termini of the protein as well as distinct 3' untranslated regions (UTRs). Interestingly, one Nramp2 mRNA contains an iron-responsive element (IRE) in its 3'UTR. The IRE is an RNA secondary structure present in the 5'- or the 3'-UTR of animal mRNAs encoding proteins involved in iron metabolism. The second Nramp2 splice isoform (without-IRE, isoform II) encodes a protein in which the C-terminal 18-aa of the IRE form (with IRE, isoform I) are replaced by a novel 25-aa segment and codes for a distinct 3' UTR lacking the IRE. The two isoforms are differentially localized and regulated in GI tract and kidney. It has recently been demonstrated that the Nramp2 gene is mutated (Gly185 to Arg at TM4) in both the mk and Belgarde (b) animal models exhibiting a severe microcytic hypochromic anemia marked by a defect in iron absorption by intestinal cells and in erythroid iron use.

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