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homology analyses revealed that Acdp proteins shared very strong AA homologies to the bacteria CorC protein and yeast Amip3 protein. CorA, B, C and D belong to a protein family involved in both influx and efflux of magnesium and cobalt. It has been shown that CorA mutants confer resistance to cobalt toxicity [9]. Amip3 appears to be a homologous to CorC protein which is involved in efflux of magnesium and cobalt in bacteria. Amip3 mutants confer resistant to copper toxicity. Acdp proteins also possess the domains that are found in bacteria CorC and yeast Amip3 proteins, such as the CBS domains, DUF21 domain and transmembrane domains. In addition, a cNMP-binding domain was found in all Acdp proteins, which is usually present in ion channels and cNMP-dependent kinases [10-13]. Using antibody produced by Acdp1 C-terminal peptide, we have shown that Acdp1 is predominantly localized on the plasma membrane in hippocampus neurons. In our previous study, we found human ACDP proteins are predominantly localized in the nucleus in HeLa cells [1]. The discrepancy for Acdp localization in neuronal cells could be caused by non-specificity for previous antibody which was produced by the recombinant ACD domain, or different cells used. In current study, the Acdp1 C-terminus antibody only recognizes Acdp1 in brain tissue extracts as well as in HEK293, 3T3 and PC12 cell lysates, suggesting the specificity of the antibody. Our observations suggested that Acdp might be involved in ion transport in mammalian cells. However, more detailed functional studies are needed to demonstrate the real functions of these proteins."}

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