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Gene Review

SMF2  -  divalent metal ion transporter SMF2

Saccharomyces cerevisiae S288c

Synonyms: Manganese transporter SMF2, YHR050W
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Disease relevance of SMF2


High impact information on SMF2


Biological context of SMF2

  • Wild-type and mutant variants of the Nramp1 and Nramp2 proteins were expressed in a yeast mutant bearing null alleles at the SMF1 and SMF2 loci, and complementation of the phenotypes of this yeast mutant was investigated [1].
  • These data are consistent with the concept that uptake of divalent metal ions by SMF1 and SMF2 is essential to yeast cell growth [5].
  • Consistent with this, we found that increased sensitivity of yeast to EGTA in the high Na(+) medium is due to inhibition of SMF1- and SMF2-mediated metal ion transport by uncoupled Na(+) pathway [5].
  • We suggest that SMF1 and SMF2 are mitochondrial membrane proteins that influence PEP-dependent protein import, possibly at the step of protein translocation [6].

Anatomical context of SMF2

  • Under manganese-replete conditions, Bsd2p facilitates trafficking of Smf1p and Smf2p to the vacuole, where these transport proteins are degraded [2].
  • Na(+) inhibited metal ion uptake mediated by SMF1 and SMF2 expressed in oocytes [5].
  • We propose a model in which Smf2p-containing vesicles play a central role in manganese trafficking to the mitochondria and other cellular sites as well [4].

Associations of SMF2 with chemical compounds

  • SMF2-disrupted cells exhibited significantly greater resistance to adriamycin, whereas the resistance of SMF1-disrupted cells was only slightly improved [7].
  • SMF2 (but not SMF3) mediated significant increases in both Fe(2+) and Na(+) transport compared with control oocytes [5].

Other interactions of SMF2

  • Smf1p and Smf2p are regulated at the post-translational level by manganese, whereas Smf3p is regulated by iron through a mechanism that, up until now, was unknown [8].


  1. Functional complementation of the yeast divalent cation transporter family SMF by NRAMP2, a member of the mammalian natural resistance-associated macrophage protein family. Pinner, E., Gruenheid, S., Raymond, M., Gros, P. J. Biol. Chem. (1997) [Pubmed]
  2. Saccharomyces cerevisiae expresses three functionally distinct homologues of the nramp family of metal transporters. Portnoy, M.E., Liu, X.F., Culotta, V.C. Mol. Cell. Biol. (2000) [Pubmed]
  3. The Saccharomyces cerevisiae high affinity phosphate transporter encoded by PHO84 also functions in manganese homeostasis. Jensen, L.T., Ajua-Alemanji, M., Culotta, V.C. J. Biol. Chem. (2003) [Pubmed]
  4. Manganese superoxide dismutase in Saccharomyces cerevisiae acquires its metal co-factor through a pathway involving the Nramp metal transporter, Smf2p. Luk, E.E., Culotta, V.C. J. Biol. Chem. (2001) [Pubmed]
  5. Yeast SMF1 mediates H(+)-coupled iron uptake with concomitant uncoupled cation currents. Chen, X.Z., Peng, J.B., Cohen, A., Nelson, H., Nelson, N., Hediger, M.A. J. Biol. Chem. (1999) [Pubmed]
  6. Two related genes encoding extremely hydrophobic proteins suppress a lethal mutation in the yeast mitochondrial processing enhancing protein. West, A.H., Clark, D.J., Martin, J., Neupert, W., Hartl, F.U., Horwich, A.L. J. Biol. Chem. (1992) [Pubmed]
  7. A novel role for Bsd2 in the resistance of yeast to adriamycin. Takahashi, T., Furuchi, T., Naganuma, A. J. Cell. Physiol. (2005) [Pubmed]
  8. The distinct methods by which manganese and iron regulate the Nramp transporters in yeast. Portnoy, M.E., Jensen, L.T., Culotta, V.C. Biochem. J. (2002) [Pubmed]
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