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Gene Review

SPF1  -  ion-transporting P-type ATPase SPF1

Saccharomyces cerevisiae S288c

Synonyms: COD1, Manganese-transporting ATPase 1, PER9, PIO1, YEL031W
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High impact information on SPF1

  • Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+ homeostasis [1].
  • This role for Cod1p is distinctly different from that of the well-characterized Ca(2+) P-type ATPase Pmr1p which is neither required for Hmg2p degradation nor its control [2].
  • Our data suggested that Cod1p is a calcium transporter required for regulating Hmg2p degradation [2].
  • The identification of Cod1p is especially intriguing in light of the role Ca(2+) plays in the regulated degradation of mammalian HMGR [2].
  • The effects of ste24- and spf1-null mutations on invertase secretion are additive, cell generation time is increased 60%, and cells become sensitive to cold and to heat shock [3].

Biological context of SPF1

  • Expression of the altered SPF1, with Asp487 replaced by Asn, did not suppress the SMKT-resistant phenotype of spf1 mutants, suggesting that the catalytic activity of this ATPase is required for acquisition of sensitivity to SMKT [4].
  • To investigate the function of Spf1p, Asp487, the putative phosphorylation site of Spf1p, was replaced by Asn [4].
  • The Saccharomyces cerevisiae Pas3p, a homologue of per9p, restored peroxisome biogenesis and peroxisomal protein import in the delta per9 mutant, allowing it to grow again on methanol as sole carbon and energy source [5].

Anatomical context of SPF1

  • PIO1 is SPF1, encoding a P-type ATPase located in the endoplasmic reticulum (ER) or Golgi. spf1-null mutants are modestly sensitive to EGTA [3].
  • Furthermore, Cod1p, like Pmr1p, is also needed for the outer chain modification of carbohydrates in the Golgi apparatus despite its ER localization [6].
  • This result shows that heterologous complementation of peroxisome function in yeast is indeed feasible and furthermore suggests that H. polymorpha delta per9 may be the candidate of choice to attempt the isolation of Per9p homologues from higher eukaryotes by functional complementation [5].

Associations of SPF1 with chemical compounds

  • Pmr1p is the Golgi Ca(2+) ATPase and Spf1p may be the equivalent ER pump [3].
  • The spf1 disruptant also showed increased expression of Kar2p and sensitivity to tunicamycin [4].

Other interactions of SPF1

  • Our findings imply a homeostatic role for Mdm39p, which may be related to the regulation of calcium ion fluxes in the ER, and is indispensable for mutants that lack Spf1p [7].
  • Regulation of HMG-CoA reductase degradation requires the P-type ATPase Cod1p/Spf1p [2].
  • Cells lacking Spf1p had an abnormal fractionation pattern of Sec12p [4].
  • Subcellular fractionation experiments indicated that the fractionation pattern of Spf1p was similar to that of an early Golgi protein, Och1p [4].


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