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Gene Review

SEC53  -  phosphomannomutase SEC53

Saccharomyces cerevisiae S288c

Synonyms: ALG4, PMM, Phosphomannomutase, YFL045C
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High impact information on SEC53

  • Myoinositol gets incorporated into numerous membrane glycoproteins of Saccharomyces cerevisiae; incorporation is dependent on phosphomannomutase (sec53) [1].
  • These results suggested that the Sec53 protein does not function directly in the translocation and glycosylation of prepro-alpha-factor [2].
  • To examine this point further, we isolated membranes from sec53 cells that had been grown at the non-permissive temperature prior to disruption [2].
  • Analysis of sec53 presented an opportunity not only to see if mutants could be examined in recently developed yeast in vitro translocation systems, but also to characterize further the nature of this mutant originally postulated to be defective in protein translocation [2].
  • The in vitro phenotype of sec53 could be mimicked by isolating rough microsomes from wild-type cells that had been grown for 1 h in the presence of tunicamycin [2].

Biological context of SEC53


Anatomical context of SEC53


Associations of SEC53 with chemical compounds


Other interactions of SEC53

  • There was virtually no outer chain addition in the alg2 and alg4 mutants. alg4 was the only mutant that failed to secrete invertase [10].
  • A functional, epitope-tagged Kre1p is shown to be highly modified in a SEC53-dependent manner [11].
  • The nucleotide sequence of GGP1 predicts a 60-kDa polypeptide, in agreement with the molecular mass of the gp115 precursor detected in sec53 mutant cells at restrictive temperature [12].
  • The fission yeast sns mutants arrest with a similar cell cycle block and interact genetically with the Ran system. sns-A10, sns-B2 and sns-B9 have mutations in the fission yeast homologues of S. cerevisiae Sar1p, Sec31p and Sec53p, respectively, which are required for the early steps of the protein secretory pathway [13].

Analytical, diagnostic and therapeutic context of SEC53


  1. Myoinositol gets incorporated into numerous membrane glycoproteins of Saccharomyces cerevisiae; incorporation is dependent on phosphomannomutase (sec53). Conzelmann, A., Fankhauser, C., Desponds, C. EMBO J. (1990) [Pubmed]
  2. Secretion in yeast: in vitro analysis of the sec53 mutant. Hibbs, A.R., Meyer, D.I. EMBO J. (1988) [Pubmed]
  3. Characterization of a gene product (Sec53p) required for protein assembly in the yeast endoplasmic reticulum. Bernstein, M., Hoffmann, W., Ammerer, G., Schekman, R. J. Cell Biol. (1985) [Pubmed]
  4. KlSEC53 is an essential Kluyveromyces lactis gene and is homologous with the SEC53 gene of Saccharomyces cerevisiae. Staneva, D., Uccelletti, D., Farina, F., Venkov, P., Palleschi, C. Yeast (2004) [Pubmed]
  5. Targeting and assembly of an oligomeric bacterial enterotoxoid in the endoplasmic reticulum of Saccharomyces cerevisiae. Schonberger, O., Hirst, T.R., Pines, O. Mol. Microbiol. (1991) [Pubmed]
  6. The yeast SEC53 gene encodes phosphomannomutase. Kepes, F., Schekman, R. J. Biol. Chem. (1988) [Pubmed]
  7. Functional significance of PMM2 mutations in mildly affected patients with congenital disorders of glycosylation Ia. Westphal, V., Peterson, S., Patterson, M., Tournay, A., Blumenthal, A., Treacy, E.P., Freeze, H.H. Genet. Med. (2001) [Pubmed]
  8. Sec53, a protein required for an early step in secretory protein processing and transport in yeast, interacts with the cytoplasmic surface of the endoplasmic reticulum. Ruohola, H., Ferro-Novick, S. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  9. Molecular and functional analysis of phosphomannomutase (PMM) from higher plants and genetic evidence for the involvement of PMM in ascorbic acid biosynthesis in Arabidopsis and Nicotiana benthamiana. Qian, W., Yu, C., Qin, H., Liu, X., Zhang, A., Johansen, I.E., Wang, D. Plant J. (2007) [Pubmed]
  10. Yeast mutants deficient in protein glycosylation. Huffaker, T.C., Robbins, P.W. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  11. Yeast Kre1p is a cell surface O-glycoprotein. Roemer, T., Bussey, H. Mol. Gen. Genet. (1995) [Pubmed]
  12. Isolation and deduced amino acid sequence of the gene encoding gp115, a yeast glycophospholipid-anchored protein containing a serine-rich region. Vai, M., Gatti, E., Lacanà, E., Popolo, L., Alberghina, L. J. Biol. Chem. (1991) [Pubmed]
  13. Three proteins required for early steps in the protein secretory pathway also affect nuclear envelope structure and cell cycle progression in fission yeast. Matynia, A., Salus, S.S., Sazer, S. J. Cell. Sci. (2002) [Pubmed]
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