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Gene Review

SEC20  -  Sec20p

Saccharomyces cerevisiae S288c

Synonyms: D9719.4, Protein transport protein SEC20, YDR498C
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Disease relevance of SEC20


High impact information on SEC20


Biological context of SEC20

  • We have cloned the SEC20 gene by complementation of the temperature sensitive phenotype of a sec20-1 strain [5].
  • The DNA sequence predicts a 44 kDa protein with a single membrane-spanning region; Sec20p has an apparent molecular weight of 50 kDa and behaves as an integral membrane protein with carbohydrate modifications that appear to be O-linked [5].
  • Divergence of eukaryotic secretory components: the Candida albicans homolog of the Saccharomyces cerevisiae ++Sec20 protein is N terminally truncated, and its levels determine antifungal drug resistance and growth [1].
  • These results demonstrate the occurrence and function of Sec20p in a fungal species other than S. cerevisiae, but the lack of the N-terminal domain and the apparent absence of a close TIP20 homolog in the C. albicans genome also indicate a considerable diversity in mechanisms of retrograde vesicle traffic in eukaryotes [1].

Anatomical context of SEC20


Associations of SEC20 with chemical compounds


Physical interactions of SEC20


Other interactions of SEC20

  • Sec20p and Tip20p were previously identified as two interacting proteins involved in early steps of the secretory pathway in Saccharomyces cerevisiae [7].
  • Based on the previously reported association with Ufe1 and Sec22, Sec20 likely contributes the fourth SNARE to the SNAREpin [8].
  • We also discovered that in vivo, Sly1p was associated with a SNARE complex formed on the ER, and that in vitro, the SM protein directly interacted with the ER-localized nonsyntaxin SNAREs Use1p/Slt1p and Sec20p [9].

Analytical, diagnostic and therapeutic context of SEC20

  • Coimmunoprecipitation and immunofluorescence using Tip1p and Sec20p or its cytoplasmic domain showed that the two proteins physically interact to form a stable complex [4].


  1. Divergence of eukaryotic secretory components: the Candida albicans homolog of the Saccharomyces cerevisiae ++Sec20 protein is N terminally truncated, and its levels determine antifungal drug resistance and growth. Weber, Y., Santore, U.J., Ernst, J.F., Swoboda, R.K. J. Bacteriol. (2001) [Pubmed]
  2. SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum. Lewis, M.J., Pelham, H.R. Cell (1996) [Pubmed]
  3. A novel SNARE complex implicated in vesicle fusion with the endoplasmic reticulum. Lewis, M.J., Rayner, J.C., Pelham, H.R. EMBO J. (1997) [Pubmed]
  4. The TIP1 gene of Saccharomyces cerevisiae encodes an 80 kDa cytoplasmic protein that interacts with the cytoplasmic domain of Sec20p. Sweet, D.J., Pelham, H.R. EMBO J. (1993) [Pubmed]
  5. The Saccharomyces cerevisiae SEC20 gene encodes a membrane glycoprotein which is sorted by the HDEL retrieval system. Sweet, D.J., Pelham, H.R. EMBO J. (1992) [Pubmed]
  6. Sec20p-interacting proteins (Tip20p, Ufe1p) in the retrograde secretory pathway of the fungal pathogen Candida albicans. Weber, Y., Swoboda, R.K., Ernst, J.F. Mol. Genet. Genomics (2002) [Pubmed]
  7. The Sec20/Tip20p complex is involved in ER retrieval of dilysine-tagged proteins. Cosson, P., Schröder-Köhne, S., Sweet, D.S., Démollière, C., Hennecke, S., Frigerio, G., Letourneur, F. Eur. J. Cell Biol. (1997) [Pubmed]
  8. A SNARE required for retrograde transport to the endoplasmic reticulum. Burri, L., Varlamov, O., Doege, C.A., Hofmann, K., Beilharz, T., Rothman, J.E., Söllner, T.H., Lithgow, T. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  9. Structure-based functional analysis reveals a role for the SM protein Sly1p in retrograde transport to the endoplasmic reticulum. Li, Y., Gallwitz, D., Peng, R. Mol. Biol. Cell (2005) [Pubmed]
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