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Gene Review

YIP3  -  Yip3p

Saccharomyces cerevisiae S288c

Synonyms: N2650, PRA1, Prenylated Rab acceptor 1, YNL044W
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Disease relevance of YIP3


High impact information on YIP3

  • Replacement of the deleted VAMP2 transmembrane domain by a CAAX prenylation signal can not restore binding to PRA1 [3].
  • PRA1 is a 21-kDa protein associated with Golgi membranes that binds to prenylated Rab proteins in their GTP-bound state [1].
  • Furthermore, gp41 sequences important for PRA1 binding were mapped to a central leucine-rich, amphipathic alpha-helix in the SIV gp41 cytoplasmic tail [1].
  • Envelope glycoprotein cytoplasmic domains from diverse lentiviruses interact with the prenylated Rab acceptor [1].
  • The assembly and release of infectious virus particles was studied under conditions of PRA1 overexpression in a transient transfection assay or suppression by RNA interference [2].

Biological context of YIP3


Anatomical context of YIP3

  • These data indicate that Yip3p may have multiple functions and that its interaction with Rabs is not critical for their recruitment to organelle membranes [6].

Physical interactions of YIP3


Other interactions of YIP3

  • However, Ypt1p did not copurify with Rtn1p, indicating that Yip3p is a component of at least two different protein complexes [6].

Analytical, diagnostic and therapeutic context of YIP3


  1. Envelope glycoprotein cytoplasmic domains from diverse lentiviruses interact with the prenylated Rab acceptor. Evans, D.T., Tillman, K.C., Desrosiers, R.C. J. Virol. (2002) [Pubmed]
  2. PRA1 co-localizes with envelope but does not influence primate lentivirus production, infectivity or envelope incorporation. Blancou, P., Evans, D.T., Desrosiers, R.C. J. Gen. Virol. (2005) [Pubmed]
  3. Isolation and characterization of a dual prenylated Rab and VAMP2 receptor. Martincic, I., Peralta, M.E., Ngsee, J.K. J. Biol. Chem. (1997) [Pubmed]
  4. Identification of proteins highly expressed in the hyphae of Candida albicans by two-dimensional electrophoresis. Choi, W., Yoo, Y.J., Kim, M., Shin, D., Jeon, H.B., Choi, W. Yeast (2003) [Pubmed]
  5. Identification of potential cell-surface proteins in Candida albicans and investigation of the role of a putative cell-surface glycosidase in adhesion and virulence. Alberti-Segui, C., Morales, A.J., Xing, H., Kessler, M.M., Willins, D.A., Weinstock, K.G., Cottarel, G., Fechtel, K., Rogers, B. Yeast (2004) [Pubmed]
  6. Saccharomyces cerevisiae Rab-GDI displacement factor ortholog Yip3p forms distinct complexes with the Ypt1 Rab GTPase and the reticulon Rtn1p. Geng, J., Shin, M.E., Gilbert, P.M., Collins, R.N., Burd, C.G. Eukaryotic Cell (2005) [Pubmed]
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