Endoplasmic protein tyrosine phosphatase

Gu, F., Nguyen, D.T., Stuible, M., Dube, N., Tremblay, M.L. and Chevet, E. (2004) Protein-tyrosine phosphatase IB potentiates IREl signaling during endoplasmic reticulum stress. J. Biol. Chem. 279, 49689-49693. 

Fig. 4. The domain organizations of some CUE and LIP domain-containing proteins. Yeast Der3p/Hrdlp and Cuelp are proteins of the endoplasmic reticulum degradation pathway. As human autocrine motility factor receptor (AMFR) contains the same domain organization of a conceptual Der3p/Hrdlp and Cuelp fusion, it is proposed that DerSp/Hrdlp and Cuelp interact physically (Pouting, 2000). The C. elegans sequence most similar to human Tollip contains a C-terminal extension containing an F-box domain and an incomplete LIP domain. Over 190 LIP domains occur in at least 172 C. elegans hypothetical proteins, but have not been observed in other species sequences the functions of this domain remain unknown. LIP domains frequently co-occur with F-box domains and in one case (C33F10.8) a protein tyrosine phosphatase-like (FTP) domain.

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