InterPro domain: IPR029347

Human Raptor is involved in the control of the mammalian target of rapamycin complex 1 (mTORC1) activity which regulates cell growth and survival, and autophagy in response to nutrient and hormonal signals. It functions as a scaffold for recruiting mTORC1 substrates [ 1 ].

All Raptor orthologs contain a unique conserved region in their N-terminal half (raptor N-terminal conserved, also called the RNC domain) followed by three HEAT (huntingtin, elongation factor 3, A subunit of protein phosphatase 2A and TOR1) repeats and seven WD-40 repeats near the C terminus [ 2 , 2 ].

This entry reprsents the RNC domain, which consists of 3 blocks with at least 67 to 79% sequence similarity and is predicted to have a high propensity to form alpha helices. The RNC domain is characterised by the presence of invariant catalytic Cys-His dyad, which is structurally and evolutionarily related to known caspases, suggesting that the raptor proteins may have protease activity [ 3 ].

1. mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell 110, 163-75
2. Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action. Cell 110, 177-89
3. Raptor protein contains a caspase-like domain. Trends Biochem. Sci. 29, 522-4