SMART: Pfam domain Raptor

Raptor_N

PFAM accession number:	PF14538
Interpro abstract (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 [ (PUBMED:12150925) ]. 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 [ (PUBMED:12150925) (PUBMED:12150926) ]. 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 [ (PUBMED:15450605) ].

PFAM accession number:

PF14538

Interpro abstract (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 [ (PUBMED:12150925) ].

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 [ (PUBMED:12150925) (PUBMED:12150926) ].

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 [ (PUBMED:15450605) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Raptor_N