Letunic et al. (2017) Nucleic Acids Res doi: 10.1093/nar/gkx922
Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937

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Raptor_N Raptor N-terminal CASPase like domain

SMART accession number:	SM01302
Description:	This domain is found at the N-terminus of the Raptor protein. It has been identified to have a CASPase like structure PMID:15450605. It conserves the characteristic cys/his dyad of the caspases suggesting it may have a peptidase activity.
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) ].
Family alignment:	View or CHROMA formatHMM/Web logoCLUSTALW formatMSF formatFASTA formatPIR format

There are 1906 Raptor_N domains in 1904 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Taxonomic distribution of proteins containing Raptor_N domain.

  This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Raptor_N domain is also avaliable.

  Click on the protein counts, or double click on taxonomic names to display all proteins containing Raptor_N domain in the selected taxonomic class.

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Ginalski K, Zhang H, Grishin NV
  • Raptor protein contains a caspase-like domain.
  • Trends Biochem Sci. 2004; 29: 522-4
  • Display abstract

  • Using state-of-the-art sequence analysis and structure-prediction methods acaspase-like domain in the N-terminal region of raptor proteins has beenidentified. This domain, which is characterized by the presence of invariantcatalytic Cys-His dyad, is evolutionarily and structurally related to knowncaspases and might have protease activity. This finding suggests severalunexpected aspects of raptor function in the target of rapamycin (TOR) signaling pathway.

• Links (links to other resources describing this domain)

• INTERPRO	IPR029347
  PFAM	Raptor_N

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