Structural highlights
Function
NACA_HUMAN Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER). Binds to nascent polypeptide chains as they emerge from the ribosome and blocks their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. Also reduces the inherent affinity of ribosomes for protein translocation sites in the ER membrane (M sites). May act as a specific coactivator for JUN, binding to DNA and stabilizing the interaction of JUN homodimers with target gene promoters.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Moller I, Beatrix B, Kreibich G, Sakai H, Lauring B, Wiedmann M. Unregulated exposure of the ribosomal M-site caused by NAC depletion results in delivery of non-secretory polypeptides to the Sec61 complex. FEBS Lett. 1998 Dec 11;441(1):1-5. PMID:9877153
- ↑ Beatrix B, Sakai H, Wiedmann M. The alpha and beta subunit of the nascent polypeptide-associated complex have distinct functions. J Biol Chem. 2000 Dec 1;275(48):37838-45. PMID:10982809 doi:10.1074/jbc.M006368200
- ↑ Lopez S, Stuhl L, Fichelson S, Dubart-Kupperschmitt A, St Arnaud R, Galindo JR, Murati A, Berda N, Dubreuil P, Gomez S. NACA is a positive regulator of human erythroid-cell differentiation. J Cell Sci. 2005 Apr 15;118(Pt 8):1595-605. Epub 2005 Mar 22. PMID:15784678 doi:jcs.02295
