Ras converting CAAX endopeptidase 1 (RCE1)

Ras converting CAAX endopeptidase 1 (RCE1) is an integral membrane enzyme located in the endoplasmic reticulum that functions as an intramembrane metalloproteinase. It cleaves the C-terminal tripeptide ("-AAX") from prenylated proteins containing a CAAX motif, including the Ras family of small GTPases, nuclear lamins, and various protein kinases and phosphatases. This post-translational modification is essential for correct localization and function of these proteins, many of which are involved in key cellular signaling pathways. Disruption of RCE1 activity affects multiple signaling proteins and has been linked to cancer and other diseases, making RCE1 a potential therapeutic target under active investigation[1][2][3][5].

Other names

CAAX prenyl protease 2FACE2FACE-2FACE2_HUMANhRCE1RCE1ARCE1BFarnesylated proteins-converting enzyme 2Prenyl protein-specific endoprotease 2RCE1 homologPrenyl protein peptidaseType II CAAX prenyl endopeptidase

Inhibition of RCE1 disrupts cleavage of CAAX motif, leading to mislocalization and impaired function of Ras and other prenylated proteins