Prenylated Rab acceptor protein 1 (RABAC1)

Prenylated Rab acceptor protein 1 (RABAC1, also known as PRA1) is a highly conserved, multi-pass integral membrane protein primarily localized to the Golgi apparatus and also found at endoplasmic reticulum (ER)–mitochondria membrane contact sites. RABAC1 binds prenylated Rab GTPases and helps direct their proper targeting to distinct membrane compartments, thereby regulating vesicular trafficking and protein transport[1][2]. It interacts with various proteins involved in cell signaling and trafficking, including α-synuclein and viral proteins, indicating its functional relevance to intracellular signaling, lipid metabolism, and potential disease processes. RABAC1 exhibits tumor-suppressive activity in certain contexts by promoting apoptosis and inhibiting cancer cell migration and proliferation. It is downregulated in models of retinal degeneration, highlighting a possible role in neurodegeneration. Despite early hypotheses of its function as a general Rab GTPase regulator, recent studies suggest it may also have specialized roles in lipid handling and maintenance of early secretory pathway integrity[1][2].

Other names

PRA1PRAF1YIP3PRA1 family protein 1PRA1 domain family 1Rab acceptor 1 (prenylated)prenylated Rab acceptor 1prenylated Rab acceptor protein 1RABAC1