Rabbit haemorrhagic disease virus (RHDV) is a highly virulent and species-specific virus of the European rabbit (Oryctolagus cuniculus). Little is known about the molecular biology and virulence mechanisms of RHDV, mainly due to the lack of an effective cell culture system. Many non-structural viral proteins determine critical replication strategies and influence host cell responses to infection. Identifying the intracellular compartment in which viral proteins accumulate is often the key to understanding protein functions and the knowledge of their subcellular localisation may even point to possible host cell interaction partners. To increase our understanding of RHDV replication, we investigated the subcellular localisation of all RHDV non-structural proteins and observed a wide range of different localisation patterns in transiently transfected cells. While some proteins did not associate with any distinct structures or compartments in the cells (e.g. VPg and the protease), others showed a defined subcellular localisation (e.g. p16, p23, the helicase, p29 and the polymerase). Furthermore, we show evidence for oligomerisation of p23 and an ability of the viral protease to cleave the p16:p23 junction in trans, i.e. outside the context of the nascent polyprotein chain. Notably, expression of the viral polymerase alone and in the context of the entire RHDV polyprotein resulted in a redistribution of the Golgi network. This suggests that, similar to other positive-strand RNA viruses, RHDV may recruit membranes of the secretory pathway during replication, and that the viral polymerase may play a critical role during this process.