Involved in capsid formation and genome binding. Shortly after infection, interaction between incoming particle-associated Gag proteins and host dynein allows centrosomal targeting of the viral genome (associated to Gag), prior to nucleus translocation and integration into host genome (By similarity). Gag protein specifically interacts with the N-terminus of leader peptide. This specific interaction between Gag protein and Env glycoprotein may compensate for the lack of a Gag membrane targeting signal, and allow particle egress. The capsid is composed of multimeric Gag protein. Interacts with host TSG101. Interacts with host light chain cytoplasmic dynein DYNLL1; this interaction is critical for intracellular microtubule-dependent viral genome transport toward the centrosome (By similarity). Nuclear at initial phase, cytoplasmic at assembly. Shortly after infection, Gag protein is targeted to centrosomes. It is then actively transported into the nucleus thanks to its nuclear localization signal. In the late phases of infection, Gag proteins assemble in the cytoplasm to form the virion's capsids (By similarity). Gag protein contains 3 glycine-arginine motifs (GR-boxes) necessary for RNA packaging, the first of which has nucleic acid binding properties in vitro. Late-budding 'domains' (L domains) are short sequence motifs essential for viral particle budding. They recruit proteins of the host ESCRT machinery (Endosomal Sorting Complex Required for Transport) or ESCRT-associated proteins. Nucleocapsid protein p14 contains one L domain: a PTAP/PSAP motif, which interacts with the UEV domain of TSG101 (By similarity). Specific enzymatic cleavages in vivo by viral protease yield mature proteins. The protease is not cleaved off from Pol. Since cleavage efficiency is not optimal for all sites, intermediary molecules are expressed (By similarity). Foamy viruses are distinct from other retroviruses in many respects. Their protease is active as an uncleaved Pro-Pol protein. Mature particles do not include the usual processed retroviral structural protein (MA, CA and NC), but instead contain two large Gag proteins. Their functional nucleic acid appears to be either RNA or dsDNA (up to 20% of extracellular particles), because they probably proceed either to an early (before integration) or late reverse transcription (after assembly). Foamy viruses have the ability to retrotranspose intracellularly with high efficiency. They bud predominantly into the endoplasmic reticulum (ER) and occasionally at the plasma membrane. Budding requires the presence of Env proteins. Most viral particles probably remain within the infected cell.