Matrix protein p16 forms the outer shell of the core of the virus, lining the inner surface of the viral membrane. Capsid protein p26 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex. Interaction between incoming particle-associated Gag proteins and host dynein allows intracellular microtubule-dependent virus transport toward the perinuclear region, prior to nucleus translocation and integration into host genome. Nucleocapsid protein p13 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity). Interacts with host light chain cytoplasmic dynein DYNLL1; this interaction is critical for intracellular microtubule-dependent viral genome transport. This strategy of translation probably allows the virus to modulate the quantity of each viral protein. 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. Gag polyprotein contains one L domain: a PTAP/PSAP motif, which interacts with the UEV domain of TSG101 (By similarity). The sequence shown is that of isolate R29-127. Produced by conventional translation. Belongs to the bovine lentivirus group gag polyprotein family.