Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence. Targets the polyprotein to the plasma membrane. Forms the core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Encapsulates and protects viral dimeric unspliced genomic RNA (gRNA). Binds these RNAs through its zinc fingers. Acts as a nucleic acid chaperone which is involved in rearrangement of nucleic acid secondary structure during gRNA retrotranscription. Also facilitates template switch leading to recombination. 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. Specific enzymatic cleavages by the viral protease yield mature proteins. Produced by conventional translation. Belongs to the Ovine/caprine lentivirus group gag polyprotein family. Extended N-terminus.