Matrix protein. Nucleocapsid protein p14: Nucleocapsid protein. Capsid protein. The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Enhances the activity of the reverse transcriptase. May be part of the mature RT. dUTP + H2O = diphosphate + dUMP + H(+) Homodimer (By similarity). Interacts with the reverse transcriptase/ribonuclease H (PubMed:22171253). Homotrimer (PubMed:17169987). Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. Phosphorylated protein pp24 and phosphorylated protein pp18 contains two L domains: a PTAP/PSAP motif which interacts with the UEV domain of TSG101, and a PPXY motif which binds to the WW domains of the ubiquitin ligase NEDD4. Both motifs contribute to viral release. The PSAP motif acts as an additional L domain and promotes the efficient release of the virions but requires an intact PPPY motif to perform its function. The glycine-rich G-patch domain (GPD) is present at the C-terminus of the protease from which it is then detached by the protease itself. Released by autocatalytic processing. The protease can undergo further autoprocessing to yield 2 shorter but enzymatically active forms of 12 kDa and 13 kDa without the GDP domain. the 12 kDa form is monomeric. Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles. Specific enzymatic cleavages in vivo yield mature proteins. Produced by -1 ribosomal frameshifting between gag-pro.