Matrix protein. Nucleocapsid protein. Capsid protein. Interacts with host DYNLT1; this interaction probably targets the viral polyproteins to the cytoplasmic assembly site. 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. 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 conventional translation.