Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices (PubMed:11285213). This capsid constitutes the middle concentric layer of the viral mature particle (PubMed:11285213). The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes (By similarity). VP6 is required for the transcription activity of the DLP (PubMed:12097594). Homotrimer (PubMed:11285213). Interacts with the inner capsid protein VP2 (PubMed:12097594, PubMed:11285213). Interacts with the outer capsid glycoprotein VP7 (PubMed:11285213, PubMed:19487668). Interacts with the outer capsid protein VP5* (By similarity). Component of the intermediate capsid (PubMed:11285213). Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging (Potential). The N-terminus is blocked. Sumoylated with SUMO1 and SUMO2. Sumoylation of viral proteins seems to have a positive role on viral replication. The VP6 trimer contains a zinc ion located at the center of the molecule (PubMed:11285213). The zinc ion is not essential for either trimerization or transcription activity of the DLP. Zinc-depleted VP6 has an increased sensitivity to proteases (PubMed:12610135). Belongs to the rotavirus VP6 family.