AC MF_04129; DC Protein; auto TR HAMAP; MF_04129; -; 1; level=0 XX Names: Rota_VP6_A XX ID VP6 DE RecName: Full=Intermediate capsid protein VP6; XX CC -!- FUNCTION: Intermediate capsid protein that self assembles to form an CC icosahedral capsid with a T=13 symmetry, which consists of 230 trimers CC of VP6, with channels at each of its five-fold vertices. This capsid CC constitutes the middle concentric layer of the viral mature particle. CC The innermost VP2 capsid and the intermediate VP6 capsid remain intact CC following cell entry to protect the dsRNA from degradation and to CC prevent unfavorable antiviral responses in the host cell during all the CC replication cycle of the virus. Nascent transcripts are transcribed CC within the structural confines of this double-layered particle (DLP) CC and are extruded through the channels at the five-fold axes. VP6 is CC required for the transcription activity of the DLP. CC -!- SUBCELLULAR LOCATION: Virion. Note=Component of the intermediate CC capsid. Also found in spherical cytoplasmic structures, called virus CC factories, that appear early after infection and are the site of viral CC replication and packaging. CC -!- SUBUNIT: Homotrimer. Interacts with the inner capsid protein VP2. CC Interacts with the outer capsid glycoprotein VP7. Interacts with the CC outer capsid protein VP5*. CC -!- PTM: The N-terminus is blocked. CC -!- PTM: Sumoylated with SUMO1 and SUMO2. Sumoylation of viral proteins CC seems to have a positive role on viral replication. CC -!- MISCELLANEOUS: The VP6 trimer contains a zinc ion located at the center CC of the molecule. The zinc ion is not essential for either trimerization CC or transcription activity of the DLP. Zinc-depleted VP6 has an CC increased sensitivity to proteases. CC -!- SIMILARITY: Belongs to the rotavirus VP6 family. XX DR Pfam; PF00980; Rota_Capsid_VP6; 1; trigger=no XX KW Calcium KW Metal-binding KW Zinc KW Ubl conjugation KW Capsid protein KW Intermediate capsid protein KW Virion XX GO GO:0019031; C:viral envelope GO GO:0039626; C:viral intermediate capsid GO GO:0046789; F:host cell surface receptor binding GO GO:0005198; F:structural molecule activity GO GO:0019064; P:fusion of virus membrane with host plasma membrane GO GO:0046872; F:metal ion binding XX FT From: VP6_ROTRF (P04509) FT BINDING 153 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between all trimeric FT partners" FT Condition: H FT BINDING 266 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Condition: N FT BINDING 286 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Condition: D FT From: VP6_ROTSH (P04509) FT REGION 62..73 FT /note="Interaction with the inner capsid protein VP2" XX Size: 390-400; Related: MF_04126; Template: P04509; A2T3T0; P18610; Q91N61; Scope: Viruses; Rotavirus Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.5 2022/11/19 //