ID VP6_ROTH6 Reviewed; 397 AA. AC B1NKQ8; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 22-FEB-2023, entry version 46. DE RecName: Full=Intermediate capsid protein VP6 {ECO:0000255|HAMAP-Rule:MF_04129}; OS Rotavirus A (strain RVA/Human/Indonesia/69M/1980/G8P4[10]) (RV-A). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A. OX NCBI_TaxID=10947; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=18216098; DOI=10.1128/jvi.02257-07; RA Matthijnssens J., Ciarlet M., Heiman E.M., Arijs I., Delbeke T., RA McDonald S.M., Palombo E.A., Iturriza-Gomara M., Maes P., Patton J.T., RA Rahman M., Van Ranst M.; RT "Full genome-based classification of rotaviruses reveals a common origin RT between human Wa-Like and porcine rotavirus strains and human DS-1-like and RT bovine rotavirus strains."; RL J. Virol. 82:3204-3219(2008). 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. {ECO:0000255|HAMAP- CC Rule:MF_04129}. 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*. {ECO:0000255|HAMAP-Rule:MF_04129}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04129}. CC Note=Component of the intermediate capsid. Also found in spherical CC cytoplasmic structures, called virus factories, that appear early after CC infection and are the site of viral replication and packaging. CC {ECO:0000255|HAMAP-Rule:MF_04129}. CC -!- PTM: The N-terminus is blocked. {ECO:0000255|HAMAP-Rule:MF_04129}. CC -!- PTM: Sumoylated with SUMO1 and SUMO2. Sumoylation of viral proteins CC seems to have a positive role on viral replication. {ECO:0000255|HAMAP- CC Rule:MF_04129}. 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. {ECO:0000255|HAMAP-Rule:MF_04129}. CC -!- SIMILARITY: Belongs to the rotavirus VP6 family. {ECO:0000255|HAMAP- CC Rule:MF_04129}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EF583016; ABU87825.1; -; Genomic_RNA. DR SMR; B1NKQ8; -. DR Proteomes; UP000001455; Genome. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule. DR GO; GO:0039626; C:viral intermediate capsid; IEA:UniProtKB-UniRule. DR GO; GO:0046789; F:host cell surface receptor binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule. DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule. DR Gene3D; 2.60.120.170; -; 1. DR Gene3D; 1.10.1350.10; Viral capsid alpha domain; 1. DR HAMAP; MF_04126; Rota_VP6; 1. DR HAMAP; MF_04129; Rota_VP6_A; 1. DR InterPro; IPR008980; Capsid_hemagglutn. DR InterPro; IPR001385; Rotavirus_A/C_VP6. DR InterPro; IPR008935; Virus_capsid_a-hlx_vir. DR Pfam; PF00980; Rota_Capsid_VP6; 1. DR SUPFAM; SSF48345; A virus capsid protein alpha-helical domain; 1. DR SUPFAM; SSF49818; Viral protein domain; 1. PE 3: Inferred from homology; KW Calcium; Capsid protein; Intermediate capsid protein; Metal-binding; KW Ubl conjugation; Virion; Zinc. FT CHAIN 1..397 FT /note="Intermediate capsid protein VP6" FT /id="PRO_0000368175" FT REGION 62..73 FT /note="Interaction with the inner capsid protein VP2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04129" FT BINDING 153 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between all trimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04129" FT BINDING 266 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04129" FT BINDING 286 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04129" SQ SEQUENCE 397 AA; 44814 MW; 4B876883EA5E63C1 CRC64; MDVLYSLSKT LKDARDKIVE GTLYSNVSDL IQQFNQMIIT MNGTEFQTGG IGNLPIRNWN FGFGLLGTTL LNLDANYVET ARNTIDYFVD FVDNVCMDEM VRESQRNGIA PQSDSLRKLS GIKFKRINFD NSSEYIENWN LQNRRQRTGF TFHKPNIFPY SASFTLNRSQ PAHDNLMGTM WLNAGSEIQV AGFDYSCAIN APANTQQFEH IVQLRRVLTT ATITLLPDAE RFSFPRVINS ADGATTWYFN PVILRPNNVE VEFLLNGQII NTYQARFGTI IARNFDTIRL SFQLMRPPNM TPAVAALFPN AQPFEHHATV GLTLRIESAV CESVLADASE TMLANVTSVR QEYAIPVGPV FPPGMNWTDL ITNYSPSRED NLQRVFTVAS IRSMLVK //