ID VP6_ROTGA Reviewed; 391 AA. AC P26015; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 08-NOV-2023, entry version 49. DE RecName: Full=Intermediate capsid protein VP6 {ECO:0000255|HAMAP-Rule:MF_04126}; OS Rotavirus B (isolate RVB/Human/China/ADRV/1982) (RV-B) (Rotavirus B OS (isolate adult diarrhea rotavirus)). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus B. OX NCBI_TaxID=10942; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=1850929; DOI=10.1016/0042-6822(91)90623-j; RA Chen G.-M., Werner-Eckert R., Tao H., Mackow E.R.; RT "Expression of the major inner capsid protein of the group B rotavirus RT ADRV: primary characterization of genome segment 5."; RL Virology 182:820-829(1991). 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_04126}. CC -!- SUBUNIT: Homotrimer. Interacts with the inner capsid protein VP2. CC Interacts with the outer capsid glycoprotein VP7. {ECO:0000255|HAMAP- CC Rule:MF_04126}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04126}. 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_04126}. CC -!- SIMILARITY: Belongs to the rotavirus VP6 family. {ECO:0000255|HAMAP- CC Rule:MF_04126}. 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; M55982; AAA47353.1; -; Genomic_RNA. DR PIR; A39993; VPXRHB. 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: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 HAMAP; MF_04126; Rota_VP6; 1. DR InterPro; IPR001385; Rotavirus_A/C_VP6. PE 3: Inferred from homology; KW Capsid protein; Intermediate capsid protein; Virion. FT CHAIN 1..391 FT /note="Intermediate capsid protein VP6" FT /id="PRO_0000149566" SQ SEQUENCE 391 AA; 43671 MW; A20BBA506E9F1AC3 CRC64; MDLIETVNAC VKLQKRVLGL APNTNLNTAE QSVLNDYNAL PSRVNGKTYA LLNQIAVYTP YTINAPIISL AVRISTDDYD DMRSGIESIL DVLAAAIRTE GSRPTRVIER RVLEQNVKQL VDDLRLKSLI SDLSIANLAA VDTAMIQPEV IETENPLYAD IIEQIVHRPN IGMNGGNIRA TLGRWSGNKG VVTCMSGMDS EHRFTVELKT RTCGIINIVY IPTAGTILIP MPAGRNREGD LIDVSAEMMA DDFAIDFMDD DKIIQTETGV GVYSFPMCNR IRFRINPWNT QKDDDNLGTV HMINWAQGTA PKQPAISFMF ETRRTFTEGN YQHLSRCAPK AQYMMDTQFN DVSFTNRPAV DWNIQSLLTS NTQRVWCQKI AMLIAAFAAK I //