ID VP6_ROTBS Reviewed; 395 AA. AC Q00734; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 08-NOV-2023, entry version 79. DE RecName: Full=Intermediate capsid protein VP6 {ECO:0000255|HAMAP-Rule:MF_04126}; OS Rotavirus C (isolate RVC/Cow/Japan/Shintoku/1991/G2P[3]) (RV-C). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus C. OX NCBI_TaxID=33723; OH NCBI_TaxID=9913; Bos taurus (Bovine). RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1326819; DOI=10.1016/0042-6822(92)91250-x; RA Jiang B., Tsunemitsu H., Gentsch J.R., Glass R.I., Green K.Y., Qian Y.A., RA Saif L.J.; RT "Nucleotide sequence of gene 5 encoding the inner capsid protein (VP6) of RT bovine group C rotavirus: comparison with corresponding genes of group C, RT A, and B rotaviruses."; RL Virology 190:542-547(1992). 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; M88768; AAA03235.1; -; mRNA. DR PIR; A43386; A43386. DR SMR; Q00734; -. 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 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 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 2: Evidence at transcript level; KW Capsid protein; Intermediate capsid protein; Virion. FT CHAIN 1..395 FT /note="Intermediate capsid protein VP6" FT /id="PRO_0000149563" SQ SEQUENCE 395 AA; 44534 MW; 0CDD6C52F8853816 CRC64; MDVLFSIAKT VSELKKRVVV GTIYTNVEDI IQQTNELIRT LNGSTFHTGG IGTQPQKDWV VQLPQLGTTL LNLDDNYVQS ARGIIDYLAS FIEAVCDDEM VREASRNGMQ PQSPTLIALA SSKFKTINFN NSSQSIKNWS AQSRRENPVY EYKNPMVFEY RNSYILHRAD QQFGNAMGLR YYTTSNTCQI AAFDSTMAEN APNNTQRFIY HGRLKRPISN VLMKVERGAP NVNNPTILPD PTNQTTWLFN PVQVMNGTFT IEFYNNGQLV DMVRNMGIAT VRTFDSYRIT IDMIRPAAMT QYVQQLFPVG GPYSHQAAYM LTLSVLDATT ESVLCDSHSV DYSIVANTRR DSAMPAGTVF QPGFPWEQTL SNYTVAQEDN LERLLLVASV KRMVM //