ID   VP6_ROTGI               Reviewed;         391 AA.
AC   Q01754;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Intermediate capsid protein VP6 {ECO:0000255|HAMAP-Rule:MF_04126};
OS   Rotavirus B (isolate RVB/Rat/United States/IDIR/1984/G1P[X]) (RV-B)
OS   (Rotavirus B (isolate infectious diarrhea of infant rats)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=28877;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1316675; DOI=10.1016/0042-6822(92)90512-n;
RA   Eiden J.J., Nataro J., Vonderfecht S., Petric M.;
RT   "Molecular cloning, sequence analysis, in vitro expression, and
RT   immunoprecipitation of the major inner capsid protein of the IDIR strain of
RT   group B rotavirus (GBR).";
RL   Virology 188:580-589(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}.
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DR   EMBL; M84456; AAA47348.1; -; mRNA.
DR   PIR; A42540; VPXRIB.
DR   PRIDE; Q01754; -.
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   2: Evidence at transcript level;
KW   Capsid protein; Intermediate capsid protein; Virion.
FT   CHAIN           1..391
FT                   /note="Intermediate capsid protein VP6"
FT                   /id="PRO_0000149567"
SQ   SEQUENCE   391 AA;  43646 MW;  C50C75F115F4BCD3 CRC64;
     MDLIETVNAC VGLQKRVLKL APNTNLNTAG QSVLNDYNAL ASRVNGRTYA LLDQTAVYTP
     YTVNAPIISL AVRISTDDYD DMRSGIDSIL DILAAAIRTE GSRPTRVIER RVIEPNVKQL
     VEDLKLKSLT SEISIANMAA VDTALIQPEI IETENPLFAD IIEQVIHRPN ASMTGGNIRA
     TLGRWSGNKG IVTCMSGMDS EHRFTVDFKT RTCGIINVVY APTAGVIMIP MPTGRNREGH
     LIDVSAEMMA ENFAIDFMDD DDIIQTETGV GVFSFPMCNR IRFRINPWDM QKHNDNLWTV
     NLANWPQGTS PRQPAISFLF ETRRTFTEGD YQHLSRCAPK VQYMMDTIFP ETAFTNRPVV
     DWNVQSLLTS SSQKTWCQKI AMLIAAYAAK I