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   02-DEC-2020, entry version 76.
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; Reoviridae; Sedoreovirinae; Rotavirus.
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}.
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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   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; SSF48345; 1.
DR   SUPFAM; SSF49818; SSF49818; 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