ID   VP6_ROTHG               Reviewed;         395 AA.
AC   P69483; P30213;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   08-NOV-2023, entry version 61.
DE   RecName: Full=Intermediate capsid protein VP6 {ECO:0000255|HAMAP-Rule:MF_04126};
OS   Rotavirus C (isolate RVC/Human/United Kingdom/Preston/1992) (RV-C).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus C.
OX   NCBI_TaxID=31568;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1326817; DOI=10.1016/0042-6822(92)91248-s;
RA   Cooke S.J., Clarke I.N., Freitas R.B., Gabbay Y.B., Lambden P.R.;
RT   "The correct sequence of the porcine group C/Cowden rotavirus major inner
RT   capsid protein shows close homology with human isolates from Brazil and the
RT   U.K.";
RL   Virology 190:531-537(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; M94156; AAA47340.1; -; Genomic_RNA.
DR   PIR; A41041; VPXRCR.
DR   SMR; P69483; -.
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   3: Inferred from homology;
KW   Capsid protein; Intermediate capsid protein; Virion.
FT   CHAIN           1..395
FT                   /note="Intermediate capsid protein VP6"
FT                   /id="PRO_0000149571"
SQ   SEQUENCE   395 AA;  44720 MW;  BD1CF809C0D5E269 CRC64;
     MDVLFSIAKT VSDLKKKVVV GTIYTNVEDV VQQTNELIRT LNGNIFHTGG IGTQPQKEWN
     FQLPQLGTTL LNLDDNYVQS TRGIIDFLSS FIEAVCDDEI VREASRNGMQ PQSPALILLS
     SSKFKTINFN NSSQSIKNWN AQSRRENPVY EYKNPMLFEY KNSYILQRAN PQFGSVMGLR
     YYTTSNTCQI AAFDSTLAEN APNNTQRFVY NGRLKRPISN VLMKIEAGAP NISNPTILPD
     PNNQTTWLFN PVQLMNGTFT IEFYNNGQLI DMVRNMGIVT VRTFDSYRIT IDMIRPAAMT
     QYVQRIFPQG GPYHFQATYM LTLSILDATT ESVLCDSHSV EYSIVANVRR DSAMPAGTVF
     QPGFPWEHTL SNYTVAQEDN LERLLLIASV KRMVM
//