VP6_ROTGA
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 12-AUG-2020, entry version 47.
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; Reoviridae; Sedoreovirinae; Rotavirus.
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}.
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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