ID   VP6_ROTS1               Reviewed;         397 AA.
AC   P03531; Q6Y3A1; Q86230;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Intermediate capsid protein VP6 {ECO:0000255|HAMAP-Rule:MF_04129};
OS   Rotavirus A (strain RVA/SA11-Both/G3P5B[2]) (RV-A) (Simian Agent 11 (strain
OS   Both)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=37137;
OH   NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2551775; DOI=10.1016/0378-1119(89)90206-0;
RA   Smith R.E., Kister S.E., Carozzi N.B.;
RT   "Cloning and expression of the major inner capsid protein of SA-11 simian
RT   rotavirus in Escherichia coli.";
RL   Gene 79:239-248(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6322125; DOI=10.1093/nar/12.4.1875;
RA   Estes M.K., Mason B.B., Crawford S.E., Cohen J.;
RT   "Cloning and nucleotide sequence of the simian rotavirus gene 6 that codes
RT   for the major inner capsid protein.";
RL   Nucleic Acids Res. 12:1875-1887(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=6328048; DOI=10.1128/jvi.51.1.97-101.1984;
RA   Both G.W., Siegman L.J., Bellamy A.R., Ikegami N., Shatkin A.J.,
RA   Furuichi Y.;
RT   "Comparative sequence analysis of rotavirus genomic segment 6 -- the gene
RT   specifying viral subgroups 1 and 2.";
RL   J. Virol. 51:97-101(1984).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate temperature-sensitive mutant G;
RX   PubMed=8091686; DOI=10.1006/viro.1994.1511;
RA   Mansell E.A., Ramig R.F., Patton J.T.;
RT   "Temperature-sensitive lesions in the capsid proteins of the rotavirus
RT   mutants tsF and tsG that affect virion assembly.";
RL   Virology 204:69-81(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Mitchell D.B., Both G.W.;
RT   "Complete nucleotide sequence of Simian rotavirus.";
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
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_04129}.
CC   -!- SUBUNIT: Homotrimer. Interacts with the inner capsid protein VP2.
CC       Interacts with the outer capsid glycoprotein VP7. Interacts with the
CC       outer capsid protein VP5*. {ECO:0000255|HAMAP-Rule:MF_04129}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04129}.
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_04129}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000255|HAMAP-Rule:MF_04129}.
CC   -!- PTM: Sumoylated with SUMO1 and SUMO2. Sumoylation of viral proteins
CC       seems to have a positive role on viral replication. {ECO:0000255|HAMAP-
CC       Rule:MF_04129}.
CC   -!- MISCELLANEOUS: The VP6 trimer contains a zinc ion located at the center
CC       of the molecule. The zinc ion is not essential for either trimerization
CC       or transcription activity of the DLP. Zinc-depleted VP6 has an
CC       increased sensitivity to proteases. {ECO:0000255|HAMAP-Rule:MF_04129}.
CC   -!- SIMILARITY: Belongs to the rotavirus VP6 family. {ECO:0000255|HAMAP-
CC       Rule:MF_04129}.
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DR   EMBL; M27824; AAA47397.1; -; Genomic_RNA.
DR   EMBL; X00421; CAA25122.1; -; Genomic_RNA.
DR   EMBL; AY187029; AAO32085.1; -; Genomic_RNA.
DR   EMBL; L15384; AAA65638.1; -; Genomic_RNA.
DR   PIR; A93002; VPXR6S.
DR   PIR; JQ0019; VPXR11.
DR   SMR; P03531; -.
DR   Proteomes; UP000007180; Genome.
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:0046872; F:metal ion 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   HAMAP; MF_04129; Rota_VP6_A; 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   3: Inferred from homology;
KW   Calcium; Capsid protein; Intermediate capsid protein; Metal-binding;
KW   Reference proteome; Ubl conjugation; Virion; Zinc.
FT   CHAIN           1..397
FT                   /note="Intermediate capsid protein VP6"
FT                   /id="PRO_0000149577"
FT   REGION          62..73
FT                   /note="Interaction with the inner capsid protein VP2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04129"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="ligand shared between all trimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04129"
FT   BINDING         266
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04129"
FT   BINDING         286
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04129"
FT   VARIANT         10
FT                   /note="T -> S (in strain: Isolate temperature-sensitive
FT                   mutant G)"
FT   VARIANT         13
FT                   /note="D -> H (in strain: Isolate temperature-sensitive
FT                   mutant G)"
FT   VARIANT         121
FT                   /note="A -> G (in strain: Isolate temperature-sensitive
FT                   mutant G)"
FT   CONFLICT        164
FT                   /note="F -> Y (in Ref. 3 and 5; AAO32085)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        385
FT                   /note="V -> I (in Ref. 3 and 5; AAO32085)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   397 AA;  44873 MW;  39FAC6E17AE42A46 CRC64;
     MDVLYSLSKT LKDARDKIVE GTLYSNVSDL IQQFNQMIIT MNGNEFQTGG IGNLPIRNWN
     FNFGLLGTTL LNLDANYVET ARNTIDYFVD FVDNVCMDEM VRESQRNGIA PQSDSLRKLS
     AIKFKRINFD NSSEYIENWN LQNRRQRTGF TFHKPNIFPY SASFTLNRSQ PAHDNLMGTM
     WLNAGSEIQV AGFDYSCAIN APANIQQFEH IVPLRRVLTT ATITLLPDAE RFSFPRVINS
     ADGATTWFFN PVILRPNNVE VEFLLNGQII NTYQARFGTI VARNFDTIRL SFQLMRPPNM
     TPAVAVLFPN AQPFEHHATV GLTLRIESAV CESVLADASE TLLANVTSVR QEYAIPVGPV
     FPPGMNWTDL ITNYSPSRED NLQRVFTVAS IRSMLIK