ID   VP6_ROTE1               Reviewed;         397 AA.
AC   P16592;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Intermediate capsid protein VP6 {ECO:0000255|HAMAP-Rule:MF_04129};
OS   Rotavirus A (strain RVA/Equine/United States/FI-14/1980/G3P4[12]) (RV-A)
OS   (Rotavirus A (strain FI14)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; unclassified Rotavirus.
OX   NCBI_TaxID=36442;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2455770; DOI=10.1099/0022-1317-69-7-1659;
RA   Gorziglia M., Hoshino Y., Nishikawa K., Maloy W.L., Jones R.W.,
RA   Kapikian A.Z., Chanock R.M.;
RT   "Comparative sequence analysis of the genomic segment 6 of four rotaviruses
RT   each with a different subgroup specificity.";
RL   J. Gen. Virol. 69:1659-1669(1988).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D00323; BAA00235.1; -; mRNA.
DR   SMR; P16592; -.
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   2: Evidence at transcript level;
KW   Calcium; Capsid protein; Intermediate capsid protein; Metal-binding;
KW   Ubl conjugation; Virion; Zinc.
FT   CHAIN           1..397
FT                   /note="Intermediate capsid protein VP6"
FT                   /id="PRO_0000149564"
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"
SQ   SEQUENCE   397 AA;  44935 MW;  563314ECE9A59B81 CRC64;
     MEVLYSISKT LKDARDKIVE GTLYSNVSDI IQQFNQIIVT MNGNEFQTGG IGTLPIRNWT
     FDFGLLGTTL LNLDANYVET ARTTIEYFID FIDNVCMDEM TRESQRNGIA PQSDALRKLS
     GIKFKRINFD NSSEYIENWN LQNRRQRTGF VFHKPNIFPY SASFTLNRSQ PLHNDLMGTM
     WLNAGSEIQV AGFDYSCAIN APANTQQFEH IVQLRRALTT ATITILPDAE RFSFPRVINS
     ADGATTWFFN PVILRPNNVE VEFLLNGQII NTYQARFGTI IARNFDTIRL SFQLMRPPNM
     TPAVNALFPQ AQPFQHHATV GLTLRIDSAV CESVLADSNE TMLANVTAVR QEYAVPVGPV
     FPPGMNWTEL ITNYSPSRED NLQRVFTVAS IRSMLIK