VP6_ROTBU
ID VP6_ROTBU Reviewed; 397 AA.
AC P18610;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Intermediate capsid protein VP6 {ECO:0000255|HAMAP-Rule:MF_04129};
OS Rotavirus A (strain RVA/Cow/United Kingdom/UK/1975/G6P7[5]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10934;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2168543; DOI=10.1093/nar/18.16.4921;
RA Tarlow O., McCrae M.A.;
RT "Nucleotide sequence of group antigen (VP6) of the UK tissue culture
RT adapted strain of bovine rotavirus.";
RL Nucleic Acids Res. 18:4921-4921(1990).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS), INTERACTION WITH THE INNER CAPSID
RP PROTEIN VP2, SUBUNIT, AND FUNCTION.
RX PubMed=20122940; DOI=10.1016/j.jmb.2010.01.055;
RA McClain B., Settembre E., Temple B.R., Bellamy A.R., Harrison S.C.;
RT "X-ray crystal structure of the rotavirus inner capsid particle at 3.8 A
RT resolution.";
RL J. Mol. Biol. 397:587-599(2010).
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
CC (PubMed:20122940). This capsid constitutes the middle concentric layer
CC of the viral mature particle (PubMed:20122940). The innermost VP2
CC capsid and the intermediate VP6 capsid remain intact following cell
CC entry to protect the dsRNA from degradation and to prevent unfavorable
CC antiviral responses in the host cell during all the replication cycle
CC of the virus (By similarity). 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
CC (PubMed:20122940). VP6 is required for the transcription activity of
CC the DLP (By similarity). {ECO:0000255|HAMAP-Rule:MF_04129,
CC ECO:0000269|PubMed:20122940}.
CC -!- SUBUNIT: Homotrimer (PubMed:20122940). Interacts with the inner capsid
CC protein VP2 (PubMed:20122940). Interacts with the outer capsid
CC glycoprotein VP7. Interacts with the outer capsid protein VP5*.
CC {ECO:0000255|HAMAP-Rule:MF_04129, ECO:0000269|PubMed:20122940}.
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; X53667; CAA37708.1; -; Genomic_RNA.
DR PDB; 3KZ4; X-ray; 3.80 A; C/D/E/F/G/H/I/J/K/L/M/N/O=1-397.
DR PDBsum; 3KZ4; -.
DR SMR; P18610; -.
DR Proteomes; UP000008657; Genome.
DR GO; GO:0039621; C:T=13 icosahedral viral capsid; IDA:UniProtKB.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0039626; C:viral intermediate capsid; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Capsid protein; Intermediate capsid protein;
KW Metal-binding; Ubl conjugation; Virion; Zinc.
FT CHAIN 1..397
FT /note="Intermediate capsid protein VP6"
FT /id="PRO_0000149562"
FT REGION 62..73
FT /note="Interaction with the inner capsid protein VP2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04129,
FT ECO:0000269|PubMed:20122940"
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; 44876 MW; 10F65E5FFB71F2AA CRC64;
MDVLYSLSKT LKDARDKIVE GTLYSNVSDL IQQFNQMIIT MNGNEFQTGG IGNLPIRNWN
FDFGLLGTTL LNLDANYVET ARNTIDYFVD FVDNVCMDEM VRESQRNGIA PQSDSLRKLS
GIKFKRINFD NSSEYIENWN LQNRRQRTGF TFHKPNIFPY SASFTLNRSQ PAHDNLMGTM
WLNAGSEIQV AGFDYSCAIN APANTQQFEH IVQLRRVLTT ATITLLPDAE RFSFPRVINS
ADGATTWYFN PVILRPNNVE VEFLLNGQII NTYQARFGTI IARNFDTIRL SFQLMRPPNM
TPAVAALFPN AQPFEHQATV GLTLRIESAV CESVLADASE TMLANVTSVR QEYAIPVGPV
FPPGMNWTDL ITNYSPSRED NLQRVFTVAS IRSMLVK
