VP6_ROTW3
ID VP6_ROTW3 Reviewed; 397 AA.
AC Q8JTI5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Intermediate capsid protein VP6 {ECO:0000255|HAMAP-Rule:MF_04129};
OS Rotavirus A (strain RVA/Cow/United States/WC3/1981/G6P7[5]) (RV-A)
OS (Rotavirus (strain Wistar calf 3)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=578828;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12018701; DOI=10.1023/a:1014512314545;
RA Ciarlet M., Hyser J.M., Estes M.K.;
RT "Sequence analysis of the VP4, VP6, VP7, and NSP4 gene products of the
RT bovine rotavirus WC3.";
RL Virus Genes 24:107-118(2002).
RN [2]
RP SEQUENCE REVISION.
RA Ciarlet M., Hyser J.M., Estes M.K.;
RL Submitted (OCT-2008) 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; AF411322; AAM73767.2; -; mRNA.
DR SMR; Q8JTI5; -.
DR Proteomes; UP000007181; 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 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_0000368174"
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; 44871 MW; 0241843253B49F25 CRC64;
MDVLYSLSKT LKDARDKIVE GTLYSNVSDL IQQFNQMIIT MNGNEFQTGG IGNLPIRNWN
FDFGLLGTTL LNLDANYVET ARNTIDYFVD FVDNVCMDEM VRESQRNGIA PQSDSLRKLS
GIKFKRINFD NSSEYIENWN LQNRRQRTGF TFHKPNIFPY SASFTLNRSQ PAHDNLMGTM
WLNAGSEIQV AGFDYSCAIN APANTQQFEH VVQLRRVLTT ATITLLPDAE RFSFPRVINS
ADGATTWYFN PVILRPNNVE VEFLLNGQII NTYQARFGTI IARNFDTIRL SFQLMRPPNM
TPAVAALFPN AQPFEHHATV GLTLRIESAV CESVLADASE TMLANVTSVR QEYAIPVGPV
FPPGMNWTDL ITNYSPSRED NLQRVFTVAS IRSMLVK
