VP6_ROTSH
ID VP6_ROTSH Reviewed; 397 AA.
AC A2T3T0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Intermediate capsid protein VP6 {ECO:0000255|HAMAP-Rule:MF_04129};
OS Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A)
OS (Simian Agent 11 (isolate SI/South Africa/H96/58)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=450149;
OH NCBI_TaxID=60710; Chlorocebus pygerythrus (Vervet monkey) (Cercopithecus pygerythrus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=17059839; DOI=10.1016/j.virol.2006.09.024;
RA Small C., Barro M., Brown T.L., Patton J.T.;
RT "Genome heterogeneity of SA11 rotavirus due to reassortment with 'O'
RT agent.";
RL Virology 359:415-424(2007).
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY OF CAPSID SHELL, INTERACTION WITH THE
RP INNER CAPSID PROTEIN VP2, AND SUBUNIT.
RC STRAIN=SA11-4F;
RX PubMed=19036817; DOI=10.1128/jvi.01855-08;
RA Li Z., Baker M.L., Jiang W., Estes M.K., Prasad B.V.V.;
RT "Rotavirus architecture at subnanometer resolution.";
RL J. Virol. 83:1754-1766(2009).
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 (PubMed:19036817). Interacts with the inner capsid
CC protein VP2 (PubMed:19036817). Interacts with the outer capsid
CC glycoprotein VP7. Interacts with the outer capsid protein VP5* (By
CC similarity). {ECO:0000255|HAMAP-Rule:MF_04129,
CC ECO:0000269|PubMed:19036817}.
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; DQ838650; ABG75829.1; -; Genomic_RNA.
DR RefSeq; YP_002302229.1; NC_011509.2.
DR SMR; A2T3T0; -.
DR GeneID; 7011372; -.
DR KEGG; vg:7011372; -.
DR Proteomes; UP000001119; 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 1: Evidence at protein level;
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_0000368168"
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:19036817"
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; 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
