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Q91N61

- VP6_ROTP5

UniProt

Q91N61 - VP6_ROTP5

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Protein

Intermediate capsid protein VP6

Gene
N/A
Organism
Rotavirus A (strain Pig/United States/OSU/1977 G5-P9[7]-I5-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A) (Rotavirus A (strain Ohio State University))
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli

Functioni

Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices. This capsid constitutes the middle concentric layer of the viral mature particle. The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nacent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes. VP6 is required for the transcription activity of the DLP (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi153 – 1531Zinc; shared with all trimeric partnersBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. structural molecule activity Source: InterPro

GO - Biological processi

  1. fusion of virus membrane with host plasma membrane Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Intermediate capsid protein VP6
OrganismiRotavirus A (strain Pig/United States/OSU/1977 G5-P9[7]-I5-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A) (Rotavirus A (strain Ohio State University))
Taxonomic identifieri10915 [NCBI]
Taxonomic lineageiVirusesdsRNA virusesReoviridaeSedoreovirinaeRotavirus
Virus hostiSus scrofa (Pig) [TaxID: 9823]

Subcellular locationi

Virion
Note: Component of the intermediate capsid. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging (By similarity).By similarity

GO - Cellular componenti

  1. viral envelope Source: InterPro
  2. viral intermediate capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Intermediate capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397Intermediate capsid protein VP6PRO_0000368183Add
BLAST

Post-translational modificationi

The N-terminus is blocked.By similarity

Interactioni

Subunit structurei

Homotrimer. Interacts with VP2 (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ91N61.
SMRiQ91N61. Positions 1-397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the rotavirus VP6 family.Curated

Family and domain databases

InterProiIPR008980. Capsid_hemagglutn.
IPR001385. Rotavirus_A/C_VP6.
IPR008935. Virus_capsid_a-hlx_vir.
[Graphical view]
PfamiPF00980. Rota_Capsid_VP6. 1 hit.
[Graphical view]
ProDomiPD001812. Rota_Capsid_VP6. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF48345. SSF48345. 2 hits.
SSF49818. SSF49818. 1 hit.

Sequencei

Sequence statusi: Complete.

Q91N61-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEVLYSLSKT LKDARDKIVE GTLYSNVSDL IQQFNQMIVT MNGNEFQTGG
60 70 80 90 100
IGNLPIRNWT FDFGLLGTTL LNLDANYVEN ARTTIEYFID FIDNVCMDEI
110 120 130 140 150
ARESQRNGIA PQSEALRKLS GIKFKRINFD NSSDYIENWN LQNRRQRTGF
160 170 180 190 200
VFHKPNILPY SASFTLNRSQ PAHDNLMGTM WINAGSEIQV AGFDYSCALN
210 220 230 240 250
APANIQQFEH VVPLRRALTT ATITLLPDAE RFSFPRVINS ADGTTTWYFN
260 270 280 290 300
PVILRPSNVE VEFLLNGQII NTYQARFGTI IARNFDTIRL SFQLVRPPNM
310 320 330 340 350
TPAVANLFPQ APPFIFHATV GLTLRIESAV CESVLADASE TLLANVTSVR
360 370 380 390
QEYAIPVGPV FPPGMNWTEL ITNYSPSRED NLQRVFTVAS IRSMLIK
Length:397
Mass (Da):44,756
Last modified:December 1, 2001 - v1
Checksum:iDC94FDECE43AB856
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF317123 mRNA. Translation: AAK60604.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF317123 mRNA. Translation: AAK60604.1 .

3D structure databases

ProteinModelPortali Q91N61.
SMRi Q91N61. Positions 1-397.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR008980. Capsid_hemagglutn.
IPR001385. Rotavirus_A/C_VP6.
IPR008935. Virus_capsid_a-hlx_vir.
[Graphical view ]
Pfami PF00980. Rota_Capsid_VP6. 1 hit.
[Graphical view ]
ProDomi PD001812. Rota_Capsid_VP6. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF48345. SSF48345. 2 hits.
SSF49818. SSF49818. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Antigenic and molecular analysis of group A porcine and bovine rotaviruses isolated in the United States, Venezuela, and South Africa."
    Ciarlet M., Steele A.D., Vasquez E., Bertolotti-Ciarlet A., Sanchez-Camacho A., Pina C.I., Pujol F.H., Liprandi F.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiVP6_ROTP5
AccessioniPrimary (citable) accession number: Q91N61
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: December 1, 2001
Last modified: October 1, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

The zinc ion is not essential for either trimerization or transcription activity of the DLP. Zinc-depleted VP6 has an increased sensitivity to proteases (By similarity).By similarity

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3