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Protein

Non-structural protein V

Gene

P/V

Organism
Measles virus (strain Ichinose-B95a) (MeV) (Subacute sclerose panencephalitis virus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Plays an essential role in the inhibition of host immune response. Prevents the establishment of cellular antiviral state by blocking interferon-alpha/beta (IFN-alpha/beta) production and signaling pathway. Interacts with host IFIH1/MDA5 and DHX58/LGP2 to inhibit the transduction pathway involved in the activation of IFN-beta promoter, thus protecting the virus against cell antiviral state. Blocks the type I interferon signaling pathway by interacting with host TYK2 and thereby inhibiting downstream STAT1 and STAT2 phosphorylation. Moderately affects the type II interferon signaling.6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi232 – 2321Zinc 1By similarity
Metal bindingi251 – 2511Zinc 1By similarity
Metal bindingi255 – 2551Zinc 2By similarity
Metal bindingi267 – 2671Zinc 2By similarity
Metal bindingi269 – 2691Zinc 2By similarity
Metal bindingi272 – 2721Zinc 2By similarity
Metal bindingi276 – 2761Zinc 1By similarity
Metal bindingi279 – 2791Zinc 1By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host IRF7 by virus, Inhibition of host MDA5 by virus, Inhibition of host RLR pathway by virus, Inhibition of host STAT2 by virus, Interferon antiviral system evasion, Viral immunoevasion

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Non-structural protein V
Gene namesi
Name:P/V
OrganismiMeasles virus (strain Ichinose-B95a) (MeV) (Subacute sclerose panencephalitis virus)
Taxonomic identifieri645098 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeParamyxovirinaeMorbillivirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008699 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 299299Non-structural protein VPRO_0000394721Add
BLAST

Interactioni

Subunit structurei

Interacts with host IFIH1/MDA5 and DHX58/LGP2. Interacts with host TYK2; this interaction inhibits the type I interferon signaling pathway whithout affecting the type II pathway. Interacts with host IRF7; this interaction inhibits IRF7 translocation to the nucleus. Interacts with host CHUK and RELA. Interacts (via C-terminus) with host STAT2.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RELAQ042063EBI-3650423,EBI-73886From a different organism.
STAT2P526304EBI-3650423,EBI-1546963From a different organism.

Protein-protein interaction databases

DIPiDIP-61740N.
IntActiP0C774. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliP0C774.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi213 – 2186Poly-Pro

Sequence similaritiesi

Belongs to the paramyxoviruses V protein family.Curated

Family and domain databases

InterProiIPR024279. Paramyx_V_Zn-bd.
IPR028243. Paramyxo_P/V_N.
[Graphical view]
PfamiPF13825. Paramyxo_PNT. 1 hit.
PF13008. zf-Paramyx-P. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C774-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEEQARHVK NGLECIRALK AEPIGSLAVE EAMAAWSEIS DNPGQDRATC
60 70 80 90 100
KEEEAGSSGL SKPCLSAIGS TEGGAPRIRG QGSGESDDDA ETLGIPSRNL
110 120 130 140 150
QASSTGLQCY HVYDHSGEAV KGIQDADSIM VQSGLDGDST LSGGDDESEN
160 170 180 190 200
SDVDIGEPDT EGYAITDRGS APISMGFRAS DVETAEGGEI HELLKLQSRG
210 220 230 240 250
NNFPKLGKTL NVPPPPNPSR ASTSETPIKK GHRREIGLIW NGDRVFIDRW
260 270 280 290
CNPMCSKVTL GTIRARCTCG ECPRVCEQCR TDTGVDTRIW YHNLPEIPE
Length:299
Mass (Da):32,016
Last modified:June 15, 2010 - v1
Checksum:iFEDBD36B65E382D0
GO

RNA editingi

Edited at position 231.
Partially edited. RNA editing at this position consists of an insertion of one guanine nucleotide. The sequence displayed here is the V protein, derived from the edited RNA. The unedited RNA gives rise to the P protein (AC Q9WMB4).

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016162 Genomic RNA. No translation available.

Keywords - Coding sequence diversityi

RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016162 Genomic RNA. No translation available.

3D structure databases

ProteinModelPortaliP0C774.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61740N.
IntActiP0C774. 3 interactions.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR024279. Paramyx_V_Zn-bd.
IPR028243. Paramyxo_P/V_N.
[Graphical view]
PfamiPF13825. Paramyxo_PNT. 1 hit.
PF13008. zf-Paramyx-P. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Comparative nucleotide sequence analyses of the entire genomes of B95a cell-isolated and vero cell-isolated measles viruses from the same patient."
    Takeuchi K., Miyajima N., Kobune F., Tashiro M.
    Virus Genes 20:253-257(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Measles virus V protein blocks interferon (IFN)-alpha/beta but not IFN-gamma signaling by inhibiting STAT1 and STAT2 phosphorylation."
    Takeuchi K., Kadota S.I., Takeda M., Miyajima N., Nagata K.
    FEBS Lett. 545:177-182(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "STAT2 is a primary target for measles virus V protein-mediated alpha/beta interferon signaling inhibition."
    Ramachandran A., Parisien J.P., Horvath C.M.
    J. Virol. 82:8330-8338(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST STAT2.
  4. "Measles virus V protein is a decoy substrate for IkappaB kinase alpha and prevents Toll-like receptor 7/9-mediated interferon induction."
    Pfaller C.K., Conzelmann K.K.
    J. Virol. 82:12365-12373(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST IRF7 AND CHUK.
    Strain: Schwarz vaccine.
  5. "A shared interface mediates paramyxovirus interference with antiviral RNA helicases MDA5 and LGP2."
    Parisien J.P., Bamming D., Komuro A., Ramachandran A., Rodriguez J.J., Barber G., Wojahn R.D., Horvath C.M.
    J. Virol. 83:7252-7260(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST IFIH1 AND DHX58.
  6. "The measles virus V protein binds to p65 (RelA) to suppress NF-kappaB activity."
    Schuhmann K.M., Pfaller C.K., Conzelmann K.K.
    J. Virol. 85:3162-3171(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST RELA.
    Strain: Schwarz vaccine.
  7. "Morbillivirus v proteins exhibit multiple mechanisms to block type 1 and type 2 interferon signalling pathways."
    Chinnakannan S.K., Nanda S.K., Baron M.D.
    PLoS ONE 8:E57063-E57063(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST JAK1 AND TYK2.
    Strain: Dublin.

Entry informationi

Entry nameiV_MEASC
AccessioniPrimary (citable) accession number: P0C774
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: March 16, 2016
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.