Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Non-structural protein V

Gene

P/V

Organism
Rinderpest virus (strain Kabete O) (RDV)
Status
Reviewed-Annotation score: -Experimental evidence at transcript 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 (By similarity).By similarity1 Publication

Miscellaneous

Highly virulent strain of Rinderpest virus can blocks the phosphorylation of host JAK1 kinase, thereby blocking the type II interferon signaling as well.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi232Zinc 1By similarity1
Metal bindingi251Zinc 1By similarity1
Metal bindingi255Zinc 2By similarity1
Metal bindingi267Zinc 2By similarity1
Metal bindingi269Zinc 2By similarity1
Metal bindingi272Zinc 2By similarity1
Metal bindingi276Zinc 1By similarity1
Metal bindingi279Zinc 1By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processHost-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host interferon signaling pathway by virus, Inhibition of host MDA5 by virus, Inhibition of host RLR pathway by virus, Inhibition of host STAT1 by virus, Inhibition of host STAT2 by virus, Interferon antiviral system evasion, Viral immunoevasion
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Non-structural protein V
Gene namesi
Name:P/V
OrganismiRinderpest virus (strain Kabete O) (RDV)
Taxonomic identifieri11242 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeMorbillivirus
Virus hostiBos indicus (Zebu) [TaxID: 9915]
Bos taurus (Bovine) [TaxID: 9913]
Bubalus bubalis (Domestic water buffalo) [TaxID: 89462]
Capra hircus (Goat) [TaxID: 9925]
Gazella (gazelles) [TaxID: 9933]
Giraffa camelopardalis (Giraffe) [TaxID: 9894]
Hippopotamus [TaxID: 9832]
Ovis aries (Sheep) [TaxID: 9940]
Suidae (pigs) [TaxID: 9821]

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Host cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001428231 – 299Non-structural protein VAdd BLAST299

Interactioni

Subunit structurei

Interacts with host IFIH1/MDA5 and DHX58/LGP2. Interacts with host TYK2; this interaction inhibits the type I interferon signaling pathway (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliP60169
SMRiP60169
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the paramyxoviruses V protein family.Curated

Family and domain databases

InterProiView protein in InterPro
IPR024279 Paramyx_V_Zn-bd
IPR028243 Paramyxo_P/V_N
PfamiView protein in Pfam
PF13825 Paramyxo_PNT, 1 hit
PF13008 zf-Paramyx-P, 1 hit

Sequencei

Sequence statusi: Complete.

P60169-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEEQAYHVN KGLECIKALR ARPLDPLVVE EALAAWVETS EGQTLDRMSS
60 70 80 90 100
DEAEADHQDI SKPCFPAAGP GKSSMSRCHD QGLGGSNSCD EELGAFIGDS
110 120 130 140 150
SMHSTEVQHY HVYDHSGEKV EGVEDADSIL VQSGADDGVE VWGGDEESEN
160 170 180 190 200
SDVDSGEPDP EGSAPADWGS SPISPATRAS DVETVEGDEI QKLLEDQSRI
210 220 230 240 250
RKMTKAGKTL VVPPIPSQER PTASEKPIKK GHRREIDLIW NDGRVFIDRW
260 270 280 290
CNPTCSKVTV GTVRAKCICG ECPRVCEQCI TDSGIENRIW YHNLADIPE
Length:299
Mass (Da):32,575
Last modified:December 15, 2003 - v1
Checksum:i03EE07539D065100
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 P35945).

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S44819 mRNA No translation available.

Keywords - Coding sequence diversityi

RNA editing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S44819 mRNA No translation available.

3D structure databases

ProteinModelPortaliP60169
SMRiP60169
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiView protein in InterPro
IPR024279 Paramyx_V_Zn-bd
IPR028243 Paramyxo_P/V_N
PfamiView protein in Pfam
PF13825 Paramyxo_PNT, 1 hit
PF13008 zf-Paramyx-P, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiV_RINDK
AccessioniPrimary (citable) accession number: P60169
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: February 15, 2017
This is version 46 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again