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P11207 (V_SV5) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Non-structural protein V
Gene names
Name:P/V
OrganismSimian virus 5 (strain W3) (SV5) [Complete proteome]
Taxonomic identifier11208 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeParamyxovirinaeRubulavirus
Virus hostCanis familiaris (Dog) (Canis lupus familiaris) [TaxID: 9615]
Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Efficiently blocks type I IFN signaling following infection by behaving as a substrate receptor for CUL4-DDB1 E3 ligase complex and targeting host STAT1 for proteasomal degradation. Ref.6 Ref.8 Ref.9 Ref.10

Subunit structure

Interacts with host DDB1, STAT2 and IFIH1/MDA5. Ref.2 Ref.4 Ref.7 Ref.8

Subcellular location

Host cytoplasm By similarity.

Sequence similarities

Belongs to the paramyxoviruses V protein family.

RNA editing

Edited at position 164.
Partially edited. RNA editing at this position consists of an insertion of two guanine nucleotides. The sequence displayed here is the V protein, derived from the unedited RNA. The edited RNA gives rise to the P protein (AC P11208). Ref.1

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DDB1Q165313EBI-6148694,EBI-350322From a different organism.
DHX58Q96C102EBI-6148694,EBI-744193From a different organism.
IFIH1Q9BYX42EBI-6148694,EBI-6115771From a different organism.
STAT2P526302EBI-6148694,EBI-1546963From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 222222Non-structural protein V
PRO_0000142830

Sites

Metal binding1711Zinc 1
Metal binding1901Zinc 1
Metal binding1941Zinc 2
Metal binding2061Zinc 2
Metal binding2081Zinc 2
Metal binding2111Zinc 2
Metal binding2151Zinc 1
Metal binding2181Zinc 1

Secondary structure

........................... 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11207 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 13D2F1627D15AFA3

FASTA22223,935
        10         20         30         40         50         60 
MDPTDLSFSP DEINKLIETG LNTVEYFTSQ QVTGTSSLGK NTIPPGVTGL LTNAAEAKIQ 

        70         80         90        100        110        120 
ESTNHQKGSV GGGAKPKKPR PKIAIVPADD KTVPGKPIPN PLLGLDSTPS TQTVLDLSGK 

       130        140        150        160        170        180 
TLPSGSYKGV KLAKFGKENL MTRFIEEPRE NPIATSSPID FKRGRDTGGF HRREYSIGWV 

       190        200        210        220 
GDEVKVTEWC NPSCSPITAA ARRFECTCHQ CPVTCSECER DT 

« Hide

References

[1]"Two mRNAs that differ by two nontemplated nucleotides encode the amino coterminal proteins P and V of the paramyxovirus SV5."
Thomas S.M., Lamb R.A., Paterson R.G.
Cell 54:891-902(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], RNA EDITING.
[2]"NP:P and NP:V interactions of the paramyxovirus simian virus 5 examined using a novel protein:protein capture assay."
Randall R.E., Bermingham A.
Virology 224:121-129(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PROTEIN NP.
[3]"The RNA binding region of the paramyxovirus SV5 V and P proteins."
Lin G.Y., Paterson R.G., Lamb R.A.
Virology 238:460-469(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING.
[4]"The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-beta promoter."
Andrejeva J., Childs K.S., Young D.F., Carlos T.S., Stock N., Goodbourn S., Randall R.E.
Proc. Natl. Acad. Sci. U.S.A. 101:17264-17269(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN IFIH1/MDA5, INTERFERON EVASION.
[5]"In vitro and in vivo specificity of ubiquitination and degradation of STAT1 and STAT2 by the V proteins of the paramyxoviruses simian virus 5 and human parainfluenza virus type 2."
Precious B., Young D.F., Andrejeva L., Goodbourn S., Randall R.E.
J. Gen. Virol. 86:151-158(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION OF HUMAN STAT1 AND HUMAN STAT2.
[6]"The role of simian virus 5 V protein on viral RNA synthesis."
Lin Y., Horvath F., Aligo J.A., Wilson R., He B.
Virology 338:270-280(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Simian virus 5 V protein acts as an adaptor, linking DDB1 to STAT2, to facilitate the ubiquitination of STAT1."
Precious B., Childs K., Fitzpatrick-Swallow V., Goodbourn S., Randall R.E.
J. Virol. 79:13434-13441(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN DDB1 AND HUMAN STAT2.
[8]"Paramyxovirus V proteins interact with the RNA Helicase LGP2 to inhibit RIG-I-dependent interferon induction."
Childs K., Randall R., Goodbourn S.
J. Virol. 86:3411-3421(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HOST DHX58.
[9]"Structure of DDB1 in complex with a paramyxovirus V protein: viral hijack of a propeller cluster in ubiquitin ligase."
Li T., Chen X., Garbutt K.C., Zhou P., Zheng N.
Cell 124:105-117(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-222, FUNCTION.
[10]"Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery."
Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., Zheng N.
Nature 443:590-593(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH HUMAN CUL4A; DDB1 AND ROC1, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03142 mRNA. Translation: AAA47882.1.
AF052755 Genomic RNA. Translation: AAC95512.1.
PIRMNNZSP. A31594.
RefSeqYP_138513.1. NC_006430.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2B5LX-ray2.85C/D1-222[»]
2HYEX-ray3.10B1-222[»]
2K48NMR-A95-108[»]
4I1SX-ray2.29B168-219[»]
ProteinModelPortalP11207.
SMRP11207. Positions 10-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48759N.
IntActP11207. 6 interactions.
MINTMINT-6623137.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3160800.

Family and domain databases

InterProIPR024279. Paramyx_V_Zn-bd.
IPR025909. Soyouz_module.
[Graphical view]
PfamPF14313. Soyouz_module. 1 hit.
PF13008. zf-Paramyx-P. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP11207.

Entry information

Entry nameV_SV5
AccessionPrimary (citable) accession number: P11207
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: June 11, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references