Non-structural protein V - Simian virus 5 (strain W3) (SV5)

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P11207 (V_SV5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 66. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Non-structural protein V

Gene names

Name:

P/V

Organism

Simian virus 5 (strain W3) (SV5) [Complete proteome]

Taxonomic identifier

11208 [NCBI]

Taxonomic lineage

Viruses › ssRNA negative-strand viruses › Mononegavirales › Paramyxoviridae › Paramyxovirinae › Rubulavirus ›

Virus host

Canis familiaris (Dog) (Canis lupus familiaris) [TaxID: 9615]
Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	222 AA.
Sequence status	Complete.
Protein existence	Evidence 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 targeting host STAT1 for proteasomal degradation. Ref.6 Ref.8
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

Ontologies

Keywords
Biological process	Host-virus interaction Inhibition of host IFN-mediated response initiation by virus Inhibition of host MDA5 by virus Inhibition of host STAT1 by virus Inhibition of host innate immune response by virus Inhibition of host interferon signaling pathway by virus Interferon antiviral system evasion Viral immunoevasion
Cellular component	Host cytoplasm
Coding sequence diversity	RNA editing
Ligand	Metal-binding RNA-binding Zinc
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	suppression by virus of host MDA-5 activity Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host STAT1 activity Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host type I interferon production Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host type I interferon-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 222

222

Non-structural protein V

PRO_0000142830

Sites

Metal binding

171

Zinc 1

Metal binding

190

Zinc 1

Metal binding

194

Zinc 2

Metal binding

206

Zinc 2

Metal binding

208

Zinc 2

Metal binding

211

Zinc 2

Metal binding

215

Zinc 1

Metal binding

218

Zinc 1

Secondary structure

222

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P11207 [UniParc].

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

FASTA

222

23,935

        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

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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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03142 mRNA. Translation: AAA47882.1.
AF052755 Genomic RNA. Translation: AAC95512.1.

PIR

MNNZSP. A31594.

RefSeq

YP_138513.1. NC_006430.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2B5L	X-ray	2.85	C/D	1-222	[»]
2HYE	X-ray	3.10	B	1-222	[»]
2K48	NMR	-	A	95-108	[»]
4I1S	X-ray	2.29	B	168-219	[»]

ProteinModelPortal

P11207.

SMR

P11207. Positions 10-222.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48759N.

IntAct

P11207. 3 interactions.

MINT

MINT-6623137.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3160800.

Family and domain databases

InterPro

IPR024279. Paramyx_V_Zn-bd.
IPR025909. Soyouz_module.
[Graphical view]

Pfam

PF14313. Soyouz_module. 1 hit.
PF13008. zf-Paramyx-P. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P11207.

Entry information

Entry name

V_SV5

Accession

Primary (citable) accession number: P11207

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 1, 2013
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Family and domain databases

Other

Entry information

Relevant documents