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P11207

- V_SV5

UniProt

P11207 - V_SV5

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Protein

Non-structural protein V

Gene
P/V
Organism
Simian virus 5 (strain W3) (SV5)
Status
Reviewed - Annotation score: 5 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. 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.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi171 – 1711Zinc 1
Metal bindingi190 – 1901Zinc 1
Metal bindingi194 – 1941Zinc 2
Metal bindingi206 – 2061Zinc 2
Metal bindingi208 – 2081Zinc 2
Metal bindingi211 – 2111Zinc 2
Metal bindingi215 – 2151Zinc 1
Metal bindingi218 – 2181Zinc 1

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein binding Source: IntAct
  3. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. suppression by virus of host MDA-5 activity Source: CACAO
  2. suppression by virus of host STAT1 activity Source: UniProtKB-KW
  3. suppression by virus of host type I interferon-mediated signaling pathway Source: UniProtKB-KW
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 MDA5 by virus, Inhibition of host RLR pathway by virus, Inhibition of host STAT1 by virus, Interferon antiviral system evasion, Ubl conjugation pathway, Viral immunoevasion

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Non-structural protein V
Gene namesi
Name:P/V
OrganismiSimian virus 5 (strain W3) (SV5)
Taxonomic identifieri11208 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesMononegaviralesParamyxoviridaeParamyxovirinaeRubulavirus
Virus hostiCanis familiaris (Dog) (Canis lupus familiaris) [TaxID: 9615]
Homo sapiens (Human) [TaxID: 9606]
ProteomesiUP000007232: Genome

Subcellular locationi

Host cytoplasm By similarity

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 222222Non-structural protein VPRO_0000142830Add
BLAST

Interactioni

Subunit structurei

Interacts with host DDB1, STAT2 and IFIH1/MDA5.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
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.

Protein-protein interaction databases

DIPiDIP-48759N.
IntActiP11207. 6 interactions.
MINTiMINT-6623137.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 3210
Beta strandi95 – 973
Turni101 – 1044
Beta strandi109 – 1168
Beta strandi119 – 1213
Helixi127 – 13812
Beta strandi143 – 1464
Beta strandi164 – 1674
Beta strandi170 – 18011
Beta strandi183 – 19210
Beta strandi202 – 2043
Beta strandi207 – 2093
Helixi216 – 2183

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B5LX-ray2.85C/D1-222[»]
2HYEX-ray3.10B1-222[»]
2K48NMR-A95-108[»]
4I1SX-ray2.29B168-219[»]
ProteinModelPortaliP11207.
SMRiP11207. Positions 10-222.

Miscellaneous databases

EvolutionaryTraceiP11207.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR024279. Paramyx_V_Zn-bd.
IPR025909. Soyouz_module.
[Graphical view]
PfamiPF14313. Soyouz_module. 1 hit.
PF13008. zf-Paramyx-P. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11207-1 [UniParc]FASTAAdd to Basket

« Hide

MDPTDLSFSP DEINKLIETG LNTVEYFTSQ QVTGTSSLGK NTIPPGVTGL    50
LTNAAEAKIQ ESTNHQKGSV GGGAKPKKPR PKIAIVPADD KTVPGKPIPN 100
PLLGLDSTPS TQTVLDLSGK TLPSGSYKGV KLAKFGKENL MTRFIEEPRE 150
NPIATSSPID FKRGRDTGGF HRREYSIGWV GDEVKVTEWC NPSCSPITAA 200
ARRFECTCHQ CPVTCSECER DT 222
Length:222
Mass (Da):23,935
Last modified:July 1, 1989 - v1
Checksum:i13D2F1627D15AFA3
GO

RNA editingi

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).1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03142 mRNA. Translation: AAA47882.1.
AF052755 Genomic RNA. Translation: AAC95512.1.
PIRiA31594. MNNZSP.
RefSeqiYP_138513.1. NC_006430.1.

Genome annotation databases

GeneIDi3160800.

Keywords - Coding sequence diversityi

RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03142 mRNA. Translation: AAA47882.1 .
AF052755 Genomic RNA. Translation: AAC95512.1 .
PIRi A31594. MNNZSP.
RefSeqi YP_138513.1. NC_006430.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P11207.
SMRi P11207. Positions 10-222.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48759N.
IntActi P11207. 6 interactions.
MINTi MINT-6623137.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3160800.

Miscellaneous databases

EvolutionaryTracei P11207.

Family and domain databases

InterProi IPR024279. Paramyx_V_Zn-bd.
IPR025909. Soyouz_module.
[Graphical view ]
Pfami PF14313. Soyouz_module. 1 hit.
PF13008. zf-Paramyx-P. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiV_SV5
AccessioniPrimary (citable) accession number: P11207
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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