V_PIV5
ID V_PIV5 Reviewed; 222 AA.
AC P11207;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Non-structural protein V;
GN Name=P/V;
OS Parainfluenza virus 5 (strain W3) (PIV5) (Simian virus 5).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Orthorubulavirus; Mammalian orthorubulavirus 5.
OX NCBI_TaxID=11208;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RX PubMed=3044614; DOI=10.1016/s0092-8674(88)91285-8;
RA Thomas S.M., Lamb R.A., Paterson R.G.;
RT "Two mRNAs that differ by two nontemplated nucleotides encode the amino
RT coterminal proteins P and V of the paramyxovirus SV5.";
RL Cell 54:891-902(1988).
RN [2]
RP INTERACTION WITH PROTEIN NP.
RX PubMed=8862406; DOI=10.1006/viro.1996.0513;
RA Randall R.E., Bermingham A.;
RT "NP:P and NP:V interactions of the paramyxovirus simian virus 5 examined
RT using a novel protein:protein capture assay.";
RL Virology 224:121-129(1996).
RN [3]
RP RNA-BINDING.
RX PubMed=9400618; DOI=10.1006/viro.1997.8866;
RA Lin G.Y., Paterson R.G., Lamb R.A.;
RT "The RNA binding region of the paramyxovirus SV5 V and P proteins.";
RL Virology 238:460-469(1997).
RN [4]
RP INTERACTION WITH HUMAN IFIH1/MDA5, AND INTERFERON EVASION.
RX PubMed=15563593; DOI=10.1073/pnas.0407639101;
RA Andrejeva J., Childs K.S., Young D.F., Carlos T.S., Stock N., Goodbourn S.,
RA Randall R.E.;
RT "The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase,
RT mda-5, and inhibit its activation of the IFN-beta promoter.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17264-17269(2004).
RN [5]
RP UBIQUITINATION OF HUMAN STAT1 AND HUMAN STAT2.
RX PubMed=15604442; DOI=10.1099/vir.0.80263-0;
RA Precious B., Young D.F., Andrejeva L., Goodbourn S., Randall R.E.;
RT "In vitro and in vivo specificity of ubiquitination and degradation of
RT STAT1 and STAT2 by the V proteins of the paramyxoviruses simian virus 5 and
RT human parainfluenza virus type 2.";
RL J. Gen. Virol. 86:151-158(2005).
RN [6]
RP FUNCTION.
RX PubMed=15950997; DOI=10.1016/j.virol.2005.05.014;
RA Lin Y., Horvath F., Aligo J.A., Wilson R., He B.;
RT "The role of simian virus 5 V protein on viral RNA synthesis.";
RL Virology 338:270-280(2005).
RN [7]
RP INTERACTION WITH HUMAN DDB1 AND HUMAN STAT2.
RX PubMed=16227264; DOI=10.1128/jvi.79.21.13434-13441.2005;
RA Precious B., Childs K., Fitzpatrick-Swallow V., Goodbourn S., Randall R.E.;
RT "Simian virus 5 V protein acts as an adaptor, linking DDB1 to STAT2, to
RT facilitate the ubiquitination of STAT1.";
RL J. Virol. 79:13434-13441(2005).
RN [8]
RP FUNCTION, AND INTERACTION WITH HOST DHX58.
RX PubMed=22301134; DOI=10.1128/jvi.06405-11;
RA Childs K., Randall R., Goodbourn S.;
RT "Paramyxovirus V proteins interact with the RNA Helicase LGP2 to inhibit
RT RIG-I-dependent interferon induction.";
RL J. Virol. 86:3411-3421(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-222, AND FUNCTION.
RX PubMed=16413485; DOI=10.1016/j.cell.2005.10.033;
RA Li T., Chen X., Garbutt K.C., Zhou P., Zheng N.;
RT "Structure of DDB1 in complex with a paramyxovirus V protein: viral hijack
RT of a propeller cluster in ubiquitin ligase.";
RL Cell 124:105-117(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH HUMAN CUL4A; DDB1 AND
RP ROC1, AND FUNCTION.
RX PubMed=16964240; DOI=10.1038/nature05175;
RA Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., Zheng N.;
RT "Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase
RT machinery.";
RL Nature 443:590-593(2006).
CC -!- FUNCTION: Plays an essential role in the inhibition of host immune
CC response. Prevents the establishment of cellular antiviral state by
CC blocking interferon-alpha/beta (IFN-alpha/beta) production and
CC signaling pathway. Interacts with host IFIH1/MDA5 and DHX58/LGP2 to
CC inhibit the transduction pathway involved in the activation of IFN-beta
CC promoter, thus protecting the virus against cell antiviral state.
CC Efficiently blocks type I IFN signaling following infection by behaving
CC as a substrate receptor for CUL4-DDB1 E3 ligase complex and targeting
CC host STAT1 for proteasomal degradation. {ECO:0000269|PubMed:15950997,
CC ECO:0000269|PubMed:16413485, ECO:0000269|PubMed:16964240,
CC ECO:0000269|PubMed:22301134}.
CC -!- SUBUNIT: Interacts with host DDB1, STAT2 and IFIH1/MDA5.
CC {ECO:0000269|PubMed:15563593, ECO:0000269|PubMed:16227264,
CC ECO:0000269|PubMed:16964240, ECO:0000269|PubMed:22301134,
CC ECO:0000269|PubMed:8862406}.
CC -!- INTERACTION:
CC P11207; Q16531: DDB1; Xeno; NbExp=4; IntAct=EBI-6148694, EBI-350322;
CC P11207; Q96C10: DHX58; Xeno; NbExp=2; IntAct=EBI-6148694, EBI-744193;
CC P11207; Q8R5F7-1: Ifih1; Xeno; NbExp=3; IntAct=EBI-6148694, EBI-16019291;
CC P11207; Q9BYX4: IFIH1; Xeno; NbExp=3; IntAct=EBI-6148694, EBI-6115771;
CC P11207; A7LCX1: MDA5; Xeno; NbExp=2; IntAct=EBI-6148694, EBI-16032125;
CC P11207; P52630: STAT2; Xeno; NbExp=2; IntAct=EBI-6148694, EBI-1546963;
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=164 {ECO:0000269|PubMed:3044614};
CC Note=Partially edited. RNA editing at this position consists of an
CC insertion of two guanine nucleotides. The sequence displayed here is
CC the V protein, derived from the unedited RNA. The edited RNA gives rise
CC to the P protein (AC P11208).;
CC -!- SIMILARITY: Belongs to the paramyxoviruses V protein family.
CC {ECO:0000305}.
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DR EMBL; J03142; AAA47882.1; -; mRNA.
DR EMBL; AF052755; AAC95512.1; -; Genomic_RNA.
DR PIR; A31594; MNNZSP.
DR PDB; 2B5L; X-ray; 2.85 A; C/D=1-222.
DR PDB; 2HYE; X-ray; 3.10 A; B=1-222.
DR PDB; 2K48; NMR; -; A=95-108.
DR PDB; 4I1S; X-ray; 2.29 A; B=168-219.
DR PDBsum; 2B5L; -.
DR PDBsum; 2HYE; -.
DR PDBsum; 2K48; -.
DR PDBsum; 4I1S; -.
DR SMR; P11207; -.
DR DIP; DIP-48759N; -.
DR IntAct; P11207; 12.
DR MINT; P11207; -.
DR EvolutionaryTrace; P11207; -.
DR Proteomes; UP000007232; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0039554; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host MDA-5 activity; IDA:CACAO.
DR InterPro; IPR024279; Paramyx_V_Zn-bd.
DR InterPro; IPR025909; Soyouz_module.
DR Pfam; PF14313; Soyouz_module; 1.
DR Pfam; PF13008; zf-Paramyx-P; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host MDA5 by virus; Inhibition of host RLR pathway by virus;
KW Inhibition of host STAT1 by virus; Interferon antiviral system evasion;
KW Metal-binding; RNA editing; RNA-binding; Ubl conjugation pathway;
KW Viral immunoevasion; Zinc.
FT CHAIN 1..222
FT /note="Non-structural protein V"
FT /id="PRO_0000142830"
FT REGION 61..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:2B5L"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2B5L"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:2B5L"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:2B5L"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2B5L"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:2B5L"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:2B5L"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:2B5L"
FT STRAND 170..180
FT /evidence="ECO:0007829|PDB:4I1S"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:4I1S"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:2B5L"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4I1S"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:4I1S"
SQ SEQUENCE 222 AA; 23935 MW; 13D2F1627D15AFA3 CRC64;
MDPTDLSFSP DEINKLIETG LNTVEYFTSQ QVTGTSSLGK NTIPPGVTGL LTNAAEAKIQ
ESTNHQKGSV GGGAKPKKPR PKIAIVPADD KTVPGKPIPN PLLGLDSTPS TQTVLDLSGK
TLPSGSYKGV KLAKFGKENL MTRFIEEPRE NPIATSSPID FKRGRDTGGF HRREYSIGWV
GDEVKVTEWC NPSCSPITAA ARRFECTCHQ CPVTCSECER DT
