V_NIPAV
ID V_NIPAV Reviewed; 456 AA.
AC Q997F2; Q8QU01;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Non-structural protein V;
GN Name=P/V/C;
OS Nipah virus.
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Henipavirus.
OX NCBI_TaxID=121791;
OH NCBI_TaxID=58060; Cynopterus brachyotis (Lesser short-nosed fruit bat) (Pachysoma brachyotis).
OH NCBI_TaxID=58065; Eonycteris spelaea (Lesser dawn bat) (Macroglossus spelaeus).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9405; Pteropus hypomelanus (Island flying fox) (Variable flying fox).
OH NCBI_TaxID=132908; Pteropus vampyrus (Large flying fox).
OH NCBI_TaxID=153297; Scotophilus kuhlii (Lesser asiatic yellow bat).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10827955; DOI=10.1126/science.288.5470.1432;
RA Chua K.B., Bellini W.J., Rota P.A., Harcourt B.H., Tamin A., Lam S.K.,
RA Ksiazek T.G., Rollin P.E., Zaki S.R., Shieh W., Goldsmith C.S.,
RA Gubler D.J., Roehrig J.T., Eaton B., Gould A.R., Olson J., Field H.,
RA Daniels P., Ling A.E., Peters C.J., Anderson L.J., Mahy B.W.;
RT "Nipah virus: a recently emergent deadly paramyxovirus.";
RL Science 288:1432-1435(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11504554; DOI=10.1006/viro.2001.1026;
RA Harcourt B.H., Tamin A., Halpin K., Ksiazek T.G., Rollin P.E.,
RA Bellini W.J., Rota P.A.;
RT "Molecular characterization of the polymerase gene and genomic termini of
RT Nipah virus.";
RL Virology 287:192-201(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate UMMC1, and Isolate UMMC2;
RX PubMed=11514724; DOI=10.1099/0022-1317-82-9-2151;
RA Chan Y.P., Chua K.B., Koh C.L., Lim M.E., Lam S.K.;
RT "Complete nucleotide sequences of Nipah virus isolates from Malaysia.";
RL J. Gen. Virol. 82:2151-2155(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Malaysian flying-fox;
RX PubMed=11880045; DOI=10.1016/s1286-4579(01)01522-2;
RA Chua K.B., Koh C.L., Hooi P.S., Wee K.F., Khong J.H., Chua B.H., Chan Y.P.,
RA Lim M.E., Lam S.K.;
RT "Isolation of Nipah virus from Malaysian island flying-foxes.";
RL Microbes Infect. 4:145-151(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate NV/MY/99/UM-0128, Isolate NV/MY/99/VRI-1413, and
RC Isolate NV/MY/99/VRI-2794;
RX PubMed=15663869; DOI=10.3201/eid1012.040452;
RA Abubakar S., Chang L.Y., Mohdali A.R., Sharifah S.H., Yusoff K., Zamrod Z.;
RT "Isolation and molecular identification of Nipah virus from pigs.";
RL Emerg. Infect. Dis. 10:2228-2230(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate NV/MY/99/VRI-0626;
RA Abubakar S., Li-Yen C., Mohdali A.R., Sharifah S.H.;
RT "Identification of a new Nipah virus strain from pigs.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND INTERACTION WITH HOST STAT1 AND STAT2.
RX PubMed=12388709; DOI=10.1128/jvi.76.22.11476-11483.2002;
RA Rodriguez J.J., Parisien J.P., Horvath C.M.;
RT "Nipah virus V protein evades alpha and gamma interferons by preventing
RT STAT1 and STAT2 activation and nuclear accumulation.";
RL J. Virol. 76:11476-11483(2002).
RN [8]
RP INTERACTION WITH HOST STAT1.
RX PubMed=15140960; DOI=10.1128/jvi.78.11.5633-5641.2004;
RA Shaw M.L., Garcia-Sastre A., Palese P., Basler C.F.;
RT "Nipah virus V and W proteins have a common STAT1-binding domain yet
RT inhibit STAT1 activation from the cytoplasmic and nuclear compartments,
RT respectively.";
RL J. Virol. 78:5633-5641(2004).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=19141449; DOI=10.1099/vir.0.007294-0;
RA Lo M.K., Harcourt B.H., Mungall B.A., Tamin A., Peeples M.E., Bellini W.J.,
RA Rota P.A.;
RT "Determination of the henipavirus phosphoprotein gene mRNA editing
RT frequencies and detection of the C, V and W proteins of Nipah virus in
RT virus-infected cells.";
RL J. Gen. Virol. 90:398-404(2009).
RN [10]
RP FUNCTION, AND INTERACTION WITH HOST IFIH1 AND DHX58.
RX PubMed=19403670; DOI=10.1128/jvi.00153-09;
RA Parisien J.P., Bamming D., Komuro A., Ramachandran A., Rodriguez J.J.,
RA Barber G., Wojahn R.D., Horvath C.M.;
RT "A shared interface mediates paramyxovirus interference with antiviral RNA
RT helicases MDA5 and LGP2.";
RL J. Virol. 83:7252-7260(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HOST UBXN1.
RX PubMed=29769705; DOI=10.1038/s41598-018-25815-9;
RA Uchida S., Horie R., Sato H., Kai C., Yoneda M.;
RT "Possible role of the Nipah virus V protein in the regulation of the
RT interferon beta induction by interacting with UBX domain-containing
RT protein1.";
RL Sci. Rep. 8:7682-7682(2018).
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 Blocks the type I interferon signaling pathway by interacting with host
CC STAT1 and STAT2 and thereby inhibiting their phosphorylation and
CC subsequent nuclear translocation. Efficiently blocks the type II
CC interferon signaling pathway. Suppresses interferon induction by
CC interacting with and stabilizing host UBXN1, a negative regulator of
CC both RIG-I-like receptors (RLR) and NF-kappa-B pathways.
CC {ECO:0000269|PubMed:12388709, ECO:0000269|PubMed:19403670,
CC ECO:0000269|PubMed:29769705}.
CC -!- SUBUNIT: Interacts with host IFIH1/MDA5, DHX58/LGP2, STAT1 and STAT2.
CC Interacts (via N-terminus) with host UBXN1 (via C-terminal UBX domain);
CC this interaction inhibits interferon-alpha/beta (IFN-alpha/beta)
CC production (PubMed:29769705). {ECO:0000269|PubMed:12388709,
CC ECO:0000269|PubMed:15140960, ECO:0000269|PubMed:19403670,
CC ECO:0000269|PubMed:29769705}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:19141449,
CC ECO:0000269|PubMed:29769705}.
CC -!- RNA EDITING: Modified_positions=406; Note=Partially edited. RNA editing
CC at this position consists of an insertion of one or two guanine
CC nucleotides. The sequence displayed here is the V protein, derived from
CC the +1G edited RNA. The unedited RNA gives rise to the P protein (AC
CC Q9IK91), the +2G edited RNA gives rise to the W protein (AC P0C1C7).;
CC -!- MISCELLANEOUS: The P/V/C gene has two overlapping open reading frames.
CC One encodes the P/V/W proteins and the other the C protein.
CC -!- SIMILARITY: Belongs to the paramyxoviruses V protein family.
CC {ECO:0000305}.
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DR EMBL; AF212302; AAK29090.1; -; Genomic_RNA.
DR EMBL; AY029768; AAK50551.1; -; Genomic_RNA.
DR EMBL; AY029767; AAK50547.1; -; Genomic_RNA.
DR EMBL; AF376747; AAM13407.1; -; Genomic_RNA.
DR EMBL; AJ564621; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AJ564622; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AJ564623; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AJ627196; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR RefSeq; NP_112023.1; NC_002728.1.
DR SMR; Q997F2; -.
DR IntAct; Q997F2; 42.
DR MINT; Q997F2; -.
DR GeneID; 920952; -.
DR Proteomes; UP000002330; Genome.
DR Proteomes; UP000007527; Genome.
DR Proteomes; UP000008676; Genome.
DR Proteomes; UP000100567; Genome.
DR Proteomes; UP000110983; Genome.
DR Proteomes; UP000130871; Genome.
DR Proteomes; UP000170143; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion 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:0039564; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW.
DR GO; GO:0039501; P:suppression by virus of host type I interferon production; IDA:UniProtKB.
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; IEA:UniProtKB-KW.
DR InterPro; IPR024279; Paramyx_V_Zn-bd.
DR InterPro; IPR035430; Paramyxo_PNT.
DR InterPro; IPR025909; Soyouz_module.
DR Pfam; PF14320; Paramyxo_PNT; 1.
DR Pfam; PF14313; Soyouz_module; 1.
DR Pfam; PF13008; zf-Paramyx-P; 1.
PE 1: Evidence at protein level;
KW 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; Inhibition of host STAT2 by virus;
KW Interferon antiviral system evasion; Metal-binding; Phosphoprotein;
KW Reference proteome; RNA editing; Viral immunoevasion; Zinc.
FT CHAIN 1..456
FT /note="Non-structural protein V"
FT /id="PRO_0000236015"
FT REGION 53..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 427
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 445
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 257
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 350
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT VARIANT 206
FT /note="P -> L (in strain: Isolate Malaysian flying-fox)"
FT VARIANT 274
FT /note="S -> R (in strain: Isolate NV/MY/99/VRI-0626)"
FT VARIANT 304
FT /note="T -> A (in strain: Isolate NV/MY/99/VRI-0626)"
FT VARIANT 378
FT /note="E -> K (in strain: Isolate NV/MY/99/VRI-0626)"
SQ SEQUENCE 456 AA; 50325 MW; 5E6735DC205B0EF9 CRC64;
MDKLELVNDG LNIIDFIQKN QKEIQKTYGR SSIQQPSIKD QTKAWEDFLQ CTSGESEQVE
GGMSKDDGDV ERRNLEDLSS TSPTDGTIGK RVSNTRDWAE GSDDIQLDPV VTDVVYHDHG
GECTGYGFTS SPERGWSDYT SGANNGNVCL VSDAKMLSYA PEIAVSKEDR ETDLVHLENK
LSTTGLNPTA VPFTLRNLSD PAKDSPVIAE HYYGLGVKEQ NVGPQTSRNV NLDSIKLYTS
DDEEADQLEF EDEFAGSSSE VIVGISPEDE EPSSVGGKPN ESIGRTIEGQ SIRDNLQAKD
NKSTDVPGAG PKDSAVKEEP PQKRLPMLAE EFECSGSEDP IIRELLKENS LINCQQGKDA
QPPYHWSIER SISPDKTEIV NGAVQTADRQ RPGTPMPKSR GIPIKKGHRR EISICWDGKR
AWVEEWCNPA CSRITPLPRR QECQCGECPT ECFHCG
