V_NDVB1
ID V_NDVB1 Reviewed; 239 AA.
AC P0C765;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Protein V;
GN Name=V;
OS Newcastle disease virus (strain Chicken/United States/B1/48) (NDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC Orthoavulavirus; Avian orthoavulavirus 1.
OX NCBI_TaxID=652953;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Sellers H.S., Seal B.S.;
RT "Complete sequence for the B1 strain of Newcastle disease virus.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION.
RX PubMed=12885886; DOI=10.1128/jvi.77.16.8676-8685.2003;
RA Huang Z., Krishnamurthy S., Panda A., Samal S.K.;
RT "Newcastle disease virus V protein is associated with viral pathogenesis
RT and functions as an alpha interferon antagonist.";
RL J. Virol. 77:8676-8685(2003).
RN [3]
RP FUNCTION.
RX PubMed=26859759; DOI=10.1371/journal.pone.0148560;
RA Qiu X., Fu Q., Meng C., Yu S., Zhan Y., Dong L., Song C., Sun Y., Tan L.,
RA Hu S., Wang X., Liu X., Peng D., Liu X., Ding C.;
RT "Newcastle Disease Virus V Protein Targets Phosphorylated STAT1 to Block
RT IFN-I Signaling.";
RL PLoS ONE 11:E0148560-E0148560(2016).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HOST CACYBP.
RX PubMed=30234028; DOI=10.3389/fcimb.2018.00304;
RA Chu Z., Wang C., Tang Q., Shi X., Gao X., Ma J., Lu K., Han Q., Jia Y.,
RA Wang X., Adam F.E.A., Liu H., Xiao S., Wang X., Yang Z.;
RT "Newcastle Disease Virus V Protein Inhibits Cell Apoptosis and Promotes
RT Viral Replication by Targeting CacyBP/SIP.";
RL Front. Cell. Infect. Microbiol. 8:304-304(2018).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30213106; DOI=10.3390/v10090489;
RA Chu Z., Ma J., Wang C., Lu K., Li X., Liu H., Wang X., Xiao S., Yang Z.;
RT "Newcastle Disease Virus V Protein Promotes Viral Replication in HeLa Cells
RT through the Activation of MEK/ERK Signaling.";
RL Viruses 10:0-0(2018).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HOST TXNL1.
RX PubMed=30290847; DOI=10.1186/s13567-018-0599-6;
RA Wang C., Chu Z., Liu W., Pang Y., Gao X., Tang Q., Ma J., Lu K.,
RA Adam F.E.A., Dang R., Xiao S., Wang X., Yang Z.;
RT "Newcastle disease virus V protein inhibits apoptosis in DF-1 cells by
RT downregulating TXNL1.";
RL Vet. Res. 49:102-102(2018).
CC -!- FUNCTION: Protects the virus against cell antiviral state by blocking
CC host interferon signaling. Mechanistically, targets host phosphorylated
CC STAT1 (phospho-STAT1) for degradation, thereby inhibiting the
CC interferon alpha signaling pathway (PubMed:12885886, PubMed:26859759).
CC Plays a role in the inhibition of host apoptosis (PubMed:30290847).
CC Interacts with and down-regulates the expression of host TXNL1. In
CC turn, inhibits TXNL1-induced apoptosis through the BCL2-BAX-caspase 3
CC pathway (PubMed:30290847). Inhibits host apoptosis also by negatively
CC regulating host CacyBP/SIP (PubMed:30234028). Promotes viral
CC replication by activating the extracellular signal-regulated kinase
CC (ERK) pathway (PubMed:30213106). {ECO:0000269|PubMed:12885886,
CC ECO:0000269|PubMed:26859759, ECO:0000269|PubMed:30213106,
CC ECO:0000269|PubMed:30234028, ECO:0000269|PubMed:30290847}.
CC -!- SUBUNIT: Interacts with host STAT1. Interacts with host TXNL1
CC (PubMed:30290847). Interacts (via C-terminus) with host CacyBP; this
CC interaction inhibits host cell apoptosis (PubMed:30234028).
CC {ECO:0000269|PubMed:30234028, ECO:0000269|PubMed:30290847}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:30213106,
CC ECO:0000269|PubMed:30234028, ECO:0000269|PubMed:30290847}. Host nucleus
CC {ECO:0000269|PubMed:30213106, ECO:0000269|PubMed:30234028,
CC ECO:0000269|PubMed:30290847}.
CC -!- RNA EDITING: Modified_positions=136 {ECO:0000250}; Note=Partially
CC edited. RNA editing at this position consists of an insertion of one or
CC two guanine nucleotides. The sequence displayed here is the V protein,
CC derived from the +1G edited RNA. The unedited RNA gives rise to the P
CC protein (AC Q9DLD6), the +2G edited RNA gives rise to the W protein (AC
CC P0C766) (By similarity). {ECO:0000250};
CC -!- MISCELLANEOUS: The protein V from strain B1 contains one putative zinc-
CC binding domain on its C-terminal region whereas protein V from wild-
CC type avulavirus strains possess two.
CC -!- SIMILARITY: Belongs to the paramyxoviruses V protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF309418; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR IntAct; P0C765; 10.
DR Proteomes; UP000002328; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019050; P:suppression by virus of host apoptotic process; IDA:UniProtKB.
DR GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IDA:UniProtKB.
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; IPR025909; Soyouz_module.
DR Pfam; PF14313; Soyouz_module; 1.
DR Pfam; PF13008; zf-Paramyx-P; 1.
PE 1: Evidence at protein level;
KW Host cytoplasm; Host nucleus; Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host MDA5 by virus; Inhibition of host RLR pathway by virus;
KW Interferon antiviral system evasion; Metal-binding;
KW Modulation of host cell apoptosis by virus; Reference proteome;
KW RNA editing; Viral immunoevasion; Zinc.
FT CHAIN 1..239
FT /note="Protein V"
FT /id="PRO_0000390629"
FT REGION 47..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 239 AA; 25730 MW; 138E77CC0952A468 CRC64;
MATFTDAEID ELFETSGTVI DNIITAQGKP AETVGRSAIP QGKTKVLSAA WEKHGSIQPP
ASQDNPDRQD RSDKQPSTPE QTTPHDSPPA TSADQPPTQA TDEAVDTQLR TGASNSLLLM
LDKLSNKSSN AKKGPMVEPP RGESPTSDST AGESTQSRKQ SGKTAEPSQG RPWKPGHRRE
HSISWTMGGV TTISWCNPSW SPIKAEPKQY PCFCGSFPPT CRLCASDDVY YGGDFPKSK
