ID   V_NDVU2                 Reviewed;         239 AA.
AC   Q06428;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Non-structural protein V;
GN   Name=P/V;
OS   Newcastle disease virus (strain Ulster/2C) (NDV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Avulavirinae;
OC   Orthoavulavirus; Avian orthoavulavirus 1.
OX   NCBI_TaxID=36411;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA / MRNA], AND RNA EDITING.
RX   PubMed=8277263; DOI=10.1099/0022-1317-74-12-2539;
RA   Steward M., Vipond I.B., Millar N.S., Emmerson P.T.;
RT   "RNA editing in Newcastle disease virus.";
RL   J. Gen. Virol. 74:2539-2547(1993).
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. Plays a role in the inhibition of
CC       host apoptosis. Interacts with and down-regulates the expression of
CC       host TXNL1. In turn, inhibits TXNL1-induced apoptosis through the BCL2-
CC       BAX-caspase 3 pathway. Inhibits host apoptosis also by negatively
CC       regulating host CacyBP/SIP. Promotes viral replication by activating
CC       the extracellular signal-regulated kinase (ERK) pathway.
CC       {ECO:0000250|UniProtKB:P0C765}.
CC   -!- SUBUNIT: Interacts with host STAT1. Interacts with host TXNL1.
CC       Interacts (via C-terminus) with host CacyBP; this interaction inhibits
CC       host cell apoptosis. {ECO:0000250|UniProtKB:P0C765}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:P0C765}.
CC       Host nucleus {ECO:0000250|UniProtKB:P0C765}.
CC   -!- RNA EDITING: Modified_positions=135 {ECO:0000269|PubMed:8277263};
CC       Note=Partially edited. RNA editing at this position consists of an
CC       insertion of one guanine nucleotide. The sequence displayed here is the
CC       V protein, derived from the edited RNA. The unedited RNA gives rise to
CC       the P protein (AC Q06427).;
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DR   EMBL; Z26249; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   SMR; Q06428; -.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; 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; IPR025909; Soyouz_module.
DR   Pfam; PF14313; Soyouz_module; 1.
DR   Pfam; PF13008; zf-Paramyx-P; 1.
PE   3: Inferred from homology;
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; RNA editing;
KW   Viral immunoevasion; Zinc.
FT   CHAIN           1..239
FT                   /note="Non-structural protein V"
FT                   /id="PRO_0000142813"
FT   REGION          30..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..104
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         200
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         212
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
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;  25379 MW;  E60075ADDAC40DE6 CRC64;
     MATFTDAEID ELFETSGTVI DSIITAQGKP VETVGRSAIP RGKTKALSSA WEKHGSVQSP
     ASQDTPDRQD RSDKQLSTPE QVTPHDSPPA TSTDQPPTQA ADEAGDTQLK TGASNSLLSM
     LDKLSNKSSN AKKGPMVKPP GRASSTSDST AGESTKPRKQ SRETAEPGQG RPWKPGHRRE
     HSISWTMGGV TTISWCNPSC SPIRAEPRQY SCTCGSCPAT CRLCASDDVY DGGDITEGK