V_SV41
ID V_SV41 Reviewed; 225 AA.
AC P36315;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Non-structural protein V;
GN Name=P/V;
OS Simian virus 41 (SV41).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Orthorubulavirus.
OX NCBI_TaxID=2560766;
OH NCBI_TaxID=314293; Simiiformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
RC STRAIN=Toshiba/Chanock;
RX PubMed=8492098; DOI=10.1099/0022-1317-74-5-911;
RA Kawano M., Tsurudome M., Oki N., Nishio M., Komada H., Matsumura H.,
RA Kusagawa S., Ohta H., Ito Y.;
RT "Sequence determination of the P gene of simian virus 41: presence of
RT irregular deletions near the RNA-editing sites of paramyxoviruses.";
RL J. Gen. Virol. 74:911-916(1993).
RN [2]
RP FUNCTION.
RX PubMed=11533180; DOI=10.1128/jvi.75.19.9165-9176.2001;
RA Nishio M., Tsurudome M., Ito M., Kawano M., Komada H., Ito Y.;
RT "High resistance of human parainfluenza type 2 virus protein-expressing
RT cells to the antiviral and anti-cell proliferative activities of alpha/beta
RT interferons: cysteine-rich V-specific domain is required for high
RT resistance to the interferons.";
RL J. Virol. 75:9165-9176(2001).
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 (By similarity). Interacts with host IFIH1/MDA5 and
CC DHX58/LGP2 to inhibit the transduction pathway involved in the
CC activation of IFN-beta promoter, thus protecting the virus against cell
CC antiviral state. Efficiently blocks type I and type II IFN signaling
CC following infection, probably by targeting host STAT1 for proteasomal
CC degradation. {ECO:0000250, ECO:0000269|PubMed:11533180}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=164 {ECO:0000269|PubMed:8492098};
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 Q86606).;
CC -!- SIMILARITY: Belongs to the paramyxoviruses V protein family.
CC {ECO:0000305}.
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DR EMBL; S60811; AAB26639.1; -; Genomic_RNA.
DR EMBL; X64275; CAA45571.1; -; Genomic_RNA.
DR PIR; JQ2040; JQ2040.
DR SMR; P36315; -.
DR Proteomes; UP000108270; 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: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; 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-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; Reference proteome; RNA editing; Viral immunoevasion; Zinc.
FT CHAIN 1..225
FT /note="Non-structural protein V"
FT /id="PRO_0000142831"
FT REGION 145..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 211
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 218
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"
SQ SEQUENCE 225 AA; 24048 MW; 1A749260CAB7D71E CRC64;
MAEEPTYTAE QVNDVVHAGL GTVDFFLSRP VDGQSSLGKG SVPPGITAVL TNAAELKAKT
AAAAPVKPKR KKIQHMTPAY TIADNGDPNR LPANTPIANP LIPIERPPGR MTDLDLATGT
VTQGTYKGVE LAKAGKNALL TRFSSGPSLT DQASSKDPNF KRGGEIDGRH KGRHRREWSI
AWVGDEVKVY EWCNPTCAPV TATDRKFSCT CGTCPDRCGE CEGDN
