V_SENDA
ID V_SENDA Reviewed; 369 AA.
AC Q9DUE1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Protein V;
GN Name=P/V/C;
OS Sendai virus (strain Hamamatsu) (SeV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=302271;
OH NCBI_TaxID=10144; Cavia cutleri (Guinea pig).
OH NCBI_TaxID=36483; Cricetidae sp. (Hamster).
OH NCBI_TaxID=10090; Mus musculus (Mouse).
OH NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11210938; DOI=10.1023/a:1008130318633;
RA Fujii Y., Kiyotani K., Yoshida T., Sakaguchi T.;
RT "Conserved and non-conserved regions in the Sendai virus genome: evolution
RT of a gene possessing overlapping reading frames.";
RL Virus Genes 22:47-52(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12163573; DOI=10.1128/jvi.76.17.8540-8547.2002;
RA Fujii Y., Sakaguchi T., Kiyotani K., Huang C., Fukuhara N., Egi Y.,
RA Yoshida T.;
RT "Involvement of the leader sequence in Sendai virus pathogenesis revealed
RT by recovery of a pathogenic field isolate from cDNA.";
RL J. Virol. 76:8540-8547(2002).
RN [3]
RP FUNCTION.
RX PubMed=12954223; DOI=10.1016/s0042-6822(03)00350-7;
RA Sakaguchi T., Kiyotani K., Watanabe H., Huang C., Fukuhara N., Fujii Y.,
RA Shimazu Y., Sugahara F., Nagai Y., Yoshida T.;
RT "Masking of the contribution of V protein to Sendai virus pathogenesis in
RT an infection model with a highly virulent field isolate.";
RL Virology 313:581-587(2003).
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 Interacts also with and inhibits host IRF3 (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:12954223}.
CC -!- SUBUNIT: Interacts with host IFIH1/MDA5, DDX58 and DHX58/LGP2.
CC Interacts with host IRF3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The C-terminal zinc-binding domain is involved in binding to
CC IFIH1/MDA5. This domain is also involved in viral pathogenesis (By
CC similarity). {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=318 {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 Q9DUE2), the +2G edited RNA gives rise to the W protein (AC
CC P69286) (By similarity). {ECO:0000250};
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/Y proteins.
CC -!- SIMILARITY: Belongs to the paramyxoviruses V protein family.
CC {ECO:0000305}.
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DR EMBL; AB039658; BAB20021.1; -; Genomic_RNA.
DR EMBL; AB065186; BAC79127.1; -; Genomic_RNA.
DR EMBL; AB065187; BAC07507.1; -; Genomic_RNA.
DR EMBL; AB065188; BAC79135.1; -; Genomic_RNA.
DR EMBL; AB065189; BAC79143.1; -; Genomic_RNA.
DR SMR; Q9DUE1; -.
DR Proteomes; UP000007191; Genome.
DR Proteomes; UP000008510; Genome.
DR Proteomes; UP000008857; Genome.
DR Proteomes; UP000180650; Genome.
DR Proteomes; UP000180718; 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: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 GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
DR InterPro; IPR024279; Paramyx_V_Zn-bd.
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 IRF3 by virus; Inhibition of host MDA5 by virus;
KW Inhibition of host RLR pathway by virus;
KW Interferon antiviral system evasion; Metal-binding; Phosphoprotein;
KW Reference proteome; RNA editing; Viral immunoevasion; Zinc.
FT CHAIN 1..369
FT /note="Protein V"
FT /id="PRO_0000142825"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 249
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 257
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 260
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 369 AA; 40149 MW; 04CAA3D5C099BCA9 CRC64;
MDQDALISKE DSEVEREASG GRESLSDVIG FLDAVLSSEP TDIGGDRSWL HNTINTLQRP
GSTHRAKGEG EGEVSTSSTQ DNRSGEESRV SGGTSEPEAE AHARNVDKQN IHWATGRGAS
TDSVPQDLGN GRDSGILEDP PNEGGYPRSG AEDENREMAA NPDKRGEDQA EGLPEEIRRS
APLPDEGEGR ADNNGRGVES GSPHSARVTG VLVIPSPELE EAVLQRNKRR PANSGSRSLT
PVVVPSTRSP PPDHDNSTRS PPRKPPTTQD EHTNPRNTPA VRIKDRRPPT GTRSAPDRPT
DGYPTHPGPE TDATKKGHRR EHIIYERDGY IVNESWCNPV CSRIRVISRR ELCVCKACPK
ICKLCRDDI
