V_SENDO
ID V_SENDO Reviewed; 369 AA.
AC P69287;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Protein V;
GN Name=P/V/C;
OS Sendai virus (strain Ohita) (SeV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=302272;
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=9400971; DOI=10.1099/0022-1317-78-12-3207;
RA Itoh M., Isegawa Y., Hotta H., Homma M.;
RT "Isolation of an avirulent mutant of Sendai virus with two amino acid
RT mutations from a highly virulent field strain through adaptation to LLC-MK2
RT cells.";
RL J. Gen. Virol. 78:3207-3215(1997).
RN [2]
RP FUNCTION, AND INTERACTION WITH HOST DHX58.
RX PubMed=22301134; DOI=10.1128/jvi.06405-11;
RA Childs K., Randall R., Goodbourn S.;
RT "Paramyxovirus V proteins interact with the RNA Helicase LGP2 to inhibit
RT RIG-I-dependent interferon induction.";
RL J. Virol. 86:3411-3421(2012).
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:22301134}.
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 O57285), the +2G edited RNA gives rise to the W protein (AC
CC P69288) (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; AB005796; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P69287; -.
DR Proteomes; UP000006563; 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 1: Evidence at protein level;
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 RNA editing; Viral immunoevasion; Zinc.
FT CHAIN 1..369
FT /note="Protein V"
FT /id="PRO_0000142828"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..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 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..194
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; 40254 MW; D6B31BD0827336A5 CRC64;
MDQDALISKE DSEVEREASG GRESLSDVIG FLDAVLSSEP TDIGGDRSWL HNTINTLQRP
GSTHRVKGEG EGEVSTSSTQ DNRSGEESRV SGGTSEPEAE AHARNVDKQN IHWATGRGAS
TDSVPQDLGN GRDSGILEDP PNEGGYPRSG AEDENREMAA NPDKRGEDQA EGLPEEIRRS
APLPDEREGR ADNNGRGVEP GSPHSARVTG VLVIPSPELE EAVLQRNKRR PANSGSRSLT
PVVVPSTRSP PPDHDNSTRS PPRKPPTTQD EHTNPRNTPA VRIKDRRPPT GTRSAPDRPT
DGYPTHPSPE TDATKKGHRR EHIIYERDGY IVNESWCNPV CSRIRVVPRR ELCVCKACPK
ICKLCRDGI
