V_SENDH
ID V_SENDH Reviewed; 384 AA.
AC P69280;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Protein V;
GN Name=P/V/C;
OS Sendai virus (strain Harris) (SeV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11196;
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=6317203; DOI=10.1016/0092-8674(83)90115-0;
RA Giorgi C., Blumberg B.M., Kolakofsky D.;
RT "Sendai virus contains overlapping genes expressed from a single mRNA.";
RL Cell 35:829-836(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Kolakofsky D.;
RL Submitted (JAN-2005) to UniProtKB.
RN [3]
RP FUNCTION, AND RNA EDITING.
RX PubMed=9034340; DOI=10.1093/emboj/16.3.578;
RA Kato A., Kiyotani K., Sakai Y., Yoshida T., Nagai Y.;
RT "The paramyxovirus, Sendai virus, V protein encodes a luxury function
RT required for viral pathogenesis.";
RL EMBO J. 16:578-587(1997).
RN [4]
RP FUNCTION, ZINC-BINDING DOMAIN, AND RNA EDITING.
RX PubMed=9514977; DOI=10.1006/viro.1998.9027;
RA Delenda C., Taylor G., Hausmann S., Garcin D., Kolakofsky D.;
RT "Sendai viruses with altered P, V, and W protein expression.";
RL Virology 242:327-337(1998).
RN [5]
RP INTERACTION WITH HUMAN IFIH1/MDA5, AND INTERFERON EVASION.
RX PubMed=15563593; DOI=10.1073/pnas.0407639101;
RA Andrejeva J., Childs K.S., Young D.F., Carlos T.S., Stock N., Goodbourn S.,
RA Randall R.E.;
RT "The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase,
RT mda-5, and inhibit its activation of the IFN-beta promoter.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:17264-17269(2004).
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:9034340, ECO:0000269|PubMed:9514977}.
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.
CC -!- RNA EDITING: Modified_positions=318 {ECO:0000269|PubMed:9034340,
CC ECO:0000269|PubMed:9514977}; Note=Partially edited. RNA editing at this
CC position consists of an insertion of one or two guanine nucleotides.
CC The sequence displayed here is the V protein, derived from the +1G
CC edited RNA. The unedited RNA gives rise to the P protein (AC P04859),
CC the +2G edited RNA gives rise to the W protein (AC P69281).;
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 SMR; P69280; -.
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..384
FT /note="Protein V"
FT /id="PRO_0000142827"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..318
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 86..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
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 68
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 125
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 192
FT /note="Phosphoserine; by host"
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"
FT VARIANT 311
FT /note="S -> T"
SQ SEQUENCE 384 AA; 41602 MW; 54CAECCBEB047BB2 CRC64;
MDQDAFILKE DSEVEREAPG GRESLSDVIG FLDAVLSSEP TDIGGDRSWL HNTINTPQGP
GSAHRAKSEG EGEVSTPSTQ DNRSGEESRV SGRTSKPEAE AHAGNLDKQN IHRAFGGRTG
TNSVSQDLGD GGDSGILENP PNERGYPRSG IEDENREMAA HPDKRGEDQA EGLPEEVRGG
TSLPDEGEGG ASNNGRSMEP GSSHSARVTG VLVIPSPELE EAVLRRNKRR PTNSGSKPLT
PATVPGTRSP PLNRYNSTGS PPGKPPSTQD EHINSGDTPA VRVKDRKPPI GTRSVSDCPA
NGRPIHPGLE SDSTKKGHRR EHIIYERDGY IVDESWCNPV CSRIRIIPRR ELCVCKTCPK
VCKLCRDDIQ CMRPDPFCRE IFRS
