V_SENDZ
ID V_SENDZ Reviewed; 384 AA.
AC P69282;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Protein V;
GN Name=P/V/C;
OS Sendai virus (strain Z) (SeV) (Sendai virus (strain HVJ)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Respirovirus.
OX NCBI_TaxID=11198;
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=6316257; DOI=10.1093/nar/11.21.7317;
RA Shioda T., Hidaka Y., Kanda T., Shibuta H., Nomoto A., Iwasaki K.;
RT "Sequence of 3,687 nucleotides from the 3' end of Sendai virus genome RNA
RT and the predicted amino acid sequences of viral NP, P and C proteins.";
RL Nucleic Acids Res. 11:7317-7330(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Shibuta H.;
RL Submitted (FEB-1985) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP RNA EDITING.
RX PubMed=1655410; DOI=10.1002/j.1460-2075.1991.tb07860.x;
RA Curran J., Boeck R., Kolakofsky D.;
RT "The Sendai virus P gene expresses both an essential protein and an
RT inhibitor of RNA synthesis by shuffling modules via mRNA editing.";
RL EMBO J. 10:3079-3085(1991).
RN [4]
RP ZINC-BINDING DOMAIN, AND MUTAGENESIS OF CYS-337; CYS-341; CYS-353; CYS-355;
RP CYS-358 AND CYS-365.
RX PubMed=10933690; DOI=10.1128/jvi.74.17.7834-7841.2000;
RA Huang C., Kiyotani K., Fujii Y., Fukuhara N., Kato A., Nagai Y.,
RA Yoshida T., Sakaguchi T.;
RT "Involvement of the zinc-binding capacity of Sendai virus V protein in
RT viral pathogenesis.";
RL J. Virol. 74:7834-7841(2000).
RN [5]
RP MUTAGENESIS OF HIS-318; ARG-319; ARG-320; GLU-321; TRP-336; PRO-339;
RP 337-CYS--CYS-341; 353-CYS--CYS-358 AND 362-CYS--CYS-365.
RX PubMed=12202220; DOI=10.1006/viro.2002.1516;
RA Fukuhara N., Huang C., Kiyotani K., Yoshida T., Sakaguchi T.;
RT "Mutational analysis of the Sendai virus V protein: importance of the
RT conserved residues for Zn binding, virus pathogenesis, and efficient RNA
RT editing.";
RL Virology 299:172-181(2002).
RN [6]
RP INTERFERON EVASION.
RX PubMed=15231393; DOI=10.1016/j.virol.2004.04.025;
RA Komatsu T., Takeuchi K., Yokoo J., Gotoh B.;
RT "C and V proteins of Sendai virus target signaling pathways leading to IRF-
RT 3 activation for the negative regulation of interferon-beta production.";
RL Virology 325:137-148(2004).
RN [7]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH HOST IRF3; DDX58 AND
RP IFIH1.
RX PubMed=22532687; DOI=10.1128/jvi.06705-11;
RA Irie T., Kiyotani K., Igarashi T., Yoshida A., Sakaguchi T.;
RT "Inhibition of interferon regulatory factor 3 activation by paramyxovirus V
RT protein.";
RL J. Virol. 86:7136-7145(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.
CC {ECO:0000269|PubMed:22532687}.
CC -!- SUBUNIT: Interacts with host IFIH1/MDA5, DDX58 and DHX58/LGP2.
CC Interacts with host IRF3. {ECO:0000269|PubMed:22532687}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:22532687}.
CC -!- DOMAIN: The C-terminal zinc-binding domain is involved in binding to
CC IFIH1/MDA5 (By similarity). This domain is also involved in viral
CC pathogenesis. {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=318 {ECO:0000269|PubMed:1655410};
CC Note=Partially edited. RNA editing at this position consists of an
CC insertion of one or two guanine nucleotides. The sequence displayed
CC here is the V protein, derived from the +1G edited RNA. The unedited
CC RNA gives rise to the P protein (AC P04860), the +2G edited RNA gives
CC rise to the W protein (AC P69283).;
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; X00087; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P69282; -.
DR Proteomes; UP000006560; Genome.
DR GO; GO:0044164; C:host cell cytosol; IDA:CACAO.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; IMP:CACAO.
DR GO; GO:0039503; P:suppression by virus of host innate immune response; IMP:CACAO.
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; IDA:CACAO.
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 Reference proteome; RNA editing; Viral immunoevasion; Zinc.
FT CHAIN 1..384
FT /note="Protein V"
FT /id="PRO_0000142829"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..317
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 MUTAGEN 318
FT /note="H->N: Attenuates viral pathogenicity in mice."
FT /evidence="ECO:0000269|PubMed:12202220"
FT MUTAGEN 319
FT /note="R->W: 80% decrease of in vitro zinc binding.
FT Attenuates viral pathogenicity in mice."
FT /evidence="ECO:0000269|PubMed:12202220"
FT MUTAGEN 320
FT /note="R->G: Attenuates viral pathogenicity in mice."
FT /evidence="ECO:0000269|PubMed:12202220"
FT MUTAGEN 321
FT /note="E->K: Attenuates viral pathogenicity in mice."
FT /evidence="ECO:0000269|PubMed:12202220"
FT MUTAGEN 336
FT /note="W->G: Attenuates viral pathogenicity in mice."
FT /evidence="ECO:0000269|PubMed:12202220"
FT MUTAGEN 337..341
FT /note="CNPVC->SNPVS: 60% decrease of in vitro zinc binding,
FT attenuates viral pathogenicity in mice."
FT /evidence="ECO:0000269|PubMed:12202220"
FT MUTAGEN 337
FT /note="C->S: 50% decrease of in vitro zinc-binding."
FT /evidence="ECO:0000269|PubMed:10933690"
FT MUTAGEN 339
FT /note="P->T: Decreases viral pathogenicity in mice."
FT /evidence="ECO:0000269|PubMed:12202220"
FT MUTAGEN 341
FT /note="C->S: 32% decrease of in vitro zinc-binding,
FT attenuates viral pathogenicity in mice."
FT /evidence="ECO:0000269|PubMed:10933690"
FT MUTAGEN 353..358
FT /note="CVCKTC->RVRKTS: Attenuates viral pathogenicity in
FT mice."
FT /evidence="ECO:0000269|PubMed:12202220"
FT MUTAGEN 353
FT /note="C->R: 60% decrease of in vitro zinc-binding."
FT /evidence="ECO:0000269|PubMed:10933690"
FT MUTAGEN 355
FT /note="C->R: 60% decrease of in vitro zinc-binding."
FT /evidence="ECO:0000269|PubMed:10933690"
FT MUTAGEN 358
FT /note="C->S: 55% decrease of in vitro zinc-binding."
FT /evidence="ECO:0000269|PubMed:10933690"
FT MUTAGEN 362..365
FT /note="CKLC->SKLR: 60% decrease of in vitro zinc-binding.
FT Attenuates viral pathogenicity in mice."
FT /evidence="ECO:0000269|PubMed:12202220"
FT MUTAGEN 365
FT /note="C->R: 78% decrease of in vitro zinc-binding.
FT Attenuates viral pathogenicity in mice."
FT /evidence="ECO:0000269|PubMed:10933690"
SQ SEQUENCE 384 AA; 41636 MW; 4C768258536BBF36 CRC64;
MDQDAFILKE DSEVEREAPG GRESLSDVIG FLDAVLSSEP TDIGGDRSWL HNTINTPQGP
GSAHRAKSEG EGEVSTPSTQ DNRSGEESRV SGRTSKPEAE AHAGNLDKQN IHRAFGGRTG
TNSVSQDLGD GGDSGILENP PNERGYPRSG IEDENREMAA HPDKRGEDQA EGLPEEVRGS
TSLPDEGEGG ASNNGRSMEP GSSHSARVTG VLVIPSPELE EAVLRRNKRR PTNSGSKPLT
PATVPGTRSP PLNRYNSTGS PPGKPPSTQD EHINSGDTPA VRVKDRKPPI GTRSVSDCPA
NGRSIHPGLE TDSTKKGHRR EHIIYERDGY IVDESWCNPV CSRIRIIPRR ELCVCKTCPK
VCKLCRDDIQ CMRPDPFCRE IFRS
