V_MEASC
ID V_MEASC Reviewed; 299 AA.
AC P0C774;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Non-structural protein V;
GN Name=P/V;
OS Measles virus (strain Ichinose-B95a) (MeV) (Subacute sclerose
OS panencephalitis virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=645098;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10949953; DOI=10.1023/a:1008196729676;
RA Takeuchi K., Miyajima N., Kobune F., Tashiro M.;
RT "Comparative nucleotide sequence analyses of the entire genomes of B95a
RT cell-isolated and vero cell-isolated measles viruses from the same
RT patient.";
RL Virus Genes 20:253-257(2000).
RN [2]
RP FUNCTION.
RX PubMed=12804771; DOI=10.1016/s0014-5793(03)00528-3;
RA Takeuchi K., Kadota S.I., Takeda M., Miyajima N., Nagata K.;
RT "Measles virus V protein blocks interferon (IFN)-alpha/beta but not IFN-
RT gamma signaling by inhibiting STAT1 and STAT2 phosphorylation.";
RL FEBS Lett. 545:177-182(2003).
RN [3]
RP FUNCTION, AND INTERACTION WITH HOST STAT2.
RX PubMed=18579593; DOI=10.1128/jvi.00831-08;
RA Ramachandran A., Parisien J.P., Horvath C.M.;
RT "STAT2 is a primary target for measles virus V protein-mediated alpha/beta
RT interferon signaling inhibition.";
RL J. Virol. 82:8330-8338(2008).
RN [4]
RP FUNCTION, AND INTERACTION WITH HOST IRF7 AND CHUK.
RC STRAIN=Schwarz vaccine;
RX PubMed=18922877; DOI=10.1128/jvi.01321-08;
RA Pfaller C.K., Conzelmann K.K.;
RT "Measles virus V protein is a decoy substrate for IkappaB kinase alpha and
RT prevents Toll-like receptor 7/9-mediated interferon induction.";
RL J. Virol. 82:12365-12373(2008).
RN [5]
RP FUNCTION, AND INTERACTION WITH HOST IFIH1 AND DHX58.
RX PubMed=19403670; DOI=10.1128/jvi.00153-09;
RA Parisien J.P., Bamming D., Komuro A., Ramachandran A., Rodriguez J.J.,
RA Barber G., Wojahn R.D., Horvath C.M.;
RT "A shared interface mediates paramyxovirus interference with antiviral RNA
RT helicases MDA5 and LGP2.";
RL J. Virol. 83:7252-7260(2009).
RN [6]
RP FUNCTION, AND INTERACTION WITH HOST RELA.
RC STRAIN=Schwarz vaccine;
RX PubMed=21270162; DOI=10.1128/jvi.02342-10;
RA Schuhmann K.M., Pfaller C.K., Conzelmann K.K.;
RT "The measles virus V protein binds to p65 (RelA) to suppress NF-kappaB
RT activity.";
RL J. Virol. 85:3162-3171(2011).
RN [7]
RP FUNCTION, AND INTERACTION WITH HOST JAK1 AND TYK2.
RC STRAIN=Dublin;
RX PubMed=23431397; DOI=10.1371/journal.pone.0057063;
RA Chinnakannan S.K., Nanda S.K., Baron M.D.;
RT "Morbillivirus v proteins exhibit multiple mechanisms to block type 1 and
RT type 2 interferon signalling pathways.";
RL PLoS ONE 8:E57063-E57063(2013).
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 Blocks the type I interferon signaling pathway by interacting with host
CC TYK2 and thereby inhibiting downstream STAT1 and STAT2 phosphorylation.
CC Moderately affects the type II interferon signaling.
CC {ECO:0000269|PubMed:12804771, ECO:0000269|PubMed:18579593,
CC ECO:0000269|PubMed:18922877, ECO:0000269|PubMed:19403670,
CC ECO:0000269|PubMed:21270162, ECO:0000269|PubMed:23431397}.
CC -!- SUBUNIT: Interacts with host IFIH1/MDA5 and DHX58/LGP2. Interacts with
CC host TYK2; this interaction inhibits the type I interferon signaling
CC pathway without affecting the type II pathway. Interacts with host
CC IRF7; this interaction inhibits IRF7 translocation to the nucleus.
CC Interacts with host CHUK and RELA. Interacts (via C-terminus) with host
CC STAT2. {ECO:0000269|PubMed:18579593, ECO:0000269|PubMed:18922877,
CC ECO:0000269|PubMed:19403670, ECO:0000269|PubMed:21270162,
CC ECO:0000269|PubMed:23431397}.
CC -!- INTERACTION:
CC P0C774; Q9BYX4: IFIH1; Xeno; NbExp=3; IntAct=EBI-3650423, EBI-6115771;
CC P0C774; Q04206: RELA; Xeno; NbExp=3; IntAct=EBI-3650423, EBI-73886;
CC P0C774; P52630: STAT2; Xeno; NbExp=4; IntAct=EBI-3650423, EBI-1546963;
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=231; Note=Partially edited. RNA editing
CC at this position consists of an insertion of one guanine nucleotide.
CC The sequence displayed here is the V protein, derived from the edited
CC RNA. The unedited RNA gives rise to the P protein (AC Q9WMB4).;
CC -!- SIMILARITY: Belongs to the paramyxoviruses V protein family.
CC {ECO:0000305}.
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DR EMBL; AB016162; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P0C774; -.
DR DIP; DIP-61740N; -.
DR IntAct; P0C774; 5.
DR Proteomes; UP000008699; 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:0039564; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT2 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 GO; GO:0039557; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF7 activity; IEA:UniProtKB-KW.
DR InterPro; IPR024279; Paramyx_V_Zn-bd.
DR InterPro; IPR028243; Paramyxo_P/V_N.
DR Pfam; PF13825; Paramyxo_P_V_N; 1.
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 interferon signaling pathway by virus;
KW Inhibition of host IRF7 by virus; Inhibition of host MDA5 by virus;
KW Inhibition of host RLR pathway by virus; Inhibition of host STAT2 by virus;
KW Interferon antiviral system evasion; Metal-binding; Reference proteome;
KW RNA editing; Viral immunoevasion; Zinc.
FT CHAIN 1..299
FT /note="Non-structural protein V"
FT /id="PRO_0000394721"
FT REGION 40..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 299 AA; 32016 MW; FEDBD36B65E382D0 CRC64;
MAEEQARHVK NGLECIRALK AEPIGSLAVE EAMAAWSEIS DNPGQDRATC KEEEAGSSGL
SKPCLSAIGS TEGGAPRIRG QGSGESDDDA ETLGIPSRNL QASSTGLQCY HVYDHSGEAV
KGIQDADSIM VQSGLDGDST LSGGDDESEN SDVDIGEPDT EGYAITDRGS APISMGFRAS
DVETAEGGEI HELLKLQSRG NNFPKLGKTL NVPPPPNPSR ASTSETPIKK GHRREIGLIW
NGDRVFIDRW CNPMCSKVTL GTIRARCTCG ECPRVCEQCR TDTGVDTRIW YHNLPEIPE
