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V_MEASE
ID   V_MEASE                 Reviewed;         299 AA.
AC   Q9EMA9;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Non-structural protein V;
GN   Name=P/V;
OS   Measles virus (strain Edmonston) (MeV) (Subacute sclerose panencephalitis
OS   virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=11235;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11134304; DOI=10.1128/jvi.75.2.910-920.2001;
RA   Parks C.L., Lerch R.A., Walpita P., Wang H.P., Sidhu M.S., Udem S.A.;
RT   "Comparison of predicted amino acid sequences of measles virus strains in
RT   the Edmonston vaccine lineage.";
RL   J. Virol. 75:910-920(2001).
RN   [2]
RP   RNA EDITING.
RX   PubMed=2924348; DOI=10.1016/0092-8674(89)90679-x;
RA   Cattaneo R., Kaelin K., Baczko K., Billeter M.A.;
RT   "Measles virus editing provides an additional cysteine-rich protein.";
RL   Cell 56:759-764(1989).
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 (By similarity).
CC       {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9EMA9; Q96C10: DHX58; Xeno; NbExp=2; IntAct=EBI-6598728, EBI-744193;
CC       Q9EMA9; Q9BYX4: IFIH1; Xeno; NbExp=2; IntAct=EBI-6598728, EBI-6115771;
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC   -!- RNA EDITING: Modified_positions=231 {ECO:0000269|PubMed:2924348};
CC       Note=Partially edited. RNA editing at this position consists of an
CC       insertion of one guanine nucleotide. The sequence displayed here is the
CC       V protein, derived from the edited RNA. The unedited RNA gives rise to
CC       the P protein (AC P03422).;
CC   -!- SIMILARITY: Belongs to the paramyxoviruses V protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF266288; AAF85677.2; -; Genomic_RNA.
DR   PIR; A31490; A31490.
DR   PIR; S20830; S20830.
DR   SMR; Q9EMA9; -.
DR   IntAct; Q9EMA9; 2.
DR   Proteomes; UP000141942; 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:0039574; P:suppression by virus of host JAK-STAT cascade via inhibition of host TYK2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039563; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT1 activity; 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 STAT1 by virus;
KW   Inhibition of host STAT2 by virus; Inhibition of host TYK2 by virus;
KW   Interferon antiviral system evasion; Metal-binding; RNA editing;
KW   Viral immunoevasion; Zinc.
FT   CHAIN           1..299
FT                   /note="Non-structural protein V"
FT                   /id="PRO_0000142810"
FT   REGION          41..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        134..149
FT                   /note="Polar 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;  32146 MW;  8B545804E0CF25AD CRC64;
     MAEEQARHVK NGLECIRALK AEPIGSLAIE EAMAAWSEIS DNPGQERATC REEKAGSSGL
     SKPCLSAIGS TEGGAPRIRG QGPGESDDDA ETLGIPPRNL QASSTGLQCY YVYDHSGEAV
     KGIQDADSIM VQSGLDGDST LSGGDNESEN SDVDIGEPDT EGYAITDRGS APISMGFRAS
     DVETAEGGEI HELLRLQSRG NNFPKLGKTL NVPPPPDPGR ASTSETPIKK GHRREISLIW
     NGDRVFIDRW CNPMCSKVTL GTIRARCTCG ECPRVCEQCR TDTGVDTRIW YHNLPEIPE
 
 
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