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V_MUMPM
ID   V_MUMPM                 Reviewed;         224 AA.
AC   P30928; Q783W0;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Non-structural protein V;
DE   AltName: Full=Non-structural protein NS1;
GN   Name=P/V;
OS   Mumps virus (strain Miyahara vaccine) (MuV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC   Orthorubulavirus; Mumps orthorubulavirus.
OX   NCBI_TaxID=11171;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3404121; DOI=10.1099/0022-1317-69-8-2043;
RA   Takeuchi K., Hishiyama M., Yamada A., Sugiura A.;
RT   "Molecular cloning and sequence analysis of the mumps virus gene encoding
RT   the P protein: mumps virus P gene is monocistronic.";
RL   J. Gen. Virol. 69:2043-2049(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
RX   PubMed=2389552; DOI=10.1016/0042-6822(90)90400-l;
RA   Takeuchi K., Tanabayashi K., Hishiyama M., Yamada Y.K., Yamada A.,
RA   Sugiura A.;
RT   "Detection and characterization of mumps virus V protein.";
RL   Virology 178:247-253(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1585659; DOI=10.1016/0042-6822(92)90555-4;
RA   Okazaki K., Tanabayashi K., Takeuchi K., Hishiyama M., Okazaki K.,
RA   Yamada A.;
RT   "Molecular cloning and sequence analysis of the mumps virus gene encoding
RT   the L protein and the trailer sequence.";
RL   Virology 188:926-930(1992).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH HOST STAT1; STAT2; STAT3; DDB1 AND CUL4A.
RC   STRAIN=Enders;
RX   PubMed=12743296; DOI=10.1128/jvi.77.11.6385-6393.2003;
RA   Ulane C.M., Rodriguez J.J., Parisien J.P., Horvath C.M.;
RT   "STAT3 ubiquitylation and degradation by mumps virus suppress cytokine and
RT   oncogene signaling.";
RL   J. Virol. 77:6385-6393(2003).
RN   [5]
RP   FUNCTION.
RC   STRAIN=RW;
RX   PubMed=15767445; DOI=10.1128/jvi.79.7.4451-4459.2005;
RA   Kubota T., Yokosawa N., Yokota S., Fujii N., Tashiro M., Kato A.;
RT   "Mumps virus V protein antagonizes interferon without the complete
RT   degradation of STAT1.";
RL   J. Virol. 79:4451-4459(2005).
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 and II interferon signaling pathways by interacting
CC       with host STAT1, STAT2 and STAT3, and mediating their ubiquitination
CC       and subsequent proteasomal degradation. {ECO:0000269|PubMed:12743296,
CC       ECO:0000269|PubMed:15767445}.
CC   -!- SUBUNIT: Interacts with host IFIH1/MDA5 and DHX58/LGP2. Forms with host
CC       DDB1, CUL4A, STAT1, STAT2 and STAT3 the mumps virus V-dependent complex
CC       (VDC). {ECO:0000269|PubMed:12743296}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC   -!- RNA EDITING: Modified_positions=155 {ECO:0000269|PubMed:2389552};
CC       Note=Partially edited. RNA editing at this position consists of an
CC       insertion of two guanine nucleotides. The sequence displayed here is
CC       the V protein, derived from the unedited RNA. The edited RNA gives rise
CC       to the P protein (AC P16595).;
CC   -!- SIMILARITY: Belongs to the paramyxoviruses V protein family.
CC       {ECO:0000305}.
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DR   EMBL; D00352; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   EMBL; AB040874; BAA94386.1; -; Genomic_RNA.
DR   PIR; A46343; A46343.
DR   SMR; P30928; -.
DR   Proteomes; UP000002331; 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: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   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 interferon signaling pathway by virus;
KW   Inhibition of host MDA5 by virus; Inhibition of host RLR pathway by virus;
KW   Inhibition of host STAT1 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..224
FT                   /note="Non-structural protein V"
FT                   /id="PRO_0000142820"
FT   REGION          55..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          145..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         170
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         193
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         210
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         217
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   224 AA;  24133 MW;  C680C844616D6EA3 CRC64;
     MDQFIKQDET GDLIETGMNV ANHFLSAPIQ GTNSLSKATI IPGVAPVLIG NPEQKNIQYP
     TTSHQGSKSK GRGSGARPII VSSSEGGTGG TQVPEPLFAQ TGQGGIVTTV YQDPTIQPTG
     SYRSVELAKI GKERMINRFV EKPRTSTPVT EFKRGAGSGC SRPDNPRGGH RREWSLSWVQ
     GEVRVFEWCN PICSPITAAA RFHSCKCGNC PAKCDQCERD YGPP
 
 
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