V_MUMPE
ID V_MUMPE Reviewed; 224 AA.
AC P30927;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Non-structural protein V;
DE AltName: Full=Non-structural protein NS1;
GN Name=P/V;
OS Mumps virus (strain Enders) (MuV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Orthorubulavirus; Mumps orthorubulavirus.
OX NCBI_TaxID=11167;
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 IDENTIFICATION, 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 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 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 (By similarity). {ECO:0000250}.
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) (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P30927; Q96C10: DHX58; Xeno; NbExp=2; IntAct=EBI-6599165, EBI-744193;
CC P30927; Q9BYX4: IFIH1; Xeno; NbExp=2; IntAct=EBI-6599165, EBI-6115771;
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 P16072).;
CC -!- SIMILARITY: Belongs to the paramyxoviruses V protein family.
CC {ECO:0000305}.
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DR EMBL; D00351; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P30927; -.
DR IntAct; P30927; 2.
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; RNA editing;
KW Viral immunoevasion; Zinc.
FT CHAIN 1..224
FT /note="Non-structural protein V"
FT /id="PRO_0000142819"
FT REGION 54..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..72
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; 24184 MW; 6A90961E74341373 CRC64;
MDQFIKQDET GDLIETGMNV ANHFLSAPIQ GTNSLSKASI IPGVAPVLIG NPEQKNIQHP
TASHQGSKSK GRGSGVRSII VPPSEAGNGG TQIPEPLFAQ TGQGGIVTTV YQDPTIQPTG
SYRSVELTKI GKERMINRFV EKPRISTPVT EFKRGAGSGC SRPDNPRGGH RREWSLSWVQ
GEVRVFEWCN PICSPITAAA RFHSCKCGNC PAKCDQCERD YGPP
