V_MEASI
ID V_MEASI Reviewed; 299 AA.
AC P26036;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Non-structural protein V;
GN Name=P/V;
OS Measles virus (strain IP-3-Ca) (MeV) (Subacute sclerose panencephalitis
OS virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=11237;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1585658; DOI=10.1016/0042-6822(92)90552-z;
RA Schmid A., Spielhofer P., Cattaneo R., Baczko K., Ter Meulen V.,
RA Billeter M.A.;
RT "Subacute sclerosing panencephalitis is typically characterized by
RT alterations in the fusion protein cytoplasmic domain of the persisting
RT measles virus.";
RL Virology 188:910-915(1992).
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 -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=231 {ECO:0000250}; Note=Partially
CC edited. RNA editing at this position consists of an insertion of one
CC guanine nucleotide. The sequence displayed here is the V protein,
CC derived from the edited RNA. The unedited RNA gives rise to the P
CC protein (AC P26033) (By similarity). {ECO:0000250};
CC -!- SIMILARITY: Belongs to the paramyxoviruses V protein family.
CC {ECO:0000305}.
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DR EMBL; X16566; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR SMR; P26036; -.
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 3: Inferred from homology;
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; RNA editing;
KW Viral immunoevasion; Zinc.
FT CHAIN 1..299
FT /note="Non-structural protein V"
FT /id="PRO_0000142811"
FT REGION 40..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..230
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; 32057 MW; 7B82976C5709D721 CRC64;
MAEEQARHVK NGLECIRALK AEPIGSLAIG EAMAAWSEIS DNPGQEQATC KEEEAGASGL
SKPCLSAIGS TEGGAPRIRG QGSGESDDDT ETLGFPSRNL QASSTGLQCY YVYDHSGEAV
KGIQDADSIM VQSGLDGDST LSGGDNESEN SDVDIGEPDT EGYAITDRGP APISMGFRAS
DVETAEGGEI HELLRLQSRG NNFPKLGKTL NVPPPPDPGR ASTSETPIKK GHRREISLIW
DGDRVFIDRW CNPMCSKVTL GTIRARCTCG ECPRVCEQCR TDTGVDTRIW YHNLPEIPE
