V_MEASY
ID V_MEASY Reviewed; 299 AA.
AC P60168;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Non-structural protein V;
GN Name=P/V;
OS Measles virus (strain Yamagata-1) (MeV) (Subacute sclerose panencephalitis
OS virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=11239;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RX PubMed=1536889; DOI=10.1016/0167-4781(92)90515-2;
RA Komase K., Haga T., Yoshikawa Y., Yamanouchi K.;
RT "Complete nucleotide sequence of the phosphoprotein of the Yamagata-1
RT strain of a defective subacute sclerosing panencephalitis (SSPE) virus.";
RL Biochim. Biophys. Acta 1129:342-344(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:0000269|PubMed:1536889};
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 Q00793).;
CC -!- SIMILARITY: Belongs to the paramyxoviruses V protein family.
CC {ECO:0000305}.
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DR EMBL; D10635; -; NOT_ANNOTATED_CDS; mRNA.
DR SMR; P60168; -.
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 2: Evidence at transcript 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; RNA editing;
KW Viral immunoevasion; Zinc.
FT CHAIN 1..299
FT /note="Non-structural protein V"
FT /id="PRO_0000142812"
FT REGION 40..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..163
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; 32132 MW; BB3913613CB6BD3A CRC64;
MAEEQARHVK NGLECIRALK AEPIGSLAIG EAMAAWSEIS DNPGQERATY KEEKAGGSGL
SKPCLSAIGS TEGGAPRIRG QGSGESDDDT ETLGIPSRNL QASSTGLQCH YVYDHSGEAV
KGIQDADSIM VQSGLDGDST LSEGDNESEN SDVDIGEPDT EGYAITDRGS APISMGFRAS
DVETAEGGEI HELLRLQSRG NNFPKLGKTL NVPPPPDPGR ASTSETPIKK GHRREISLIW
DGDRVFIDRW CNPMCSKVTL GTIRARCTCG ECPRVCEQCR TDTGVDTRIW YHNLPEIPE
