V_HENDH
ID V_HENDH Reviewed; 457 AA.
AC O55777;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Non-structural protein V;
GN Name=P/V/C;
OS Hendra virus (isolate Horse/Autralia/Hendra/1994).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Henipavirus.
OX NCBI_TaxID=928303;
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9402; Pteropus alecto (Black flying fox).
OH NCBI_TaxID=9403; Pteropus poliocephalus (Grey-headed flying fox).
OH NCBI_TaxID=94117; Pteropus scapulatus (Little red flying fox).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9445051; DOI=10.1128/jvi.72.2.1482-1490.1998;
RA Wang L.-F., Michalski W.P., Yu M., Pritchard L.I., Crameri G., Shiell B.,
RA Eaton B.T.;
RT "A novel P/V/C gene in a new member of the Paramyxoviridae family, which
RT causes lethal infection in humans, horses, and other animals.";
RL J. Virol. 72:1482-1490(1998).
RN [2]
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 interferon signaling pathway by interacting with host
CC STAT1 and STAT2 and thereby inhibiting their phosphorylation and
CC subsequent nuclear translocation. Efficiently blocks the type II
CC interferon signaling pathway (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with host IFIH1/MDA5, DHX58/LGP2, STAT1 and STAT2.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=407; Note=Partially edited. RNA editing
CC at this position consists of an insertion of one or two guanine
CC nucleotides. The sequence displayed here is the V protein, derived from
CC the +1G edited RNA. The unedited RNA gives rise to the P protein (AC
CC O55778), the +2G edited RNA gives rise to the W protein (AC P0C1C6).;
CC -!- MISCELLANEOUS: The P/V/C gene has two overlapping open reading frames.
CC One encodes the P/V/W proteins and the other the C protein.
CC -!- SIMILARITY: Belongs to the paramyxoviruses V protein family.
CC {ECO:0000305}.
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DR EMBL; AF010304; AAC04241.1; -; mRNA.
DR EMBL; AF017149; AAC83189.1; -; Genomic_RNA.
DR PIR; T03449; T03449.
DR RefSeq; NP_047108.1; NC_001906.3.
DR SMR; O55777; -.
DR IntAct; O55777; 6.
DR GeneID; 1446469; -.
DR Proteomes; UP000008771; 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 InterPro; IPR035430; Paramyxo_PNT.
DR InterPro; IPR025909; Soyouz_module.
DR Pfam; PF14320; Paramyxo_PNT; 1.
DR Pfam; PF14313; Soyouz_module; 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 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; Phosphoprotein;
KW Reference proteome; RNA editing; Viral immunoevasion; Zinc.
FT CHAIN 1..457
FT /note="Non-structural protein V"
FT /id="PRO_0000236014"
FT REGION 26..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 453
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 257
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 350
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 457 AA; 50648 MW; 15C63B4FF638587D CRC64;
MDKLDLVNDG LDIIDFIQKN QKEIQKTYGR SSIQQPSTKD RTRAWEDFLQ STSGEHEQAE
GGMPKNDGGT EGRNVEDLSS VTSSDGTIGQ RVSNTRAWAE DPDDIQLDPM VTDVVYHDHG
GECTGHGPSS SPERGWSYHM SGTHDGNVRA VPDTKVLPNA PKTTVPEEVR EIDLIGLEDK
FASAGLNPAA VPFVPKNQST PTEEPPVIPE YYYGSGRRGD LSKSPPRGNV NLDSIKIYTS
DDEDENQLEY EDEFAKSSSE VVIDTTPEDN DSINQEEVVG DPSDQGLEHP FPLGKFPEKE
ETPDVRRKDS LMQDSCKRGG VPKRLPMLSE EFECSGSDDP IIQELEREGS HPGGSLRLRE
PPQSSGNSRN QPDRQLKTGD AASPGGVQRP GTPMPKSRIM PIKKGHRREV SICWDGRRAW
VEEWCNPVCS RITPQPRKQE CYCGECPTEC SQCCHEE
