V_PI2HT
ID V_PI2HT Reviewed; 225 AA.
AC P23057;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Non-structural protein V;
GN Name=P/V;
OS Human parainfluenza 2 virus (strain Toshiba) (HPIV-2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Orthorubulavirus; Human parainfluenza 2 virus.
OX NCBI_TaxID=11214;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
RX PubMed=2162103; DOI=10.1016/0042-6822(90)90465-4;
RA Ohgimoto S., Bando H., Kawano M., Okamoto K., Kondo K., Tsurudome M.,
RA Nishio M., Ito Y.;
RT "Sequence analysis of P gene of human parainfluenza type 2 virus: P and
RT cysteine-rich proteins are translated by two mRNAs that differ by two
RT nontemplated G residues.";
RL Virology 177:116-123(1990).
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 Efficiently blocks type I IFN signaling following infection by
CC targeting host STAT2 for proteasomal degradation (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with host IFIH1/MDA5 and DHX58/LGP2. Forms with host
CC DDB1, CUL4A, STAT1 and STAT2 the HPIV2 virus V-dependent complex (VDC);
CC this complex targets host STAT2 to proteasomal degradation (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=164 {ECO:0000269|PubMed:2162103};
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 P23056).;
CC -!- SIMILARITY: Belongs to the paramyxoviruses V protein family.
CC {ECO:0000305}.
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DR EMBL; M37751; AAA46803.1; -; Genomic_RNA.
DR EMBL; X57559; CAA40784.1; -; Genomic_DNA.
DR PIR; A35313; MNNZVT.
DR SMR; P23057; -.
DR IntAct; P23057; 12.
DR Proteomes; UP000000472; 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: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; IPR025909; Soyouz_module.
DR Pfam; PF14313; Soyouz_module; 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 MDA5 by virus; Inhibition of host RLR pathway by virus;
KW Inhibition of host STAT2 by virus; Interferon antiviral system evasion;
KW Metal-binding; Reference proteome; RNA editing; Viral immunoevasion; Zinc.
FT CHAIN 1..225
FT /note="Non-structural protein V"
FT /id="PRO_0000142816"
FT REGION 145..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174
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="1"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 211
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="2"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 225 AA; 24151 MW; 3F9D703794CF8DDD CRC64;
MAEEPTYTTE QVDELIHAGL GTVDFFLSRP IDAQSSLGKG SIPPGVTAVL TSAAETKSKP
VAAGPVKPRR KKVISNTTPY TIADNIPPEK LPINTPIPNP LLPLARPHGK MTDIDIVTGN
ITEGSYKGVE LAKLGKQTLL TRFTSNEPVS SAGSAQDPNF KRGGANRERA RGNHRREWSI
AWVGDQVKVF EWCNPRCAPV TASARKFTCT CGSCPSICGE CEGDH
