V_PI4HB
ID V_PI4HB Reviewed; 229 AA.
AC P21740;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Non-structural protein V;
GN Name=P/V;
OS Human parainfluenza 4b virus (strain 68-333) (HPIV-4b).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC Orthorubulavirus; Human orthorubulavirus 4.
OX NCBI_TaxID=11227;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
RX PubMed=2167560; DOI=10.1016/0042-6822(90)90413-l;
RA Kondo K., Bando H., Tsurudome M., Kawano M., Nishio M., Ito Y.;
RT "Sequence analysis of the phosphoprotein (P) genes of human parainfluenza
RT type 4A and 4B viruses and RNA editing at transcript of the P genes: the
RT number of G residues added is imprecise.";
RL Virology 178:321-326(1990).
CC -!- FUNCTION: Blocks host interferon signaling. {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=153 {ECO:0000269|PubMed:2167560};
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 P21738).;
CC -!- SIMILARITY: Belongs to the paramyxoviruses V protein family.
CC {ECO:0000305}.
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DR EMBL; M55976; AAA46807.1; -; Genomic_RNA.
DR PIR; D43685; D43685.
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: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 3: Inferred from homology;
KW Host-virus interaction; 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; Interferon antiviral system evasion;
KW Metal-binding; RNA editing; Viral immunoevasion; Zinc.
FT CHAIN 1..229
FT /note="Non-structural protein V"
FT /id="PRO_0000142818"
FT REGION 28..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178
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="1"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 215
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="2"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 229 AA; 25566 MW; DE1899053A17E40E CRC64;
MSFEISVEEI DELIETGNLN IDYALKELGA TSQPPPNRPL SQISKTEENN DETRTSKNSA
SAEAPAHASS PLRSHNEESE PGKQSSDGFS MISNRPQTGM LLMGSDTQSP SPSKTYQGLI
LDAKKRALNE PRRNQKTTNE HGNTNDTWIF KRGEYSHQER GLGYTESEIK NTIFIPRHRR
EHSISWVNGR TTISEWCNPC CAPVKSIASV EKCTCGRCPK ICELCIRDP