V_RINDR
ID V_RINDR Reviewed; 299 AA.
AC Q03340;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Non-structural protein V;
GN Name=P/V;
OS Rinderpest virus (strain RBOK) (RDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=36409;
OH NCBI_TaxID=9915; Bos indicus (Zebu).
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=89462; Bubalus bubalis (Domestic water buffalo).
OH NCBI_TaxID=9925; Capra hircus (Goat).
OH NCBI_TaxID=9933; Gazella (gazelles).
OH NCBI_TaxID=9894; Giraffa camelopardalis (Giraffe).
OH NCBI_TaxID=9832; Hippopotamus.
OH NCBI_TaxID=9940; Ovis aries (Sheep).
OH NCBI_TaxID=9821; Suidae (pigs).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
RX PubMed=8429304; DOI=10.1099/0022-1317-74-2-299;
RA Baron M.D., Shaila M.S., Barrett T.;
RT "Cloning and sequence analysis of the phosphoprotein gene of rinderpest
RT virus.";
RL J. Gen. Virol. 74:299-304(1993).
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 (By similarity). {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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=231 {ECO:0000269|PubMed:8429304};
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 Q03335).;
CC -!- MISCELLANEOUS: Highly virulent strain of Rinderpest virus can blocks
CC the phosphorylation of host JAK1 kinase, thereby blocking the type II
CC interferon signaling as well.
CC -!- SIMILARITY: Belongs to the paramyxoviruses V protein family.
CC {ECO:0000305}.
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DR EMBL; X68311; CAA48390.2; -; Genomic_RNA.
DR PIR; JQ1930; JQ1930.
DR SMR; Q03340; -.
DR IntAct; Q03340; 4.
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:0039574; P:suppression by virus of host JAK-STAT cascade via inhibition of host TYK2 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; 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 MDA5 by virus; Inhibition of host RLR pathway by virus;
KW Inhibition of host TYK2 by virus; Interferon antiviral system evasion;
KW Metal-binding; RNA editing; Viral immunoevasion; Zinc.
FT CHAIN 1..299
FT /note="Non-structural protein V"
FT /id="PRO_0000142824"
FT REGION 56..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..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; 32674 MW; 0B58C872C5B9705E CRC64;
MAEEQAYHVN KGLECIKALR ARPLDPLVVE EALAAWVETS EGQTLDRMSS DEAEADHQDI
SKPCFPAAGP GKSSMSRCHD QGLRGSNSCD EELGAFIGDS SMHSTEVQHY HVYDHSGEKV
EGVEDADSIL VQSGADDGVE VWGGDEESEN SDVDSGEPDP EGSAPADWGS SPISPATRAS
DVETVEGDEI QKLLEDQSRI RKMTKAGKTL VVPPIPSQER PTASEKPIKK GHRREIDLIW
NDGRVFIDRW CNPTCSKVTV GTVRAKCICG ECPRVCEQCI TDSGIENRIW YHNLADIPE
