V_PHODV
ID V_PHODV Reviewed; 299 AA.
AC P35941;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Non-structural protein V;
GN Name=P/V;
OS Phocine distemper virus (PDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=11240;
OH NCBI_TaxID=9709; Phocidae (true seals).
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Ulster/88;
RX PubMed=1535099; DOI=10.1099/0022-1317-73-6-1587;
RA Curran M.D., Rima B.K.;
RT "The genes encoding the phospho- and matrix proteins of phocine distemper
RT virus.";
RL J. Gen. Virol. 73:1587-1591(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE, AND RNA EDITING.
RC STRAIN=2558/Hannover-88;
RA Barrett T., Goatley L.G., Haas L.;
RL Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE, AND RNA EDITING.
RC STRAIN=Isolate DK88-4A;
RX PubMed=1634877; DOI=10.1099/0022-1317-73-4-885;
RA Blixenkrone-Moeller M., Sharma B., Varsanyi T., Hu A., Norrby E.,
RA Koevamees J.;
RT "Sequence analysis of the genes encoding the nucleocapsid protein and
RT phosphoprotein (P) of phocid distemper virus, and editing of the P gene
RT transcript.";
RL J. Gen. Virol. 73:885-893(1992).
CC -!- FUNCTION: Blocks host interferon signaling. {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=231 {ECO:0000269|PubMed:1634877,
CC ECO:0000269|Ref.2}; Note=Partially edited. RNA editing at this position
CC consists of an insertion of one guanine nucleotide. The sequence
CC displayed here is the V protein, derived from the edited RNA. The
CC unedited RNA gives rise to the P protein (AC P35939).;
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DR EMBL; D10371; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; X65512; CAA46485.1; -; mRNA.
DR EMBL; X75960; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR PIR; JQ1565; JQ1565.
DR PIR; JQ1610; JQ1610.
DR RefSeq; YP_009177599.1; NC_028249.1.
DR SMR; P35941; -.
DR PRIDE; P35941; -.
DR GeneID; 26123433; -.
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; 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-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; 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_0000142814"
FT REGION 30..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..101
FT /note="Basic and 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"
FT CONFLICT 192
FT /note="A -> T (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="A -> V (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 33502 MW; F11227EECD97F0E1 CRC64;
MAEEQAYHVS KGLECIKALR ENPPNMEEIQ EVSNIRDQTY KSSKESGTTG VQEEEITQNI
DESHTPTKRS NSVSDVLQED QRGREDNTAP VEAKDRIEED TQTGPAVRRY YVYDHCGEKV
KGIEDADSLM VPAGPPSNRG FEGREGSLDD SIEDSSEDYS EGNASSNWGY TFGLNPDRAA
DVSMLMEEEL TALLGTGHNA GGQKRDGRTL QFPNSPEGSI GNQACEPIKK GHRREVSLTW
NDDRCWIDKW CNPICTQVNW GVIRAKCICG ECPPVCDDCK DDPEMQNRIW YETPTRETK
