PHOSP_EBLV2
ID PHOSP_EBLV2 Reviewed; 297 AA.
AC A4UHQ4; O56780;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
DE AltName: Full=Protein M1;
GN Name=P;
OS European bat lyssavirus 2 (strain Human/Scotland/RV1333/2002) (EBLV2).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=453116;
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Isolate Switzerland/V286/1992;
RX PubMed=12127791; DOI=10.1006/viro.2002.1492;
RA Nadin-Davis S.A., Abdel-Malik M., Armstrong J., Wandeler A.I.;
RT "Lyssavirus P gene characterisation provides insights into the phylogeny of
RT the genus and identifies structural similarities and diversity within the
RT encoded phosphoprotein.";
RL Virology 298:286-305(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=17374776; DOI=10.1099/vir.0.82692-0;
RA Marston D.A., McElhinney L.M., Johnson N., Muller T., Conzelmann K.K.,
RA Tordo N., Fooks A.R.;
RT "Comparative analysis of the full genome sequence of European bat
RT lyssavirus type 1 and type 2 with other lyssaviruses and evidence for a
RT conserved transcription termination and polyadenylation motif in the G-L 3'
RT non-translated region.";
RL J. Gen. Virol. 88:1302-1314(2007).
RN [3]
RP SEQUENCE REVISION.
RA Marston D.A., McElhinney L.M., Johnson N., Mueller T., Conzelmann K.K.,
RA Tordo N., Fooks A.R.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Non catalytic polymerase cofactor and regulatory protein that
CC plays a role in viral transcription and replication. Stabilizes the RNA
CC polymerase L to the N-RNA template and binds the soluble protein N,
CC preventing it from encapsidating non-genomic RNA. Also inhibits host
CC IFN-alpha and IFN-beta signaling by binding and retaining
CC phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding
CC of STAT1 in the nucleus (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer when phosphorylated. This trimer is stabilized by
CC binding to the L protein. Binds soluble protein N, and
CC ribonucleocapsid. Interacts with host STAT1, STAT2, DYNLL1, DYNLL2 and
CC PML. {ECO:0000305}.
CC -!- SUBUNIT: [Isoform P3]: Binds host PML (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Phosphoprotein]: Virion. Host cytoplasm
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform P2]: Host cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform P3]: Host nucleus {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform P5]: Host nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=4;
CC Name=P;
CC IsoId=A4UHQ4-1; Sequence=Displayed;
CC Name=P2;
CC IsoId=A4UHQ4-2; Sequence=VSP_027560;
CC Name=P3;
CC IsoId=A4UHQ4-3; Sequence=VSP_027559;
CC Name=P5;
CC IsoId=A4UHQ4-4; Sequence=VSP_027558;
CC -!- PTM: Phosphorylated by host PKC and by an unknown kinase.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lyssavirus protein P family. {ECO:0000305}.
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DR EMBL; AF049121; AAC04591.1; -; mRNA.
DR EMBL; EF157977; ABO65249.2; -; Genomic_RNA.
DR RefSeq; YP_001285394.2; NC_009528.2.
DR SMR; A4UHQ4; -.
DR GeneID; 5219914; -.
DR KEGG; vg:5219914; -.
DR Proteomes; UP000007206; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
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:0019083; P:viral transcription; IEA:InterPro.
DR Gene3D; 1.20.120.820; -; 1.
DR InterPro; IPR004259; PP_M1.
DR InterPro; IPR037199; PP_M1_C.
DR Pfam; PF03012; PP_M1; 1.
DR SUPFAM; SSF118173; SSF118173; 1.
PE 2: Evidence at transcript level;
KW Alternative initiation; Chaperone; Host cytoplasm; Host nucleus;
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 STAT1 by virus; Inhibition of host STAT2 by virus;
KW Interferon antiviral system evasion; Phosphoprotein; Reference proteome;
KW Viral immunoevasion; Viral RNA replication; Virion.
FT CHAIN 1..297
FT /note="Phosphoprotein"
FT /id="PRO_0000299096"
FT REGION 140..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 49..58
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT MOTIF 211..214
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 151..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 210
FT /note="Phosphoserine; by host PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 271
FT /note="Phosphoserine; by host PKC"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform P5)"
FT /evidence="ECO:0000305"
FT /id="VSP_027558"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform P3)"
FT /evidence="ECO:0000305"
FT /id="VSP_027559"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform P2)"
FT /evidence="ECO:0000305"
FT /id="VSP_027560"
FT VARIANT 153
FT /note="F -> S (in strain: Isolate Switzerland/V286/1992)"
FT VARIANT 239
FT /note="K -> R (in strain: Isolate Switzerland/V286/1992)"
FT VARIANT 253
FT /note="D -> I (in strain: Isolate Switzerland/V286/1992)"
SQ SEQUENCE 297 AA; 33322 MW; A8859B461A175DB8 CRC64;
MSKIFVNPSA IRAGLADLEM AEETVDLVNK NIEDNQAHLQ GEPIEVDALP EDMSKLQISE
RRPAQFTDNT GGKEEGSDED FYMAESEDPY IPLQSYLEGV GIQLVRQMKT GERFFKIWSQ
AVEEIISYVT VHFPMPLGKS TEDKSTQTPE EKFKPSPQQA VTKKESQSSK IKTISQESSG
PPALEWSTTN DEENASVEAE IAHQIAESFS KKYKFPSRSS GIFLFNFEQL KMNLDDIVKE
AKKIPGVVRL AQDGFRLPLR CILGGVGSVN SKKFQLLVNS DKLGKIMQDD LNRYLAY
