PHOSP_EBLV1
ID PHOSP_EBLV1 Reviewed; 298 AA.
AC A4UHP9; O56772; O56776;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 23-FEB-2022, entry version 58.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
DE AltName: Full=Protein M1;
GN Name=P;
OS European bat lyssavirus 1 (strain Bat/Germany/RV9/1968) (EBLV1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=453115;
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Isolate Bat/Denmark/V002/1986, and Isolate Bat/Holland/V023/1988;
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 [MRNA].
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).
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. 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 P5]: Host nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=P;
CC IsoId=A4UHP9-1; Sequence=Displayed;
CC Name=P2;
CC IsoId=A4UHP9-2; Sequence=VSP_027557;
CC Name=P5;
CC IsoId=A4UHP9-3; Sequence=VSP_027556;
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; AF049117; AAC04587.1; -; mRNA.
DR EMBL; AF049113; AAC04583.1; -; mRNA.
DR EMBL; EF157976; ABO65244.1; -; Genomic_RNA.
DR RefSeq; YP_001285389.1; NC_009527.1.
DR SMR; A4UHP9; -.
DR GeneID; 5219910; -.
DR KEGG; vg:5219910; -.
DR Proteomes; UP000008926; 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..298
FT /note="Phosphoprotein"
FT /id="PRO_0000299095"
FT REGION 61..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..192
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 212..215
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 151..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 163
FT /note="Phosphoserine; by host PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 211
FT /note="Phosphoserine; by host PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 272
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_027556"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform P2)"
FT /evidence="ECO:0000305"
FT /id="VSP_027557"
FT VARIANT 66
FT /note="Q -> R (in strain: Isolate Bat/Denmark/V002/1986 and
FT Isolate Bat/Germany/RV9/1968)"
FT VARIANT 147
FT /note="R -> Q (in strain: Isolate Bat/Denmark/V002/1986 and
FT Isolate Bat/Germany/RV9/1968)"
FT VARIANT 157
FT /note="A -> V (in strain: Isolate Bat/Denmark/V002/1986 and
FT Isolate Bat/Germany/RV9/1968)"
FT VARIANT 163
FT /note="S -> N (in strain: Isolate Bat/Denmark/V002/1986 and
FT Isolate Bat/Germany/RV9/1968)"
FT VARIANT 179
FT /note="S -> L (in strain: Isolate Bat/Denmark/V002/1986)"
FT VARIANT 248
FT /note="V -> E (in strain: Isolate Bat/Denmark/V002/1986)"
SQ SEQUENCE 298 AA; 33273 MW; 28A9A3FD69EFD4A6 CRC64;
MSKIFVNPSA LRSGLADLEM AEETVDLVNK NMEDSQAHLQ GIPIDVETLP EDIKRLRIAD
YKQGQQEEDA SRQEEGEDED FYMTESENSY VPLQSYLDAV GMQIVRKMKT GDGFFKIWAQ
AVEDIVSYVA TNFPAPVNKL QADKSTRTTL EKVKQAASSS APSKREGPSS NMNLDSQESS
GPPGLDWAAS NDEDDGSIEA EIAHQIAESF SKKYKFPSRS SGIFLWNFEQ LKMNLDDIVR
EVKGIPGVTR MARDGMKLPL RCMLGSVASN HSKRFQILVN SAKLGKLMQD DLNRYLAY
