PHOSP_WCBV
ID PHOSP_WCBV Reviewed; 297 AA.
AC Q5VKP1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 23-FEB-2022, entry version 65.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
DE AltName: Full=Protein M1;
GN Name=P;
OS West Caucasian bat virus (WCBV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=249584;
OH NCBI_TaxID=9433; Miniopterus schreibersii (Schreibers's long-fingered bat) (Vespertilio schreibersii).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15896400; DOI=10.1016/j.virusres.2005.03.008;
RA Kuzmin I.V., Hughes G.J., Botvinkin A.D., Orciari L.A., Rupprecht C.E.;
RT "Phylogenetic relationships of Irkut and West Caucasian bat viruses within
RT the Lyssavirus genus and suggested quantitative criteria based on the N
RT gene sequence for lyssavirus genotype definition.";
RL Virus Res. 111:28-43(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=18514350; DOI=10.1016/j.virusres.2008.04.021;
RA Kuzmin I.V., Wu X., Tordo N., Rupprecht C.E.;
RT "Complete genomes of Aravan, Khujand, Irkut and West Caucasian bat viruses,
RT with special attention to the polymerase gene and non-coding regions.";
RL Virus Res. 136:81-90(2008).
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 and PML (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Phosphoprotein]: Virion. Host cytoplasm
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform P2]: Host cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=P;
CC IsoId=Q5VKP1-1; Sequence=Displayed;
CC Name=P2;
CC IsoId=Q5VKP1-2; Sequence=VSP_026921;
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; EF614258; AAR03482.1; -; mRNA.
DR RefSeq; YP_009094269.1; NC_025377.1. [Q5VKP1-1]
DR SMR; Q5VKP1; -.
DR GeneID; 20964559; -.
DR KEGG; vg:20964559; -.
DR Proteomes; UP000095862; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; 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-virus interaction;
KW 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_0000295256"
FT REGION 57..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..176
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 208..211
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 155..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 207
FT /note="Phosphoserine; by host PKC"
FT /evidence="ECO:0000250"
FT MOD_RES 268
FT /note="Phosphoserine; by host PKC"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform P2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026921"
SQ SEQUENCE 297 AA; 33522 MW; E196A558A82A6E18 CRC64;
MSKSLIHPSD LRAGLADIEM ADETVDLVYK NLSEGQAHLQ GEPFDIKDLP EGVSKLQISD
NVRSDTSPNE YSDEDDEEGE DEYEEVYDPV SAFQDFLDET GSYLISKLKK GEKIKKTWSE
VSRVIYSYVM SNFPPRPPKP TTKDIAVQAD LKKPNEIQKI SEHKSKSEPS PREPVVEMHK
HATLENPEDD EGALESEIAH QVAESYSKKY KFPSKSSGIF LWNFEQLKMN LDDIVQVARG
VPGISQIVER GGKLPLRCML GYVGLETSKR FRSLVNQDKL CKLMQEDLNA YSVSSNN
