PHOSP_KHUV
ID PHOSP_KHUV Reviewed; 297 AA.
AC Q6X1D3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-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 Khujand virus (KHUV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=237716;
OH NCBI_TaxID=109479; Myotis mystacinus (Whiskered bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=14602198; DOI=10.1016/s0168-1702(03)00217-x;
RA Kuzmin I.V., Orciari L.A., Arai Y.T., Smith J.S., Hanlon C.A., Kameoka Y.,
RA Rupprecht C.E.;
RT "Bat lyssaviruses (Aravan and Khujand) from Central Asia: phylogenetic
RT relationships according to N, P and G gene sequences.";
RL Virus Res. 97:65-79(2003).
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 -!- 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=Q6X1D3-1; Sequence=Displayed;
CC Name=P2;
CC IsoId=Q6X1D3-2; Sequence=VSP_026895;
CC Name=P3;
CC IsoId=Q6X1D3-3; Sequence=VSP_026894;
CC Name=P5;
CC IsoId=Q6X1D3-4; Sequence=VSP_026893;
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; EF614261; AAP86777.1; -; Genomic_RNA.
DR RefSeq; YP_009094328.1; NC_025385.1. [Q6X1D3-1]
DR SMR; Q6X1D3; -.
DR GeneID; 21011768; -.
DR KEGG; vg:21011768; -.
DR Proteomes; UP000136780; 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 3: Inferred from homology;
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; Viral immunoevasion;
KW Viral RNA replication; Virion.
FT CHAIN 1..297
FT /note="Phosphoprotein"
FT /id="PRO_0000295248"
FT REGION 137..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 137..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250"
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_026893"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform P3)"
FT /evidence="ECO:0000305"
FT /id="VSP_026894"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform P2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026895"
SQ SEQUENCE 297 AA; 33540 MW; 3174CD410477D453 CRC64;
MSKIFVNPSA IRAGLADLEM AEETVDLINR NVEDNQAHLQ GEPIEVEALP EDMRRLHISE
QKHSQLSDSA CGKEEGSDDD FYMADSEDPY VPMQSYLDNV GIQIVKKMKT GERFFKIWSQ
AVEEIISYVT VNFPLPSGKS TDDKSTQTVS ERSRQNPQPS SVKKEDQLSK TKVVSQEASG
PPALEWSATN DEDDASVEAE IAHQIAESFS KKYKFPSRSS GIFLYNFEQL KTNLDDIVRE
AKRIPGVMRL AQDGLRLPLR CILGWVASTH SKRFQILVDS DKLSKIMQDD INRYLAY
