PHOSP_ARAV
ID PHOSP_ARAV Reviewed; 297 AA.
AC Q6X1D7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
DE AltName: Full=Protein M1;
GN Name=P;
OS Aravan virus (ARAV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=211977;
OH NCBI_TaxID=109482; Myotis blythii (Lesser mouse-eared 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 P4]: 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=Q6X1D7-1; Sequence=Displayed;
CC Name=P2;
CC IsoId=Q6X1D7-2; Sequence=VSP_026889;
CC Name=P4;
CC IsoId=Q6X1D7-3; Sequence=VSP_026888;
CC Name=P5;
CC IsoId=Q6X1D7-4; Sequence=VSP_026887;
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; EF614259; AAP86773.1; -; Genomic_RNA.
DR RefSeq; YP_007641393.1; NC_020808.1. [Q6X1D7-1]
DR SMR; Q6X1D7; -.
DR GeneID; 14857926; -.
DR KEGG; vg:14857926; -.
DR Proteomes; UP000007445; 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_0000295246"
FT REGION 138..172
FT /note="DYNLL1 and DYNLL2 binding"
FT /evidence="ECO:0000250"
FT REGION 140..189
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 141..183
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_026887"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform P4)"
FT /evidence="ECO:0000305"
FT /id="VSP_026888"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform P2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026889"
SQ SEQUENCE 297 AA; 33193 MW; 6178284D4DE65B18 CRC64;
MSKIFVNPSA IRAGLADLEM AEETVDLVNK NVEESQAHLQ AEPIEVDALP EDMKRLQISE
PKPCQLPDGT CMKEEGGDED FYMAESGDPY IPLQSYLDTM GIQIVRKMKT GERFFKIWSQ
SVEEIISYVA VNFPVPPGKS LADKSTQTSV EKSKPASQPT QPKKEDQLSK VNIDSQESSG
PPALDWAATN DDDDASVEAE IAHQIAESFS KKYKFPSRSS GIFLYNFEQL KMNLDDIVRE
AKGIPGVTRR AGDGVRLPLR CILGWVASTH SRRFQLLVNS DKLNKVMQDD INRYLAY
