ID   PHOSP_ABLVH             Reviewed;         297 AA.
AC   Q8JTH2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Phosphoprotein;
DE            Short=Protein P;
DE   AltName: Full=Protein M1;
GN   Name=P;
OS   Australian bat lyssavirus (isolate Human/AUS/1998) (ABLV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=446562;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9402; Pteropus alecto (Black flying fox).
OH   NCBI_TaxID=328804; Pteropus conspicillatus (Spectacled flying fox).
OH   NCBI_TaxID=9403; Pteropus poliocephalus (Grey-headed flying fox).
OH   NCBI_TaxID=94117; Pteropus scapulatus (Little red flying fox).
OH   NCBI_TaxID=446909; Saccolaimus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12083841; DOI=10.1006/viro.2002.1417;
RA   Warrilow D., Smith I.L., Harrower B., Smith G.A.;
RT   "Sequence analysis of an isolate from a fatal human infection of Australian
RT   bat lyssavirus.";
RL   Virology 297:109-119(2002).
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 P5]: Host nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=3;
CC       Name=P;
CC         IsoId=Q8JTH2-1; Sequence=Displayed;
CC       Name=P2;
CC         IsoId=Q8JTH2-2; Sequence=VSP_026886;
CC       Name=P5;
CC         IsoId=Q8JTH2-3; Sequence=VSP_026885;
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; AF418014; AAN05307.1; -; Genomic_RNA.
DR   SMR; Q8JTH2; -.
DR   Proteomes; UP000006884; 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; Reference proteome;
KW   Viral immunoevasion; Viral RNA replication; Virion.
FT   CHAIN           1..297
FT                   /note="Phosphoprotein"
FT                   /id="PRO_0000295245"
FT   REGION          136..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        136..174
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         63
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_026885"
FT   VAR_SEQ         1..19
FT                   /note="Missing (in isoform P2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_026886"
SQ   SEQUENCE   297 AA;  33396 MW;  99DB689049F54FCC CRC64;
     MSKIFVNPSA IRAGMADLEM AEETVDLINR NIEDNQAHLQ GEPIEVDSLP EDIKKLDISE
     GRSKSLVDNP QDVECRMSED FQMDEVEDPN IQFQSYLDNI GIQIVRKMRT GERFFKIWSQ
     TVEEIISYVG VNFPSQSGKT TENKSTQTTP KKVKTEPSST PAKRSDQLSK TEMAAKTASG
     PPALEWSTTN DEDDVSVEAE IAHQIAESFS KKYKFPSRSS GIFLYNFEQL KMNLDDIVKE
     AKSVPGVTSL ARDGLRLPLR CILGWVGSSH SKKFQLLVGS EKLNKIMQDD LNRYMSC