ID   PHOSP_LBV               Reviewed;         305 AA.
AC   O56773;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Phosphoprotein;
DE            Short=Protein P;
DE   AltName: Full=Protein M1;
GN   Name=P;
OS   Lagos bat virus (LBV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=38766;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Isolate Nigeria/V006/1988;
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).
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: [Phosphoprotein]: Homotrimer when phosphorylated. This trimer
CC       is stabilized by binding to the L protein. Binds soluble protein N, and
CC       ribonucleocapsid. Interacts with host STAT1, STAT2, DYNLL1, DYNLL2 and
CC       PML. {ECO:0000250}.
CC   -!- SUBUNIT: [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 P3]: Host nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=3;
CC       Name=P;
CC         IsoId=O56773-1; Sequence=Displayed;
CC       Name=P2;
CC         IsoId=O56773-2; Sequence=VSP_027562;
CC       Name=P3;
CC         IsoId=O56773-3; Sequence=VSP_027561;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF049114; AAC04584.1; -; mRNA.
DR   SMR; O56773; -.
DR   PRIDE; O56773; -.
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; Viral immunoevasion;
KW   Viral RNA replication; Virion.
FT   CHAIN           1..305
FT                   /note="Phosphoprotein"
FT                   /id="PRO_0000299097"
FT   REGION          139..195
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        139..177
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         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..52
FT                   /note="Missing (in isoform P3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_027561"
FT   VAR_SEQ         1..19
FT                   /note="Missing (in isoform P2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_027562"
SQ   SEQUENCE   305 AA;  34413 MW;  CAE2C000F95EE3DB CRC64;
     MSKGLIHPSA IRSGLVDLEM AEETVDLVHK NLADSQAHLQ GEPLNVDSLP EDMRKMRLTN
     APSEREIIEE DEEEYSSEDE YYLSQGQDPM VPFQNFLDEL GTQIVRRMKS GDGFFKIWSA
     ASEDIKGYVL STFMKPETQA TVSKPTQTDS LSVPRPSQGY TSVPRDKPSN SESQGGGVKP
     KKVQKSEWTR DTDEISDIEG EVAHQVAESF SKKYKFPSRS SGIFLWNFEQ LKMNLDDIVK
     TSMNVPGVDK IAEKGGKLPL RCILGFVSLD SSKRFRLLAD TDKVARLMQD DIHNYMTRIE
     EIDHN