PHOSP_ABLVB
ID PHOSP_ABLVB Reviewed; 297 AA.
AC Q9QSP3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 23-FEB-2022, entry version 70.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
DE AltName: Full=Protein M1;
GN Name=P;
OS Australian bat lyssavirus (isolate Bat/AUS/1996) (ABLV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=446561;
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=12367747; DOI=10.1016/s0168-1702(02)00056-4;
RA Gould A.R., Kattenbelt J.A., Gumley S.G., Lunt R.A.;
RT "Characterisation of an Australian bat lyssavirus variant isolated from an
RT insectivorous bat.";
RL Virus Res. 89:1-28(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=Q9QSP3-1; Sequence=Displayed;
CC Name=P2;
CC IsoId=Q9QSP3-2; Sequence=VSP_026884;
CC Name=P5;
CC IsoId=Q9QSP3-3; Sequence=VSP_026883;
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; AF081020; AAD47897.1; -; Genomic_RNA.
DR RefSeq; NP_478340.1; NC_003243.1.
DR SMR; Q9QSP3; -.
DR GeneID; 926731; -.
DR KEGG; vg:926731; -.
DR Proteomes; UP000006934; 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_0000295244"
FT REGION 131..187
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 133..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..185
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_026883"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform P2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026884"
SQ SEQUENCE 297 AA; 33359 MW; B4D534CA435D4B44 CRC64;
MSKIFVNPSA IRAGMADLEM AEETVDLINR NIEDNQAHLQ GEPIEVDSLP EEIGKLNINE
AKPQSFENNP IDIDGRMNED FQMKEVEDPS IQFQSYLDNI GIQIVRKMKT GERFFKIWSQ
TVEEIISYVG ANFPNPSGKT TESKSTQTTP KKVKPEPPSA PTEKPEQLSR TSMAPETTSG
PLALDWSATN DDDDVSVEAE IAHQIAESFS KKYKFPSRSS GIFLYNFEQL KMNLDDIVKE
ARGVPGIIRL AKEGLRLPLR CILGWVASSH SKKFQLLVGS EKLSKIMQDD LNRYMSC
