PHOSP_DUVV
ID PHOSP_DUVV Reviewed; 298 AA.
AC O56774;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
DE AltName: Full=Protein M1;
GN Name=P;
OS Duvenhage virus (DUVV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=38767;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Isolate Human/South Africa/V008/1988;
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: 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, DYNLL1, DYNLL2 and
CC PML. 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 P4]: Host nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=P;
CC IsoId=O56774-1; Sequence=Displayed;
CC Name=P2;
CC IsoId=O56774-2; Sequence=VSP_027555;
CC Name=P4;
CC IsoId=O56774-3; Sequence=VSP_027554;
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; AF049115; AAC04585.1; -; mRNA.
DR RefSeq; YP_007641403.1; NC_020810.1. [O56774-1]
DR PDB; 7C21; X-ray; 1.95 A; A=187-298.
DR PDBsum; 7C21; -.
DR SMR; O56774; -.
DR PRIDE; O56774; -.
DR GeneID; 14857938; -.
DR KEGG; vg:14857938; -.
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 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Chaperone; Host cytoplasm;
KW Host nucleus; Host-virus interaction;
KW 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..298
FT /note="Phosphoprotein"
FT /id="PRO_0000299094"
FT REGION 148..184
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 148..177
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 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..68
FT /note="Missing (in isoform P4)"
FT /evidence="ECO:0000305"
FT /id="VSP_027554"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform P2)"
FT /evidence="ECO:0000305"
FT /id="VSP_027555"
FT HELIX 194..208
FT /evidence="ECO:0007829|PDB:7C21"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:7C21"
FT STRAND 214..226
FT /evidence="ECO:0007829|PDB:7C21"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:7C21"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:7C21"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:7C21"
FT HELIX 260..271
FT /evidence="ECO:0007829|PDB:7C21"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:7C21"
FT HELIX 281..295
FT /evidence="ECO:0007829|PDB:7C21"
SQ SEQUENCE 298 AA; 33674 MW; C057726AC335803C CRC64;
MSKIFINPSD IRSGLADLEM AEETVELVNR NMEDSQAHLQ GVPIDVETLP EDIQRLHITD
PQASLRQDMV DEQKHQEDED FYLTGRENPL SPFQTHLDAI GLRIVRKMKT GEGFFKIWSQ
AVEDIVSYVA LNFSIPVNKL FEDKSTQTVT EKSQQASASS APNRHEKSSQ NARVNSKDAS
GPAALDWTAS NEADDESVEA EIAHQIAESF SKKYKFPSRS SGIFLWNFEQ LKMNLDEIVR
EVKEIPGVIK MAKDGMKLPL RCMLGGVAST HSRRFQILVN PEKLGKVMQE DLDKYLTY
