PHOSP_MOKV
ID PHOSP_MOKV Reviewed; 303 AA.
AC P0C569;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 23-FEB-2022, entry version 61.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
DE AltName: Full=Protein M1;
GN Name=P;
OS Mokola virus (MOKV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=12538;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH NCBI_TaxID=269271; Chodsigoa caovansunga (Van Sung's shrew).
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH NCBI_TaxID=9989; Rodentia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9225031; DOI=10.1099/0022-1317-78-7-1571;
RA Le Mercier P., Jacob Y., Tordo N.;
RT "The complete Mokola virus genome sequence: structure of the RNA-dependent
RT RNA polymerase.";
RL J. Gen. Virol. 78:1571-1576(1997).
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 P3]: Host nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=P;
CC IsoId=P0C569-1; Sequence=Displayed;
CC Name=P2;
CC IsoId=P0C569-2; Sequence=VSP_026897;
CC Name=P3;
CC IsoId=P0C569-3; Sequence=VSP_026896;
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; Y09762; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR RefSeq; YP_142351.1; NC_006429.1. [P0C569-1]
DR PDB; 2WZL; X-ray; 2.10 A; A=1-303.
DR PDBsum; 2WZL; -.
DR SMR; P0C569; -.
DR GeneID; 3159477; -.
DR KEGG; vg:3159477; -.
DR EvolutionaryTrace; P0C569; -.
DR Proteomes; UP000006826; 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 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; Reference proteome;
KW Viral immunoevasion; Viral RNA replication; Virion.
FT CHAIN 1..303
FT /note="Phosphoprotein"
FT /id="PRO_0000295249"
FT REGION 50..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..194
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 52..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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_026896"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform P2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026897"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:2WZL"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:2WZL"
FT STRAND 214..226
FT /evidence="ECO:0007829|PDB:2WZL"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:2WZL"
FT HELIX 235..242
FT /evidence="ECO:0007829|PDB:2WZL"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:2WZL"
FT HELIX 260..271
FT /evidence="ECO:0007829|PDB:2WZL"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:2WZL"
FT HELIX 281..300
FT /evidence="ECO:0007829|PDB:2WZL"
SQ SEQUENCE 303 AA; 34205 MW; 1B6EAEB985871A29 CRC64;
MSKDLVHPSL IRAGIVELEM AEETTDLINR TIESNQAHLQ GEPLYVDSLP EDMSRLRIED
KSRRTKTEEE ERDEGSSEED NYLSEGQDPL IPFQNFLDEI GARAVKRLKT GEGFFRVWSA
LSDDIKGYVS TNIMTSGERD TKSIQIQTEP TASVSSGNES RHDSESMHDP NDKKDHTPDH
DVVPDIESST DKGEIRDIEG EVAHQVAESF SKKYKFPSRS SGIFLWNFEQ LKMNLDDIVK
AAMNVPGVER IAEKGGKLPL RCILGFVALD SSKRFRLLAD NDKVARLIQE DINSYMARLE
EAE
