PHOSP_MPV15
ID PHOSP_MPV15 Reviewed; 295 AA.
AC Q5MKM7; Q50EV8;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 29-SEP-2021, entry version 50.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
GN Name=P;
OS Murine pneumonia virus (strain 15) (MPV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=296738;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=15;
RX PubMed=15604443; DOI=10.1099/vir.0.80315-0;
RA Thorpe L.C., Easton A.J.;
RT "Genome sequence of the non-pathogenic strain 15 of pneumonia virus of mice
RT and comparison with the genome of the pathogenic strain J3666.";
RL J. Gen. Virol. 86:159-169(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15744580; DOI=10.1007/s11262-004-5631-4;
RA Krempl C.D., Lamirande E.W., Collins P.L.;
RT "Complete sequence of the RNA genome of pneumonia virus of mice (PVM).";
RL Virus Genes 30:237-249(2005).
CC -!- FUNCTION: Plays critical roles in regulating RNA replication and
CC transcription through its interactions with multiple proteins. Tethers
CC the RNA-directed RNA polymerase L to the nucleoprotein-RNA complex.
CC Recruits the M2-1 protein, a processivity factor that is required for
CC efficient transcription of viral RNA. Acts as a chaperone for neo-
CC synthesized nucleoprotein by forming an N-P complex that preserves N in
CC a monomeric and RNA-free state and prevents the association of nascent
CC N with host cell RNAs. Recruits the host phosphatase PP1 to inclusion
CC bodies to regulate viral transcription. {ECO:0000250|UniProtKB:P03421}.
CC -!- SUBUNIT: Homotetramer. Interacts with protein M2-1; the interaction
CC between the two tetramers is required for the anti-termination and
CC elongation transcriptional activities of protein M2-1. Interacts with
CC host phosphatase PP1; this interaction recruits PP1 to the inclusion
CC bodies. Formation of a complex PP1/M2-1/P allows P to target host PP1
CC phosphatase to the M2-1 substrate. Interacts (via C-terminus) with the
CC nucleoprotein N (via N-terminus); the phosphorylated phosphoprotein P
CC binds to N-RNA complex. Interacts (via N-terminus) with the monomeric
CC RNA-free nucleoprotein N. Interacts (via C-terminus) with RNA-directed
CC RNA polymerase L; the association of P and L forms the polymerase
CC complex. {ECO:0000250|UniProtKB:P03421}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03421}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P03421}. Note=Localizes in cytoplasmic
CC inclusion bodies. {ECO:0000250|UniProtKB:P03421}.
CC -!- DOMAIN: The N-terminus is important for viral particle assembly. The
CC oligomerization region is central. The C-terminus part contains binding
CC regions for the RNA-directed RNA polymerase L and the nucleoprotein.
CC {ECO:0000250|UniProtKB:P03421}.
CC -!- PTM: Constitutively phosphorylated by host.
CC {ECO:0000250|UniProtKB:P03421}.
CC -!- SIMILARITY: Belongs to the pneumoviridae phosphoprotein P family.
CC {ECO:0000305}.
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DR EMBL; AY743910; AAW02835.1; -; Genomic_RNA.
DR EMBL; AY729016; AAW79177.1; -; Genomic_RNA.
DR SMR; Q5MKM7; -.
DR Proteomes; UP000133604; Genome.
DR Proteomes; UP000147186; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR InterPro; IPR003487; Pprotein_pneumovir.
DR Pfam; PF02478; Pneumo_phosprot; 1.
PE 3: Inferred from homology;
KW Host cytoplasm; Phosphoprotein; Reference proteome; Viral RNA replication;
KW Virion.
FT CHAIN 1..295
FT /note="Phosphoprotein"
FT /id="PRO_0000365784"
FT REGION 1..30
FT /note="Binding to monomeric RNA-free nucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT REGION 51..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..131
FT /note="Binding to host phosphatase PP1"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT REGION 134..156
FT /note="Binding to protein M2-1"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT REGION 166..207
FT /note="Oligomerization and binding to RNA-directed RNA
FT polymerase L"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT REGION 263..281
FT /note="Binding to RNA-directed RNA polymerase L"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT REGION 281..295
FT /note="Binding to the N-RNA complex"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT COMPBIAS 70..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 152
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03421"
SQ SEQUENCE 295 AA; 32913 MW; 157B486193061E57 CRC64;
MEKFAPEFVG EDANKKAEEF LKHRSFPSEK PLAGIPNTAT HVTKYNMPPI LRSSFKLPSP
RVAANLTEPS APPTTPPPTP PQNKEEQPKE SDVDIETMHV CKVPDNPEHS KKPCCSDDTD
TKKTRKPMVT FVEPEEKFVG LGASLYRETM QTFAADGYDE ESNLSFEETN QEPGSSSVEQ
RLDRIEEKLS YIIGLLNTIM VATAGPTTAR DEIRDALIGT REELIEMIKS DILTVNDRIV
AMEKLRDEEC SRADTDDGSA CYLTDRARIL DKIVSSNAEE AKEDLDVDDI MGINF
