ID   PHOSP_HRSVB             Reviewed;         241 AA.
AC   O42062;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   23-FEB-2022, entry version 73.
DE   RecName: Full=Phosphoprotein;
DE            Short=Protein P;
GN   Name=P;
OS   Human respiratory syncytial virus B (strain B1).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX   NCBI_TaxID=79692;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=B1;
RX   PubMed=9391135; DOI=10.1073/pnas.94.25.13961;
RA   Karron R.A., Buonagurio D.A., Georgiu A.F., Whitehead S.S., Adamus J.E.,
RA   Clements-Mann M.L., Harris D.O., Randolph V.B., Udem S.A., Murphy B.R.,
RA   Sidhu M.S.;
RT   "Respiratory syncytial virus (RSV) SH and G proteins are not essential for
RT   viral replication in vitro: clinical evaluation and molecular
RT   characterization of a cold-passaged, attenuated RSV subgroup B mutant.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:13961-13966(1997).
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. Together with the
CC       nucleoprotein, sequesters host NF-kappa-B in inclusion bodies (IBs)
CC       thereby inhibiting this host defense pathway.
CC       {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. Phosphorylation at S-116,
CC       S-117, S-119, S-232 and S-237 is required for transcription inhibition
CC       by M2-2 and viral particle egress. Phosphorylation at S-232 and S-237
CC       increases the affinity of the binding to the nucleoprotein.
CC       {ECO:0000250|UniProtKB:P03421}.
CC   -!- SIMILARITY: Belongs to the pneumoviridae phosphoprotein P family.
CC       {ECO:0000305}.
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DR   EMBL; AF013254; AAB82432.1; -; Genomic_RNA.
DR   EMBL; AF013255; AAB82443.1; -; Genomic_RNA.
DR   RefSeq; NP_056859.1; NC_001781.1.
DR   SMR; O42062; -.
DR   PRIDE; O42062; -.
DR   GeneID; 1489821; -.
DR   KEGG; vg:1489821; -.
DR   Proteomes; UP000002472; Genome.
DR   Proteomes; UP000180717; 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   GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR003487; Pprotein_pneumovir.
DR   Pfam; PF02478; Pneumo_phosprot; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Host-virus interaction;
KW   Inhibition of host NF-kappa-B by virus; Phosphoprotein; Reference proteome;
KW   Viral RNA replication; Virion.
FT   CHAIN           1..241
FT                   /note="Phosphoprotein"
FT                   /id="PRO_0000365783"
FT   REGION          1..30
FT                   /note="Binding to monomeric RNA-free nucleoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:P03421"
FT   REGION          39..57
FT                   /note="Important for viral particle assembly"
FT                   /evidence="ECO:0000250|UniProtKB:P03421"
FT   REGION          53..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..87
FT                   /note="Binding to host phosphatase PP1"
FT                   /evidence="ECO:0000250|UniProtKB:P03421"
FT   REGION          90..110
FT                   /note="Binding to protein M2-1"
FT                   /evidence="ECO:0000250|UniProtKB:P03421"
FT   REGION          120..160
FT                   /note="Oligomerization and binding to RNA-directed RNA
FT                   polymerase L"
FT                   /evidence="ECO:0000250|UniProtKB:P03421"
FT   REGION          200..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..232
FT                   /note="Binding to RNA-directed RNA polymerase L"
FT                   /evidence="ECO:0000250|UniProtKB:P03421"
FT   REGION          232..241
FT                   /note="Binding to the N-RNA complex"
FT                   /evidence="ECO:0000250|UniProtKB:P03421"
FT   COMPBIAS        53..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            108
FT                   /note="Interaction with protein M2-1"
FT                   /evidence="ECO:0000250|UniProtKB:P03421"
FT   MOD_RES         108
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03421"
FT   MOD_RES         116
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03421"
FT   MOD_RES         117
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03421"
FT   MOD_RES         119
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03421"
FT   MOD_RES         232
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03421"
FT   MOD_RES         237
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03421"
SQ   SEQUENCE   241 AA;  26992 MW;  1333E057247ADF57 CRC64;
     MEKFAPEFHG EDANNKATKF LESIKGKFAS SKDPKKKDSI ISVNSIDIEV TKESPITSGT
     NIINPTSEAD STPETKANYP RKPLVSFKED LTPSDNPFSK LYKETIETFD NNEEESSYSY
     EEINDQTNDN ITARLDRIDE KLSEILGMLH TLVVASAGPT SARDGIRDAM VGLREEMIEK
     IRAEALMTND RLEAMARLRN EESEKMAKDT SDEVPLNPTS KKLSDLLEDN DSDNDLSLDD
     F