PHOSP_BRSVA
ID PHOSP_BRSVA Reviewed; 241 AA.
AC P33454; Q77KZ1; Q77L01;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 23-FEB-2022, entry version 80.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
GN Name=P;
OS Bovine respiratory syncytial virus (strain A51908) (BRS).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=11247;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1402819; DOI=10.1099/0022-1317-73-9-2441;
RA Mallipeddi S.K., Samal S.K.;
RT "Sequence comparison between the phosphoprotein mRNAs of human and bovine
RT respiratory syncytial viruses identifies a divergent domain in the
RT predicted protein.";
RL J. Gen. Virol. 73:2441-2444(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=A51908, and ATCC 51908;
RX PubMed=11724268; DOI=10.1023/a:1011888019966;
RA Yunus A.S., Khattar S.K., Collins P.L., Samal S.K.;
RT "Rescue of bovine respiratory syncytial virus from cloned cDNA: entire
RT genome sequence of BRSV strain A51908.";
RL Virus Genes 23:157-164(2001).
RN [3]
RP INTERACTION WITH THE PHOSPHOPROTEIN.
RX PubMed=8609467; DOI=10.1099/0022-1317-77-5-1019;
RA Mallipeddi S.K., Lupiani B., Samal S.K.;
RT "Mapping the domains on the phosphoprotein of bovine respiratory syncytial
RT virus required for N-P interaction using a two-hybrid system.";
RL J. Gen. Virol. 77:1019-1023(1996).
RN [4]
RP INTERACTION WITH THE PHOSPHOPROTEIN.
RX PubMed=10772994; DOI=10.1006/viro.2000.0264;
RA Khattar S.K., Yunus A.S., Collins P.L., Samal S.K.;
RT "Mutational analysis of the bovine respiratory syncytial virus nucleocapsid
RT protein using a minigenome system: mutations that affect encapsidation, RNA
RT synthesis, and interaction with the phosphoprotein.";
RL Virology 270:215-228(2000).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=32878896; DOI=10.1128/jvi.01380-20;
RA Jobe F., Simpson J., Hawes P., Guzman E., Bailey D.;
RT "Respiratory syncytial virus sequesters NF-kappaB subunit p65 to
RT cytoplasmic inclusion bodies to inhibit innate immune signalling.";
RL J. Virol. 0:0-0(2020).
CC -!- FUNCTION: Plays critical roles in regulating RNA replication and
CC transcription through its interactions with multiple proteins (By
CC similarity). Tethers the RNA-directed RNA polymerase L to the
CC nucleoprotein-RNA complex (By similarity). Recruits the M2-1 protein, a
CC processivity factor that is required for efficient transcription of
CC viral RNA (By similarity). Acts as a chaperone for neo-synthesized
CC nucleoprotein by forming an N-P complex that preserves N in a monomeric
CC and RNA-free state and prevents the association of nascent N with host
CC cell RNAs (By similarity). Recruits the host phosphatase PP1 to
CC inclusion bodies to regulate viral transcription (By similarity).
CC Together with the nucleoprotein, sequesters host NF-kappa-B in
CC inclusion bodies (IBs) thereby inhibiting this host defense pathway
CC (PubMed:32878896). {ECO:0000250|UniProtKB:P03421,
CC ECO:0000269|PubMed:32878896}.
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:0000269|PubMed:32878896}. Note=Localizes in cytoplasmic
CC inclusion bodies. {ECO:0000269|PubMed:32878896}.
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; M93127; AAA42815.1; -; mRNA.
DR EMBL; AF295543; AAL49395.1; -; Genomic_RNA.
DR EMBL; AF295544; AAL49406.1; -; Genomic_RNA.
DR PIR; JQ1641; JQ1641.
DR SMR; P33454; -.
DR DIP; DIP-521N; -.
DR IntAct; P33454; 2.
DR Proteomes; UP000007616; 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; IPR003487; Pprotein_pneumovir.
DR Pfam; PF02478; Pneumo_phosprot; 1.
PE 1: Evidence at protein level;
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_0000142720"
FT REGION 1..30
FT /note="Binding to monomeric RNA-free nucleoprotein"
FT /evidence="ECO:0000305|PubMed:8609467"
FT REGION 39..57
FT /note="Important for viral particle assembly"
FT /evidence="ECO:0000250|UniProtKB:P03421"
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 199..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:0000305|PubMed:8609467"
FT COMPBIAS 199..216
FT /note="Basic and acidic 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"
FT VARIANT 46
FT /note="I -> V (in strain: ATCC 51908)"
FT VARIANT 61
FT /note="H -> Q (in strain: ATCC 51908)"
FT VARIANT 75
FT /note="A -> T (in strain: ATCC 51908)"
FT VARIANT 100
FT /note="K -> R (in strain: ATCC 51908)"
SQ SEQUENCE 241 AA; 27254 MW; 15B46A1A60EA05C6 CRC64;
MEKFAPEFHG EDANTKATKF LESLKGKFTS SKDSRKKDSI ISVNSIDIEL PKESPITSTN
HNINQPSEIN DTIAANQVHI RKPLVSFKEE LPSSENPFTK LYKETIETFD NNEEESSYSY
DEINDQTNDN ITARLDRIDE KLSEIIGMLH TLVVASAGPT AARDGIRDAM VGLREEMIEK
IRSEALMTND RLEAMARLRD EESEKMTKDT SDEVKLTPTS EKLNMVLEDE SSDNDLSLED
F
