PHOSP_HRSVL
ID PHOSP_HRSVL Reviewed; 241 AA.
AC P12579;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 23-FEB-2022, entry version 82.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
GN Name=P;
OS Human respiratory syncytial virus A (strain Long).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=11260;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3414184; DOI=10.1016/0168-1702(88)90020-2;
RA Lopez J.A., Villanueva N., Melero J.A., Portela A.;
RT "Nucleotide sequence of the fusion and phosphoprotein genes of human
RT respiratory syncytial (RS) virus Long strain: evidence of subtype genetic
RT heterogeneity.";
RL Virus Res. 10:249-262(1988).
RN [2]
RP PHOSPHORYLATION AT SER-116; SER-117 AND SER-119.
RX PubMed=2045795; DOI=10.1099/0022-1317-72-6-1455;
RA Navarro J., Lopez-Otin C., Villanueva N.;
RT "Location of phosphorylated residues in human respiratory syncytial virus
RT phosphoprotein.";
RL J. Gen. Virol. 72:1455-1459(1991).
RN [3]
RP DOMAIN.
RX PubMed=15166449; DOI=10.1099/vir.0.79830-0;
RA Castagne N., Barbier A., Bernard J., Rezaei H., Huet J.C., Henry C.,
RA Da Costa B., Eleouet J.F.;
RT "Biochemical characterization of the respiratory syncytial virus P-P and P-
RT N protein complexes and localization of the P protein oligomerization
RT domain.";
RL J. Gen. Virol. 85:1643-1653(2004).
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 (PubMed:15166449). The C-terminus
CC part contains binding regions for the RNA-directed RNA polymerase L and
CC the nucleoprotein (By similarity). {ECO:0000250|UniProtKB:P03421,
CC ECO:0000269|PubMed:15166449}.
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; M22644; AAA47415.1; -; Genomic_RNA.
DR PIR; S07428; RRNZPP.
DR BMRB; P12579; -.
DR SASBDB; P12579; -.
DR SMR; P12579; -.
DR iPTMnet; P12579; -.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
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 DisProt; DP00447; -.
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;
KW Viral RNA replication; Virion.
FT CHAIN 1..241
FT /note="Phosphoprotein"
FT /id="PRO_0000142724"
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 52..77
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 201..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 52..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..232
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:0000269|PubMed:2045795"
FT MOD_RES 117
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:2045795"
FT MOD_RES 119
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000269|PubMed:2045795"
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; 27147 MW; DCB2D3942973DD59 CRC64;
MEKFAPEFHG EDANNRATKF LESIKGKFTS PKDPKKKDSI ISVNSTDIEV TKESPITSNS
TIINPTNETD DNAGNKPNYQ RKPLVSFKED PIPSDNPFSK LYKETIETFD NNEEESSYSY
EEINDQTNDN ITARLDRIDE KLSEILGMLH TLVVASAGPT SARDGIRDAM VGLREEMIEK
IRTEALMTND RLEAMARLRN EESEKMAKDT SDEVSLNPTS EKLNNLLEGN DSDNDLSLED
F
