PHOSP_ORSVW
ID PHOSP_ORSVW Reviewed; 241 AA.
AC Q83956;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 29-SEP-2021, entry version 65.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
GN Name=P;
OS Ovine respiratory syncytial virus (strain WSU 83-1578) (ORSV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; unclassified Pneumoviridae.
OX NCBI_TaxID=79699;
OH NCBI_TaxID=9940; Ovis aries (Sheep).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7996153; DOI=10.1099/0022-1317-75-12-3597;
RA Alansari H.M., Potgieter L.N.D.;
RT "Molecular cloning and sequence analysis of the phosphoprotein,
RT nucleocapsid protein, matrix protein and 22K (M2) protein of the ovine
RT respiratory syncytial virus.";
RL J. Gen. Virol. 75:3597-3601(1994).
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. 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; U07232; AAA62433.1; -; mRNA.
DR SMR; Q83956; -.
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 2: Evidence at transcript level;
KW Host cytoplasm; Phosphoprotein; Viral RNA replication; Virion.
FT CHAIN 1..241
FT /note="Phosphoprotein"
FT /id="PRO_0000142721"
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 51..78
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 202..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 55..78
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; 27102 MW; 2463DA38B20B44B0 CRC64;
MEKFAPEFHG EDANTKATKF LESLKGKFTS SKDSKKKDSI ISVNSIDIEL PKESPITSAN
HNISQSGENS DTPATNQVHT RKPLVSFREE LPTSENPFTK LYKETIETFD NNEEESSYSY
DEINDQTNDN ITARLDRIDE KLSEIIGMLH TLVVASAGPT AARDGIRDAM VGLREEMIEK
IRSEALMTND RLEAMARLRN EESEKMAKDT SDDVNLNSTS EKLNTILEED NSDNDLSLED
F
