PHOSP_HMPVC
ID PHOSP_HMPVC Reviewed; 294 AA.
AC Q8B9Q8;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 29-SEP-2021, entry version 53.
DE RecName: Full=Phosphoprotein;
DE Short=Protein P;
GN Name=P;
OS Human metapneumovirus (strain CAN97-83) (HMPV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Metapneumovirus.
OX NCBI_TaxID=694067;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12727342; DOI=10.1016/s0168-1702(03)00065-0;
RA Bastien N., Normand S., Taylor T., Ward D., Peret T.C., Boivin G.,
RA Anderson L.J., Li Y.;
RT "Sequence analysis of the N, P, M and F genes of Canadian human
RT metapneumovirus strains.";
RL Virus Res. 93:51-62(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=14592754; DOI=10.1016/s0042-6822(03)00528-2;
RA Biacchesi S., Skiadopoulos M.H., Boivin G., Hanson C.T., Murphy B.R.,
RA Collins P.L., Buchholz U.J.;
RT "Genetic diversity between human metapneumovirus subgroups.";
RL Virology 315:1-9(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16306583; DOI=10.1128/jvi.79.24.15114-15122.2005;
RA Pham Q.N., Biacchesi S., Skiadopoulos M.H., Murphy B.R., Collins P.L.,
RA Buchholz U.J.;
RT "Chimeric recombinant human metapneumoviruses with the nucleoprotein or
RT phosphoprotein open reading frame replaced by that of avian metapneumovirus
RT exhibit improved growth in vitro and attenuation in vivo.";
RL J. Virol. 79:15114-15122(2005).
RN [4] {ECO:0007744|PDB:6U5O}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS) IN COMPLEX WITH THE
RP RNA-DIRECTED RNA POLYMERASE L, SUBUNIT, INTERACTION WITH RNA-DIRECTED RNA
RP POLYMERASE L, AND FUNCTION.
RX PubMed=31698413; DOI=10.1038/s41586-019-1759-1;
RA Pan J., Qian X., Lattmann S., El Sahili A., Yeo T.H., Jia H., Cressey T.,
RA Ludeke B., Noton S., Kalocsay M., Fearns R., Lescar J.;
RT "Structure of the human metapneumovirus polymerase phosphoprotein
RT complex.";
RL Nature 577:275-279(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 (PubMed:31698413). Recruits the M2-1 protein,
CC a 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 {ECO:0000250|UniProtKB:P03421, ECO:0000269|PubMed:31698413}.
CC -!- SUBUNIT: Homotetramer (PubMed:31698413). Interacts with protein M2-1;
CC the interaction between the two tetramers is required for the anti-
CC termination and elongation transcriptional activities of protein M2-1
CC (By similarity). Interacts with host phosphatase PP1; this interaction
CC recruits PP1 to the inclusion bodies (By similarity). Formation of a
CC complex PP1/M2-1/P allows P to target host PP1 phosphatase to the M2-1
CC substrate (By similarity). Interacts with the nucleoprotein N; the
CC phosphorylated phosphoprotein P binds to N-RNA complex. Interacts with
CC the monomeric RNA-free nucleoprotein N (By similarity). Interacts with
CC RNA-directed RNA polymerase L (via N-terminus); the association of P
CC and L forms the polymerase complex (PubMed:31698413).
CC {ECO:0000250|UniProtKB:P03421, ECO:0000269|PubMed:31698413}.
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 -!- 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; AY145251; AAN52865.1; -; Genomic_RNA.
DR EMBL; AY297749; AAQ67693.1; -; Genomic_RNA.
DR RefSeq; YP_012606.1; NC_004148.2.
DR PDB; 6U5O; EM; 3.70 A; P/Q/R/S=1-294.
DR PDBsum; 6U5O; -.
DR SMR; Q8B9Q8; -.
DR IntAct; Q8B9Q8; 1.
DR PRIDE; Q8B9Q8; -.
DR Proteomes; UP000001398; 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 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Phosphoprotein; Reference proteome;
KW Viral RNA replication; Virion.
FT CHAIN 1..294
FT /note="Phosphoprotein"
FT /id="PRO_0000394809"
FT REGION 12..28
FT /note="Binding to monomeric RNA-free nucleoprotein"
FT /evidence="ECO:0000305|PubMed:31698413"
FT REGION 97..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..128
FT /note="Binding to host phosphatase PP1"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT REGION 135..157
FT /note="Binding to protein M2-1"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT REGION 169..194
FT /note="Oligomerization and binding to RNA-directed RNA
FT polymerase L"
FT /evidence="ECO:0000269|PubMed:31698413"
FT REGION 251..279
FT /note="Binding to RNA-directed RNA polymerase L"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT REGION 260..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..294
FT /note="Binding to the N-RNA complex"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT COMPBIAS 97..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..282
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P03421"
SQ SEQUENCE 294 AA; 32748 MW; EFB8C2195CAEB8CC CRC64;
MSFPEGKDIL FMGNEAAKLA EAFQKSLRKP SHKRSQSIIG EKVNTVSETL ELPTISRPTK
PTILSEPKLA WTDKGGAIKT EAKQTIKVMD PIEEEEFTEK RVLPSSDGKT PAEKKLKPST
NTKKKVSFTP NEPGKYTKLE KDALDLLSDN EEEDAESSIL TFEERDTSSL SIEARLESIE
EKLSMILGLL RTLNIATAGP TAARDGIRDA MIGIREELIA DIIKEAKGKA AEMMEEEMNQ
RTKIGNGSVK LTEKAKELNK IVEDESTSGE SEEEEELKDT QENNQEDDIY QLIM
