PHOSP_AMPV1
ID PHOSP_AMPV1 Reviewed; 294 AA.
AC Q2Y2M5;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 29-SEP-2021, entry version 49.
DE RecName: Full=Phosphoprotein;
OS Avian metapneumovirus (isolate Canada goose/Minnesota/15a/2001) (AMPV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Metapneumovirus.
OX NCBI_TaxID=652954;
OH NCBI_TaxID=8847; Anser sp. (goose).
OH NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=15666873; DOI=10.1637/7208-051804r;
RA Bennett R.S., Nezworski J., Velayudhan B.T., Nagaraja K.V., Zeman D.H.,
RA Dyer N., Graham T., Lauer D.C., Njenga M.K., Halvorson D.A.;
RT "Evidence of avian pneumovirus spread beyond Minnesota among wild and
RT domestic birds in central North America.";
RL Avian Dis. 48:902-908(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16282483; DOI=10.1128/jvi.79.23.14834-14842.2005;
RA Bennett R.S., LaRue R., Shaw D., Yu Q., Nagaraja K.V., Halvorson D.A.,
RA Njenga M.K.;
RT "A wild goose metapneumovirus containing a large attachment glycoprotein is
RT avirulent but immunoprotective in domestic turkeys.";
RL J. Virol. 79:14834-14842(2005).
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. Acts as a chaperone for neo-synthesized nucleoprotein by
CC forming an N-P complex that preserves N in a monomeric and RNA-free
CC state and prevents the association of nascent N with host cell RNAs.
CC Recruits the host phosphatase PP1 to inclusion bodies to regulate viral
CC transcription (By similarity). {ECO:0000250|UniProtKB:P03421,
CC ECO:0000250|UniProtKB:Q8B9Q8}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with protein M2-1; the
CC interaction between the two tetramers is required for the anti-
CC termination and elongation transcriptional activities of protein M2-1.
CC Interacts with host phosphatase PP1; this interaction recruits PP1 to
CC the inclusion bodies. Formation of a complex PP1/M2-1/P allows P to
CC target host PP1 phosphatase to the M2-1 substrate. Interacts with the
CC nucleoprotein N; the phosphorylated phosphoprotein P binds to N-RNA
CC complex. Interacts with the monomeric RNA-free nucleoprotein N (By
CC similarity). Interacts with RNA-directed RNA polymerase L (via N-
CC terminus); the association of P and L forms the polymerase complex (By
CC similarity). {ECO:0000250|UniProtKB:P03421,
CC ECO:0000250|UniProtKB:Q8B9Q8}.
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; DQ009484; AAY81655.1; -; Viral_cRNA.
DR RefSeq; YP_443838.1; NC_007652.1.
DR SMR; Q2Y2M5; -.
DR Proteomes; UP000002471; 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 3: Inferred from homology;
KW Host cytoplasm; Phosphoprotein; Reference proteome; Viral RNA replication;
KW Virion.
FT CHAIN 1..294
FT /note="Phosphoprotein"
FT /id="PRO_0000390370"
FT REGION 12..28
FT /note="Binding to monomeric RNA-free nucleoprotein"
FT /evidence="ECO:0000250|UniProtKB:Q8B9Q8"
FT REGION 52..97
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:0000250|UniProtKB:Q8B9Q8"
FT REGION 234..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..279
FT /note="Binding to RNA-directed RNA polymerase L"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT REGION 281..294
FT /note="Binding to the N-RNA complex"
FT /evidence="ECO:0000250|UniProtKB:P03421"
FT COMPBIAS 67..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..287
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; 32541 MW; 9B82254688931B71 CRC64;
MSFPEGKDIL LMGNEAAKAA EAFQRSLKKI GHRRTQSIVG DKIITVSETV EKPTISKSTK
VTTPPERRNA WGEKPDTTRN QTEEARNEAT LEDTSRLYEE VFAPTSDGKT PAEEGMETPE
KPKKKVTFKN DESGRYTKLE MEALELLSDN EDDDAESSVL TFEEKDTSAL SLEARLESID
EKLSMILGLL RTLNVATAGP TAARDGIRDA MVGLREELIA DIIKEAKGKA AEMMKEEAKQ
KSKIGNGSVG LTEKAKELNK IVEDESTSGE SEEEEEEEDE EESNPDDDLY SLTM
