M21_MPV15
ID M21_MPV15 Reviewed; 176 AA.
AC Q5MKM1; Q50EW4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Protein M2-1;
DE AltName: Full=Envelope-associated 22 kDa protein;
DE AltName: Full=Transcription antitermination factor M2-1;
GN Name=M2-1;
OS Murine pneumonia virus (strain 15) (MPV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=296738;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=15;
RX PubMed=15604443; DOI=10.1099/vir.0.80315-0;
RA Thorpe L.C., Easton A.J.;
RT "Genome sequence of the non-pathogenic strain 15 of pneumonia virus of mice
RT and comparison with the genome of the pathogenic strain J3666.";
RL J. Gen. Virol. 86:159-169(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=15;
RX PubMed=15744580; DOI=10.1007/s11262-004-5631-4;
RA Krempl C.D., Lamirande E.W., Collins P.L.;
RT "Complete sequence of the RNA genome of pneumonia virus of mice (PVM).";
RL Virus Genes 30:237-249(2005).
CC -!- FUNCTION: Acts as a tetrameric transcription processivity factor that
CC binds in a competitive manner to RNA and the phosphoprotein (P) to
CC prevent premature termination during transcription. Transcription anti-
CC terminator that enhances readthrough of intergenic junctions during
CC viral transcription. Preferentially binds to poly(A)-rich sequences.
CC Plays a role in the association of the matrix protein with the
CC nucleocapsid, which initiates assembly and budding.
CC {ECO:0000250|UniProtKB:P04545}.
CC -!- SUBUNIT: Homotetramer. The homotetramer interacts with RNA. Interacts
CC with the phosphoprotein (P); this interaction is required for protein
CC M2-1 function, localization in host inclusion bodies. Formation of a
CC complex host PP1/M2-1/P allows P to target host PP1 phosphatase to the
CC M2-1 substrate. Interacts with the nucleoprotein (N). Interacts with
CC the matrix protein (M); this interaction directs M localization to
CC cytoplasmic inclusions comprising viral proteins L, N, P, and M2-1 and
CC mediates M association with the nucleocapsid. Interacts with host
CC PABPC1 (via C-terminus). {ECO:0000250|UniProtKB:P04545}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P04545}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P04545}. Host nucleus
CC {ECO:0000250|UniProtKB:P04545}. Note=Localizes in cytoplasmic inclusion
CC bodies substructures called inclusion bodies associated granules
CC (IBAGs). Forms a layer between the matrix and nucleocapsid.
CC {ECO:0000250|UniProtKB:P04545}.
CC -!- DOMAIN: Contains a zinc-finger domain on its N-terminus essential for
CC its anti-termination function. Contains an oligomerization domain. The
CC central globular core is responsible for binding to RNA and
CC phosphoprotein. {ECO:0000250|UniProtKB:P04545}.
CC -!- PTM: Phosphorylated by host in infected cells. Only dephosphorylated
CC M2-1 is competent for viral mRNA binding. Cyclic turnover of
CC phosphorylation-dephosphorylation of M2-1 is required for efficient
CC viral transcription. {ECO:0000250|UniProtKB:P04545}.
CC -!- SIMILARITY: Belongs to the pneumoviridae M2-1 protein family.
CC {ECO:0000305}.
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DR EMBL; AY743910; AAW02841.1; -; Genomic_RNA.
DR EMBL; AY729016; AAW79182.1; -; Genomic_RNA.
DR SMR; Q5MKM1; -.
DR Proteomes; UP000133604; Genome.
DR Proteomes; UP000147186; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044423; C:virion component; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0046782; P:regulation of viral transcription; IEA:InterPro.
DR GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-KW.
DR GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
DR InterPro; IPR009452; Pneumovirus_M2-1.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF06436; Pneumovirus_M2; 1.
DR PIRSF; PIRSF003913; Matrix_glycop-M2_paramyxo; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 3: Inferred from homology;
KW Host cytoplasm; Host nucleus; Metal-binding; Phosphoprotein;
KW Reference proteome; RNA-binding; Transcription;
KW Transcription antitermination; Transcription regulation;
KW Viral transcription; Virion; Zinc; Zinc-finger.
FT CHAIN 1..176
FT /note="Protein M2-1"
FT /id="PRO_0000365792"
FT ZN_FING 1..27
FT /note="C3H1-type"
FT /evidence="ECO:0000250|UniProtKB:P04545,
FT ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 31..48
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT REGION 75..169
FT /note="Globular core"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT REGION 125..161
FT /note="Binding to the phosphoprotein"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT SITE 7
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT SITE 8
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT SITE 91
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT SITE 149
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT MOD_RES 57
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT MOD_RES 60
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P04545"
SQ SEQUENCE 176 AA; 20204 MW; 5440FEC3904C9039 CRC64;
MSVRPCKFEV QGFCSRGRNC KYSHKYWEWP LKTLMLRQNY MLNRIYRFLD TNTDAMSDVS
GFDAPQRTAE YALGTIGVLK SYLEKTNNIT KSIACGSLIT VLQNLDVGLV IQARDSNTED
TNYLRSCNTI LSYIDKIHKK RQIIHILKRL PVGVLCNLIQ SVISIEEKIN SSMKTE
