M21_BRSVA
ID M21_BRSVA Reviewed; 186 AA.
AC P29792; Q77KY9; Q77KZ7;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 80.
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 Bovine respiratory syncytial virus (strain A51908) (BRS).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=11247;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1312130; DOI=10.1099/0022-1317-73-3-737;
RA Zamora M., Samal S.K.;
RT "Sequence analysis of M2 mRNA of bovine respiratory syncytial virus
RT obtained from an F-M2 dicistronic mRNA suggests structural homology with
RT that of human respiratory syncytial virus.";
RL J. Gen. Virol. 73:737-741(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=A51908, and ATCC 51908;
RX PubMed=11724268; DOI=10.1023/a:1011888019966;
RA Yunus A.S., Khattar S.K., Collins P.L., Samal S.K.;
RT "Rescue of bovine respiratory syncytial virus from cloned cDNA: entire
RT genome sequence of BRSV strain A51908.";
RL Virus Genes 23:157-164(2001).
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; M82816; AAA42805.1; -; mRNA.
DR EMBL; AF295543; AAL49400.1; -; Genomic_RNA.
DR EMBL; AF295544; AAL49411.1; -; Genomic_RNA.
DR PIR; JQ1482; WMNZBA.
DR SMR; P29792; -.
DR DIP; DIP-1099N; -.
DR PRIDE; P29792; -.
DR Proteomes; UP000007616; 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 SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 2: Evidence at transcript level;
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..186
FT /note="Protein M2-1"
FT /id="PRO_0000142838"
FT ZN_FING 1..28
FT /note="C3H1-type"
FT /evidence="ECO:0000250|UniProtKB:P04545,
FT ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 32..49
FT /note="Oligomerization"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT REGION 76..171
FT /note="Globular core"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT REGION 126..163
FT /note="Binding to the phosphoprotein"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT SITE 8
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT SITE 23
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT SITE 92
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT SITE 151
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT MOD_RES 58
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT MOD_RES 61
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT VARIANT 85
FT /note="S -> G (in strain: ATCC 51908)"
FT VARIANT 180..182
FT /note="NVD -> IVN (in strain: ATCC 51908)"
SQ SEQUENCE 186 AA; 21351 MW; 6EF51ED06E35F23E CRC64;
MSRRNPCKYE IRGHCLNGKK CHFSHNYFEW PPHALLVRQN FMLNKILKSM DRNNDTLSEI
SGAAELDRTE EYALGVIGVL ESYLSSINNI TKQSACVAMS KLLAEINNDD IKRLRNKEVP
TSPKIRIYNT VISYIDSNKR NTKQTIHLLK RLPADVLKKT IKNTIDIHNE INGNNQGDIN
VDEQNE
