M21_HRSVB
ID M21_HRSVB Reviewed; 195 AA.
AC O42050;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 77.
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 Human respiratory syncytial virus B (strain B1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=79692;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=B1;
RX PubMed=9391135; DOI=10.1073/pnas.94.25.13961;
RA Karron R.A., Buonagurio D.A., Georgiu A.F., Whitehead S.S., Adamus J.E.,
RA Clements-Mann M.L., Harris D.O., Randolph V.B., Udem S.A., Murphy B.R.,
RA Sidhu M.S.;
RT "Respiratory syncytial virus (RSV) SH and G proteins are not essential for
RT viral replication in vitro: clinical evaluation and molecular
RT characterization of a cold-passaged, attenuated RSV subgroup B mutant.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13961-13966(1997).
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. Also, can activate
CC host NF-kappa-B through association with host RELA.
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 RELA.
CC Interacts with host PABPC1 (via C-terminus).
CC {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; AF013254; AAB82437.1; -; Genomic_RNA.
DR EMBL; AF013255; AAB82447.1; -; Genomic_RNA.
DR RefSeq; NP_056864.1; NC_001781.1.
DR SMR; O42050; -.
DR PRIDE; O42050; -.
DR GeneID; 1489826; -.
DR KEGG; vg:1489826; -.
DR Proteomes; UP000002472; Genome.
DR Proteomes; UP000180717; 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:0039652; P:induction by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
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 Activation of host NF-kappa-B by virus; Host cytoplasm; Host nucleus;
KW Host-virus interaction; Metal-binding; Phosphoprotein; Reference proteome;
KW RNA-binding; Transcription; Transcription antitermination;
KW Transcription regulation; Viral transcription; Virion; Zinc; Zinc-finger.
FT CHAIN 1..195
FT /note="Protein M2-1"
FT /id="PRO_0000365791"
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 REGION 172..194
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT SITE 8
FT /note="Involved in RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P04545"
FT SITE 9
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"
SQ SEQUENCE 195 AA; 22310 MW; BE231D88E00C2A01 CRC64;
MSRRNPCKFE IRGHCLNGRR CHYSHNYFEW PPHALLVRQN FMLNKILKSM DKSIDTLSEI
SGAAELDRTE EYALGIVGVL ESYIGSINNI TKQSACVAMS KLLIEINSDD IKKLRDNEEP
NSPKIRVYNT VISYIESNRK NNKQTIHLLK RLPADVLKKT IKNTLDIHKS IIISNPKEST
VNDQNDQTKN NDITG
