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 02-DEC-2020, entry version 71. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:0019012; C:virion; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0039652; P:activation by virus of host NF-kappaB transcription factor activity; IEA:UniProtKB-KW. DR GO; GO:0046782; P:regulation of viral transcription; IEA:InterPro. DR InterPro; IPR009452; Pneumovirus_M2. 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 //