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 11-DEC-2019, entry version 69. DE RecName: Full=Matrix M2-1; DE AltName: Full=Envelope-associated 22 kDa protein; GN Name=M2-1; OS Human respiratory syncytial virus B (strain B1). OC Viruses; Riboviria; Negarnaviricota; Haploviricotina; Monjiviricetes; OC 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 transcriptional elongation factor to prevent CC premature termination during transcription thus allowing complete CC synthesis of RSV mRNAs. Functions also as a processivity and CC antitermination factor to permit transit of the polymerase through CC intergenic regions to access promoter distal genes. Plays a role in the CC association of the matrix protein with the nucleocapsid, which CC initiates assembly and budding. Also, can activate NF-kappa-B through CC association with host RELA (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with protein M; this interaction directs M CC localization to cytoplasmic inclusions comprising viral proteins L, N, CC P, and M2-1 and mediates M association with the nucleocapsid. Interacts CC with protein P; this interaction is required for protein M2-1 anti- CC termination and elongation transcriptional activities. Interacts with CC protein N. Interacts with host RELA (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm. CC -!- DOMAIN: Contains a zinc-finger domain on its N-terminus essential for CC its antitermination function. {ECO:0000250}. CC -!- PTM: Phosphorylated by host in infected cells. CC -!- SIMILARITY: Belongs to the pneumovirinae 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; KW Host-virus interaction; Metal-binding; Phosphoprotein; Reference proteome; KW Virion; Zinc; Zinc-finger. FT CHAIN 1..195 FT /note="Matrix M2-1" FT /id="PRO_0000365791" FT ZN_FING 7..25 FT /note="C3H1-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723" FT MOD_RES 58 FT /note="Phosphoserine; by host" FT /evidence="ECO:0000250" FT MOD_RES 61 FT /note="Phosphoserine; by host" FT /evidence="ECO:0000250" 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 //