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 05-OCT-2016, entry version 59. 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; ssRNA viruses; ssRNA negative-strand viruses; 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., RA Adamus J.E., Clements-Mann M.L., Harris D.O., Randolph V.B., RA Udem S.A., Murphy B.R., Sidhu M.S.; RT "Respiratory syncytial virus (RSV) SH and G proteins are not essential RT for viral replication in vitro: clinical evaluation and molecular RT characterization of a cold-passaged, attenuated RSV subgroup B RT 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 CC in the association of the matrix protein with the nucleocapsid, CC which initiates assembly and budding. Also, can activate NF-kappa- CC B through association with host RELA (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Interacts with protein M; this interaction directs M CC localization to cytoplasmic inclusions comprising viral proteins CC L, N, P, and M2-1 and mediates M association with the CC nucleocapsid. Interacts with protein P; this interaction is CC required for protein M2-1 anti-termination and elongation CC transcriptional activities. Interacts with protein N. Interacts CC 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 CC for 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 -!- SIMILARITY: Contains 1 C3H1-type zinc finger. CC {ECO:0000255|PROSITE-ProRule:PRU00723}. 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 GeneID; 1489826; -. DR KEGG; vg:1489826; -. DR Proteomes; UP000002472; 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 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; Complete proteome; KW Host cytoplasm; Host-virus interaction; Metal-binding; Phosphoprotein; KW Reference proteome; Virion; Zinc; Zinc-finger. FT CHAIN 1 195 Matrix M2-1. FT /FTId=PRO_0000365791. FT ZN_FING 7 25 C3H1-type. {ECO:0000255|PROSITE- FT ProRule:PRU00723}. FT MOD_RES 58 58 Phosphoserine; by host. {ECO:0000250}. FT MOD_RES 61 61 Phosphoserine; by host. {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 //