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   07-OCT-2020, entry version 70.
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; 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 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}.
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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: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
//