ID   MATRX_HRSVB             Reviewed;         256 AA.
AC   O42049;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   23-FEB-2022, entry version 60.
DE   RecName: Full=Matrix protein;
DE   AltName: Full=M protein {ECO:0000250|UniProtKB:P0DOE7};
GN   Name=M;
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].
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: Plays a crucial role in virus assembly into filaments and
CC       budding. Early in infection, localizes in the nucleus where it inhibits
CC       host cell transcription through direct binding to host chromatin. Later
CC       in infection, traffics to the cytoplasm through the action of host CRM1
CC       to associate with inclusion bodies, the site of viral transcription and
CC       replication. During virus assembly and budding, acts as a bridge
CC       between the nucleocapsid and the lipid bilayer.
CC       {ECO:0000250|UniProtKB:P0DOE7}.
CC   -!- SUBUNIT: Forms dimers. Forms higher-order oligomers. Interacts with
CC       glycoprotein G (via N-terminus). Interacts with protein M2-1; this
CC       interaction directs the matrix protein localization to cytoplasmic
CC       inclusions comprising viral proteins L, N, P, and M2-1 and mediates the
CC       matrix protein association with the nucleocapsid. Interacts with host
CC       KPNB1; this interaction mediates nuclear import of the matrix protein
CC       early during infection. Interacts with host AP3M1; this interaction
CC       plays an essential role in trafficking the matrix protein in host
CC       cells. Interacts with host CAV1; this interaction probably facilitates
CC       viral budding. Interacts with host CFL1; this interaction probably
CC       facilitates viral replication. Interacts with host ZNF502; this
CC       interaction probably facilitates viral release.
CC       {ECO:0000250|UniProtKB:P0DOE7}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P0DOE7}. Host
CC       cytoplasm {ECO:0000250|UniProtKB:P0DOE7}. Host nucleus
CC       {ECO:0000250|UniProtKB:P0DOE7}. Host cell membrane
CC       {ECO:0000250|UniProtKB:P0DOE7}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P0DOE7}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P0DOE7}. Note=In the cytoplasm, associates with
CC       inclusion bodies. During bud formation, associates at the inner side of
CC       the plasma membrane of infected cells. {ECO:0000250|UniProtKB:P0DOE7}.
CC   -!- PTM: Phosphorylation is important for oligomerization.
CC       {ECO:0000250|UniProtKB:P0DOE7}.
CC   -!- SIMILARITY: Belongs to the pneumovirinae M protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF013254; AAB82433.1; -; Genomic_RNA.
DR   EMBL; AF013255; AAB82444.1; -; Genomic_RNA.
DR   RefSeq; NP_056860.1; NC_001781.1.
DR   SMR; O42049; -.
DR   PRIDE; O42049; -.
DR   GeneID; 1489822; -.
DR   KEGG; vg:1489822; -.
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:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:InterPro.
DR   GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR   GO; GO:0019068; P:virion assembly; IEA:InterPro.
DR   Gene3D; 2.70.20.30; -; 1.
DR   InterPro; IPR005056; Pneu_matrix.
DR   InterPro; IPR043062; Pneu_matrix_N.
DR   Pfam; PF03393; Pneumo_matrix; 1.
PE   3: Inferred from homology;
KW   Host cell membrane; Host cytoplasm; Host membrane; Host nucleus;
KW   Host-virus interaction; Membrane; Phosphoprotein; Reference proteome;
KW   Viral matrix protein; Virion.
FT   CHAIN           1..256
FT                   /note="Matrix protein"
FT                   /id="PRO_0000365789"
FT   REGION          1..110
FT                   /note="Interaction with M2-1"
FT                   /evidence="ECO:0000250|UniProtKB:P0DOE7"
FT   REGION          110..183
FT                   /note="Nuclear targeting and binding to host importin
FT                   KPNB1"
FT                   /evidence="ECO:0000250|UniProtKB:P0DOE7"
FT   MOTIF           194..206
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250|UniProtKB:P0DOE7"
FT   MOD_RES         205
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P0DOE7"
SQ   SEQUENCE   256 AA;  28620 MW;  C8407C2A441B837A CRC64;
     METYVNKLHE GSTYTAAVQY NVLEKDDDPA SLTIWVPMFQ SSVPADLLIK ELASINILVK
     QISTPKGPSL RVTINSRSAV LAQMPSNFII SANVSLDERS KLAYDVTTPC EIKACSLTCL
     KVKSMLTTVK DLTMKTFNPT HEIIALCEFE NIMTSKRVII PTYLRPISVK NKDLNSLENI
     ATTEFKNAIT NAKIIPYAGL VLVITVTDNK GAFKYIKPQS QFIVDLGAYL EKESIYYVTT
     NWKHTATRFS IKPLED