ID   MATRX_BRSVA             Reviewed;         256 AA.
AC   P24615; Q77KZ0; Q77L00;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   02-DEC-2020, entry version 72.
DE   RecName: Full=Matrix protein;
DE   AltName: Full=M protein {ECO:0000250|UniProtKB:P0DOE7};
GN   Name=M;
OS   Bovine respiratory syncytial virus (strain A51908) (BRS).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX   NCBI_TaxID=11247;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1856698; DOI=10.1099/0022-1317-72-7-1715;
RA   Samal S.K., Zamora M.;
RT   "Nucleotide sequence analysis of a matrix and small hydrophobic protein
RT   dicistronic mRNA of bovine respiratory syncytial virus demonstrates
RT   extensive sequence divergence of the small hydrophobic protein from that of
RT   human respiratory syncytial virus.";
RL   J. Gen. Virol. 72:1715-1720(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=A51908, and ATCC 51908;
RX   PubMed=11724268; DOI=10.1023/a:1011888019966;
RA   Yunus A.S., Khattar S.K., Collins P.L., Samal S.K.;
RT   "Rescue of bovine respiratory syncytial virus from cloned cDNA: entire
RT   genome sequence of BRSV strain A51908.";
RL   Virus Genes 23:157-164(2001).
CC   -!- FUNCTION: Plays a crucial role in virus assembly into filaments and
CC       budding. Early in infection, localizes in the nucleus where it may
CC       inhibit host cell transcription. Later in infection, traffics to the
CC       cytoplasm through the action of host CRM1 to associate with inclusion
CC       bodies, the site of viral transcription and replication. During virus
CC       assembly and budding, acts as a bridge between the nucleocapsid and the
CC       lipid bilayer. {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. {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; D01012; BAA00812.1; -; mRNA.
DR   EMBL; AF295543; AAL49396.1; -; Genomic_RNA.
DR   EMBL; AF295544; AAL49407.1; -; Genomic_RNA.
DR   PIR; JQ1178; MFNZBR.
DR   SMR; P24615; -.
DR   Proteomes; UP000007616; 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   2: Evidence at transcript level;
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_0000142746"
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"
FT   VARIANT         13
FT                   /note="I -> T (in strain: ATCC 51908)"
FT   VARIANT         47
FT                   /note="M -> L (in strain: ATCC 51908)"
FT   VARIANT         65
FT                   /note="P -> L (in strain: ATCC 51908)"
SQ   SEQUENCE   256 AA;  28714 MW;  300E0A10C19C5535 CRC64;
     METYVNKLHE GSIYTAAVQY NVIEKDDDPA SLTIWVPMFQ SSISADMLIK ELINVNILVR
     QISTPKGPSL KIMINSRSAV LAQMPSKFTI SANVSLDERS KLAYDITTPC EIKACSLTCL
     KVKNMLTTVK DLTMKTFNPT HEIIALCEFE NIMTSKRVVI PTFLRSINVK AKDLDSLENI
     ATTEFKNAIT NAKIIPYAGL VLVITVTDNK GAFKYIKPQS QFIVDLGAYL EKESIYYVTT
     NWKHTATKFS IKPIED