ID   MATRX_HRSS2             Reviewed;         256 AA.
AC   P0DOE6; P03419; Q77YB3;
DT   12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2017, sequence version 1.
DT   03-AUG-2022, entry version 17.
DE   RecName: Full=Matrix protein;
DE   AltName: Full=M protein {ECO:0000250|UniProtKB:P0DOE7};
GN   Name=M;
OS   Human respiratory syncytial virus A (strain S-2) (HRSV-S2).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX   NCBI_TaxID=410078;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=9032893; DOI=10.1016/s0264-410x(96)00136-3;
RA   Tolley K.P., Marriott A.C., Simpson A., Plows D.J., Matthews D.A.,
RA   Longhurst S.J., Evans J.E., Johnson J.L., Cane P.A., Easton A.J.,
RA   Pringle C.R.;
RT   "Identification of mutations contributing to the reduced virulence of a
RT   modified strain of respiratory syncytial virus.";
RL   Vaccine 14:1637-1646(1996).
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. 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; U39662; AAC57024.1; -; Genomic_RNA.
DR   SMR; P0DOE6; -.
DR   Proteomes; UP000113393; 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_0000439633"
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;  28714 MW;  1E70706D65416BA0 CRC64;
     METYVNKLHE GSTYTAAVQY NVLEKDDDPA SLTIWVPMFQ SSMPADLLIK ELANVNILVK
     QISTPKGPSL RVMINSRSAV LAQMPSKFTI CANVSLDERS KLAYDVTTPC EIKACSLTCL
     KSKNMLTTVK DLTMKTLNPT HDIIALCEFE NIVTSKKVII PTYLRSISVR NKDLNTLENI
     TTTEFKNAIT NAKIIPYSGL LLVITVTDNK GAFKYIKPQS QFIVDLGAYL EKESIYYVTT
     NWKHTATRFA IKPMED