ID   MATRX_HMPVC             Reviewed;         254 AA.
AC   Q6WB99;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   23-FEB-2022, entry version 49.
DE   RecName: Full=Matrix protein;
DE   AltName: Full=M protein {ECO:0000250|UniProtKB:P0DOE7};
GN   Name=M;
OS   Human metapneumovirus (strain CAN97-83) (HMPV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Pneumoviridae; Metapneumovirus.
OX   NCBI_TaxID=694067;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=14592754; DOI=10.1016/s0042-6822(03)00528-2;
RA   Biacchesi S., Skiadopoulos M.H., Boivin G., Hanson C.T., Murphy B.R.,
RA   Collins P.L., Buchholz U.J.;
RT   "Genetic diversity between human metapneumovirus subgroups.";
RL   Virology 315:1-9(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=16306583; DOI=10.1128/jvi.79.24.15114-15122.2005;
RA   Pham Q.N., Biacchesi S., Skiadopoulos M.H., Murphy B.R., Collins P.L.,
RA   Buchholz U.J.;
RT   "Chimeric recombinant human metapneumoviruses with the nucleoprotein or
RT   phosphoprotein open reading frame replaced by that of avian metapneumovirus
RT   exhibit improved growth in vitro and attenuation in vivo.";
RL   J. Virol. 79:15114-15122(2005).
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.
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; AY297749; AAQ67694.1; -; Genomic_RNA.
DR   RefSeq; YP_012607.1; NC_004148.2.
DR   SMR; Q6WB99; -.
DR   PRIDE; Q6WB99; -.
DR   Proteomes; UP000001398; 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..254
FT                   /note="Matrix protein"
FT                   /id="PRO_0000394811"
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   254 AA;  27612 MW;  3D68234A43355FF7 CRC64;
     MESYLVDTYQ GIPYTAAVQV DLVEKDLLPA SLTIWFPLFQ ANTPPAVLLD QLKTLTITTL
     YAASQSGPIL KVNASAQGAA MSVLPKKFEV NATVALDEYS KLEFDKLTVC EVKTVYLTTM
     KPYGMVSKFV SSAKPVGKKT HDLIALCDFM DLEKNTPVTI PAFIKSVSIK ESESATVEAA
     ISSEADQALT QAKIAPYAGL IMIMTMNNPK GIFKKLGAGT QVIVELGAYV QAESISKICK
     TWSHQGTRYV LKSR