ID   MATRX_TRTV              Reviewed;         254 AA.
AC   P31620;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   10-FEB-2021, entry version 46.
DE   RecName: Full=Matrix protein;
DE   AltName: Full=M protein {ECO:0000250|UniProtKB:P0DOE7};
GN   Name=M;
OS   Turkey rhinotracheitis virus (TRTV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Pneumoviridae; Metapneumovirus.
OX   NCBI_TaxID=11264;
OH   NCBI_TaxID=9103; Meleagris gallopavo (Wild turkey).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=UK/3B/85;
RX   PubMed=1733097; DOI=10.1016/0042-6822(92)90007-c;
RA   Yu Q., Davis P.J., Li J., Cavanagh D.;
RT   "Cloning and sequencing of the matrix protein (M) gene of turkey
RT   rhinotracheitis virus reveal a gene order different from that of
RT   respiratory syncytial virus.";
RL   Virology 186:426-434(1992).
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 to associate with inclusion bodies, the site of viral
CC       transcription and replication. During virus assembly and budding, acts
CC       as a bridge 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.
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   -!- SIMILARITY: Belongs to the pneumovirinae M protein family.
CC       {ECO:0000305}.
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DR   EMBL; X58639; CAA41496.1; -; mRNA.
DR   PIR; A40817; MFNZT3.
DR   SMR; P31620; -.
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; Membrane;
KW   Viral matrix protein; Virion.
FT   CHAIN           1..254
FT                   /note="Matrix protein"
FT                   /id="PRO_0000142779"
SQ   SEQUENCE   254 AA;  27595 MW;  A13223027B604AD9 CRC64;
     MESYIIDTYQ GVPYTAAVQV DLIEKDSNPA TLTVWFPLFQ SSTPAPVLLD QLKTLSITTQ
     YTASPEGPVL QVNAAAQGAA MSALPKKFAV SAAVALDEYS RLEFGTLTVC DVRSIYLTTL
     KPYGMVSKIM TDVRSVGRKT HDLIALCDFI DIEKGVPITI PAYIKAVSIK DSESATVEAA
     ISGEADQAIT QARIAPYAGL ILIMTMNNPK GIFKKLGAGM QVIVELGPYV QAESLGKICK
     TWNHQRTRYV LRSR