ID   MATRX_ORSVW             Reviewed;         256 AA.
AC   Q84131;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   02-DEC-2020, entry version 59.
DE   RecName: Full=Matrix protein;
DE   AltName: Full=M protein {ECO:0000250|UniProtKB:P0DOE7};
GN   Name=M;
OS   Ovine respiratory syncytial virus (strain WSU 83-1578) (ORSV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Pneumoviridae; unclassified Pneumoviridae.
OX   NCBI_TaxID=79699;
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7996153; DOI=10.1099/0022-1317-75-12-3597;
RA   Alansari H.M., Potgieter L.N.D.;
RT   "Molecular cloning and sequence analysis of the phosphoprotein,
RT   nucleocapsid protein, matrix protein and 22K (M2) protein of the ovine
RT   respiratory syncytial virus.";
RL   J. Gen. Virol. 75:3597-3601(1994).
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; U02470; AAA96339.1; -; mRNA.
DR   SMR; Q84131; -.
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; Viral matrix protein; Virion.
FT   CHAIN           1..256
FT                   /note="Matrix protein"
FT                   /id="PRO_0000142747"
SQ   SEQUENCE   256 AA;  28726 MW;  D98814871B41071B CRC64;
     METYVNKLHE GSTYTAAVQY NVLEKDDDPA SLTIWVPMFQ SSISADLLIK ELINVNILVR
     QISTLKGPSL KIMINSRSAV LAQMPNKFTI SANVSLDERS KLAYDITTPC EIKACSLTCL
     KVKNMLTTVK DLTMKTFNPT HEIIALCEFE NIMTSKKVVI PTFLRSINVK AKDLDSLENI
     ATTEFKNAIT NAKIIPYAGL VLVITVTDNK GAFKYIKPQS QFIVDLGAYL EKESIYYVTT
     NWKHTATRFS IKPIED