ID   MATRX_DMSVA             Reviewed;         222 AA.
AC   A7WNB1;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   23-FEB-2022, entry version 30.
DE   RecName: Full=Matrix protein;
GN   Name=M;
OS   Drosophila melanogaster sigma virus (isolate Drosophila/USA/AP30/2005)
OS   (DMelSV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Sigmavirus.
OX   NCBI_TaxID=666363;
OH   NCBI_TaxID=7227; Drosophila melanogaster (Fruit fly).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=AP30;
RX   PubMed=17725574; DOI=10.1111/j.1365-294x.2007.03460.x;
RA   Carpenter J.A., Obbard D.J., Maside X., Jiggins F.M.;
RT   "The recent spread of a vertically transmitted virus through populations of
RT   Drosophila melanogaster.";
RL   Mol. Ecol. 16:3947-3954(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=AP30;
RA   Jiggins F.M.;
RL   Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a major role in assembly and budding of virion, by
CC       recruiting cellular partners of the ESCRT complexes that play a key
CC       role in releasing the budding particle from the host membrane.
CC       Condensates the ribonucleocapsid core during virus assembly.
CC       {ECO:0000250|UniProtKB:P03519}.
CC   -!- SUBUNIT: Homomultimer. Interacts with viral nucleocapsid. Interacts
CC       with host TSG101. {ECO:0000250|UniProtKB:P03519}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:P03519};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P03519}. Host
CC       endomembrane system {ECO:0000250|UniProtKB:P03519}; Peripheral membrane
CC       protein {ECO:0000250|UniProtKB:P03519}. Host nucleus membrane
CC       {ECO:0000250|UniProtKB:P03519}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P03519}.
CC   -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC       essential for viral particle budding. They recruit proteins of the host
CC       ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC       ESCRT-associated proteins. M contains a PTAP/PSAP motif, which
CC       interacts with the UEV domain of TSG101.
CC       {ECO:0000250|UniProtKB:P03519}.
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DR   EMBL; AM689309; CAM84586.1; -; Genomic_RNA.
DR   RefSeq; YP_003126911.1; NC_013135.1.
DR   GeneID; 8363512; -.
DR   KEGG; vg:8363512; -.
DR   Proteomes; UP000029768; Genome.
DR   GO; GO:0044200; C:host cell nuclear 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:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
DR   GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW.
DR   InterPro; IPR009397; Vesiculo_matrix.
DR   Pfam; PF06326; Vesiculo_matrix; 1.
PE   3: Inferred from homology;
KW   Host membrane; Host nucleus; Host-virus interaction; Membrane;
KW   Reference proteome; Viral budding;
KW   Viral budding via the host ESCRT complexes; Viral matrix protein;
KW   Viral release from host cell; Virion.
FT   CHAIN           1..222
FT                   /note="Matrix protein"
FT                   /id="PRO_0000432064"
FT   MOTIF           46..49
FT                   /note="PTAP/PSAP motif"
SQ   SEQUENCE   222 AA;  25703 MW;  383382DB19E502CF CRC64;
     MNKMNQLVRF VKDTVAVRKP QSEDKSYLPI PSTIGGHEVN SPFAEPTAPS LGIIQPKCKR
     ADWLIKSHLT ITTNYEIKEW ETWDRAISDI LDLYDGNPVF KPILLFVYYV LAYNARKIPG
     PSNGVRYGAY FDELTTVWHA IPELMNQEID YSYNHRVLHR KIQYVISFKI QMSSTKRRTS
     PIESFIEVTS EGLKHTPQFT TILDRARFVY SLTGGRYVIH PF