ID   MATRX_PIRYV             Reviewed;         229 AA.
AC   Q85212;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   29-SEP-2021, entry version 81.
DE   RecName: Full=Matrix protein;
GN   Name=M;
OS   Piry virus (PIRYV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Vesiculovirus.
OX   NCBI_TaxID=11274;
OH   NCBI_TaxID=126289; Gracilinanus microtarsus (Brazilian gracile mouse opossum).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1454546; DOI=10.1093/nar/20.21.5843;
RA   Barik S.;
RT   "The phosphoprotein (P) gene of the rhabdovirus Piry: its cloning,
RT   sequencing, and expression in Escherichia coli.";
RL   Nucleic Acids Res. 20:5843-5843(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8724858; DOI=10.1159/000150451;
RA   Brun G., Bao X., Prevec L.;
RT   "The relationship of Piry virus to other vesiculoviruses: a re-evaluation
RT   based on the glycoprotein gene sequence.";
RL   Intervirology 38:274-282(1995).
CC   -!- FUNCTION: Plays a major role in assembly and budding of virion.
CC       Condensates the ribonucleocapsid core during virus assembly. Shut off
CC       cellular transcription by inhibiting mRNA nuclear export through direct
CC       interaction with host RAE1-NUP98 complex. This shutoff presumably
CC       inhibit interferon signaling and thus establishment of antiviral state
CC       in virus infected cells. Induces cell-rounding, cytoskeleton
CC       disorganization and apoptosis in infected cell (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homomultimer. Interacts with viral nucleocapsid (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein.
CC       Host endomembrane system {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}.
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 two overlapping L domains: a PPXY
CC       motif which interacts with the WW domain 3 of NEDD4 and a PTAP/PSAP
CC       motif, which interacts with the UEV domain of TSG101 (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated by host. {ECO:0000250}.
CC   -!- MISCELLANEOUS: Most abundant protein in the virion. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the vesiculoviruses matrix protein family.
CC       {ECO:0000305}.
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DR   EMBL; D26175; BAA05162.1; -; Genomic_RNA.
DR   SMR; Q85212; -.
DR   GO; GO:0033645; C:host cell endomembrane system; 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   Gene3D; 3.10.460.10; -; 1.
DR   InterPro; IPR009397; Vesiculo_matrix.
DR   InterPro; IPR036711; VSV_matrix_sf.
DR   Pfam; PF06326; Vesiculo_matrix; 1.
DR   SUPFAM; SSF75404; SSF75404; 1.
PE   3: Inferred from homology;
KW   Apoptosis; Host membrane; Host-virus interaction; Membrane; Phosphoprotein;
KW   Viral budding; Viral budding via the host ESCRT complexes;
KW   Viral matrix protein; Viral release from host cell; Virion.
FT   CHAIN           1..229
FT                   /note="Matrix protein"
FT                   /id="PRO_0000287256"
FT   REGION          11..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           33..36
FT                   /note="PPXY motif"
FT   MOTIF           42..45
FT                   /note="PTAP/PSAP motif"
FT   COMPBIAS        11..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   229 AA;  26344 MW;  96FF865A99E383F9 CRC64;
     MKSIRQLLSL AKKEKKREKK SNHGSHSMEW ESPPSYNEIK SPSAPIFGYD YEDMEYLPTL
     GVQTLKLQYK CVLQVRSESP FTSYLDAVDN VANWEKQYNG FSGKKPFYRA VMVRAVQAMK
     ANPMSLQDGR SPEYTSEIEG RCLVFHSLGH IPPMMYMCEQ FTRDWSGRRN QGIVNVKIWV
     GVTDTLDNLD QIFDPKKHFS EEEMLSAATI LGLEVKKSSD NNYIISKSY