ID   MATRX_RABVB             Reviewed;         202 AA.
AC   Q66T63;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   29-SEP-2021, entry version 55.
DE   RecName: Full=Matrix protein;
DE   AltName: Full=Phosphoprotein M2;
GN   Name=M;
OS   Rabies virus (strain silver-haired bat-associated) (RABV) (SHBRV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=445793;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15520387; DOI=10.1073/pnas.0407289101;
RA   Faber M., Pulmanausahakul R., Nagao K., Prosniak M., Rice A.B.,
RA   Koprowski H., Schnell M.J., Dietzschold B.;
RT   "Identification of viral genomic elements responsible for rabies virus
RT   neuroinvasiveness.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:16328-16332(2004).
CC   -!- FUNCTION: Plays a major role in assembly, budding and uncoating of
CC       virion after membrane fusion. Completely covers the ribonucleoprotein
CC       coil and keep it in condensed bullet-shaped form. Inhibits viral
CC       transcription and stimulates replication. Plays a major role in early
CC       induction of TRAIL-mediated apoptosis in infected neurons.
CC       {ECO:0000250|UniProtKB:P16287}.
CC   -!- SUBUNIT: Homomultimer. Interacts with nucleoprotein and with the
CC       cytoplasmic domain of glycoprotein. Interacts with host ATP6V1A; this
CC       interaction plays an important role in virion uncoating after viral
CC       entry. {ECO:0000250|UniProtKB:P16287}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:P16287};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P16287}. Host
CC       endomembrane system {ECO:0000250|UniProtKB:P16287}; Peripheral membrane
CC       protein {ECO:0000250|UniProtKB:P16287}. Host cytoplasm
CC       {ECO:0000250|UniProtKB:P16287}.
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. Matrix protein contains one L domain: a PPXY
CC       motif which potentially interacts with the WW domain 3 of NEDD4 E3
CC       ubiquitin ligase (Potential). {ECO:0000305}.
CC   -!- MISCELLANEOUS: Most abundant protein in the virion. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lyssavirus matrix protein family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY705373; AAU11517.1; -; Genomic_RNA.
DR   SMR; Q66T63; -.
DR   Proteomes; UP000006845; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
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; 3.10.460.20; -; 1.
DR   InterPro; IPR006870; Rhabdo_M.
DR   InterPro; IPR038617; Rhabdovirus_M_sf.
DR   Pfam; PF04785; Rhabdo_M2; 1.
PE   3: Inferred from homology;
KW   Host cytoplasm; Host membrane; Host-virus interaction; Membrane;
KW   Phosphoprotein; Viral budding; Viral budding via the host ESCRT complexes;
KW   Viral envelope protein; Viral matrix protein; Viral release from host cell;
KW   Virion.
FT   CHAIN           1..202
FT                   /note="Matrix protein"
FT                   /id="PRO_0000295573"
FT   REGION          115..151
FT                   /note="Essential for glycoprotein binding"
FT                   /evidence="ECO:0000250"
FT   MOTIF           35..38
FT                   /note="PPXY motif"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   202 AA;  23288 MW;  BC17FDCA3C7EF4F7 CRC64;
     MNFLRKIVKT CRDEDTQKPP LVSAPPDDDD LWLPPPEYIP LKEITGKKNM RNFCVNGEVK
     VCGPNGYSFR TLRHILRSFD EIYSGNQRMI GLVKVVVGLA LSGAPVPEGM NWVYKLRRTL
     IFQWADSRGP LEGEELEYSQ EITWDDDTEF VGLEIRVSAR QCHIQGRIWC INMNSRACQF
     WSDMSLQTQR SEEDKDSSVL LE