ID   MATRX_RABVA             Reviewed;         202 AA.
AC   P15200; Q4F901;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   29-SEP-2021, entry version 82.
DE   RecName: Full=Matrix protein;
DE   AltName: Full=Phosphoprotein M2;
GN   Name=M;
OS   Rabies virus (strain PM1503/AVO1) (RABV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=11293;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate AVO1;
RX   PubMed=3147698; DOI=10.1016/0300-9084(88)90265-9;
RA   Poch O., Tordo N., Keith G.;
RT   "Sequence of the 3386 3' nucleotides of the genome of the AVO1 strain
RT   rabies virus: structural similarities in the protein regions involved in
RT   transcription.";
RL   Biochimie 70:1019-1029(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate PM1503;
RA   Stallkamp I., Lopez-Yomayuza C.C., Thiel H.-J.;
RT   "Characterization of rabies virus vaccine strains.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; X13357; CAA31736.1; -; Genomic_RNA.
DR   EMBL; DQ099525; AAZ07893.1; -; Genomic_RNA.
DR   PIR; S07816; MFVNAV.
DR   SMR; P15200; -.
DR   Proteomes; UP000008617; 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   Apoptosis; Host cytoplasm; Host membrane; Host-virus interaction; Membrane;
KW   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_0000222846"
FT   REGION          12..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT   VARIANT         27
FT                   /note="D -> Y (in strain: Isolate AVO1)"
FT   VARIANT         58
FT                   /note="D -> E (in strain: Isolate AVO1)"
FT   VARIANT         158
FT                   /note="S -> G (in strain: Isolate AVO1)"
FT   VARIANT         173
FT                   /note="T -> S (in strain: Isolate AVO1)"
SQ   SEQUENCE   202 AA;  23213 MW;  DA0A18C392BD00AE CRC64;
     MNVLRKIVKK CRDEDTQKPS PVSAPPDDDD LWLPPPEYVP LKELTSKKNM RNFCVNGDVK
     ACSPNGYSFR ILRHILRSFN EIYSGNHRMI GLVKVVVGLA LSGAPVPEGM NWVYKLRRTL
     IFQWADSRGP LEGEELEYSQ EITWDDDTEF VGLQIRVSAR QCHIQGRIWC INTNSRACQL
     WSDMSLQTQR SEEDKDSSLL LE