ID   MATRX_RABVH             Reviewed;         202 AA.
AC   Q8B6J7;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   29-SEP-2021, entry version 71.
DE   RecName: Full=Matrix protein;
DE   AltName: Full=Phosphoprotein M2;
GN   Name=M;
OS   Rabies virus (strain HEP-Flury) (RABV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=11296;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12505638; DOI=10.1016/s0166-0934(02)00249-5;
RA   Inoue K., Shoji Y., Kurane I., Iijima T., Sakai T., Morimoto K.;
RT   "An improved method for recovering rabies virus from cloned cDNA.";
RL   J. Virol. Methods 107:229-236(2003).
RN   [2]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH GLYCOPROTEIN.
RX   PubMed=10338196; DOI=10.1111/j.1348-0421.1999.tb02402.x;
RA   Nakahara K., Ohnuma H., Sugita S., Yasuoka K., Nakahara T., Tochikura T.S.,
RA   Kawai A.;
RT   "Intracellular behavior of rabies virus matrix protein (M) is determined by
RT   the viral glycoprotein (G).";
RL   Microbiol. Immunol. 43:259-270(1999).
RN   [3]
RP   INTERACTION WITH GLYCOPROTEIN.
RX   PubMed=14695448; DOI=10.1111/j.1348-0421.2003.tb03458.x;
RA   Nakahara T., Toriumi H., Irie T., Takahashi T., Ameyama S., Mizukoshi M.,
RA   Kawai A.;
RT   "Characterization of a slow-migrating component of the rabies virus matrix
RT   protein strongly associated with the viral glycoprotein.";
RL   Microbiol. Immunol. 47:977-988(2003).
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:0000269|PubMed:10338196};
CC       Peripheral membrane protein {ECO:0000269|PubMed:10338196}. Host
CC       endomembrane system {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}. Host cytoplasm {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; AB085828; BAC53867.1; -; Genomic_RNA.
DR   SMR; Q8B6J7; -.
DR   Proteomes; UP000006846; 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   1: Evidence at protein level;
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_0000295575"
FT   REGION          14..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          115..151
FT                   /note="Essential for glycoprotein binding"
FT   MOTIF           35..38
FT                   /note="PPXY motif"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   202 AA;  23160 MW;  AD27E960AE723BD8 CRC64;
     MNFLCKIVKN CRDEDTQKPS PASAPPDGDD LWLPPPEYVP LKELTSKKNM RNFCINGEVK
     VCSPNGYSFR ILRHILRSFD EIYSGNHRMI GLVKVVVGLA LSGAPAPEGM NWVYKLRRTL
     IFQWADSRGP LEGEELEHSQ EITWDDDTEF VGLQMRVSAR QCHIQGRIWC IDMNSRACQL
     WSDMSLQTQR SEEDKDSSLL LE