ID   MATRX_KHUV              Reviewed;         202 AA.
AC   Q6X1D2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   29-SEP-2021, entry version 63.
DE   RecName: Full=Matrix protein;
DE   AltName: Full=Phosphoprotein M2;
GN   Name=M;
OS   Khujand virus (KHUV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=237716;
OH   NCBI_TaxID=109479; Myotis mystacinus (Whiskered bat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=14602198; DOI=10.1016/s0168-1702(03)00217-x;
RA   Kuzmin I.V., Orciari L.A., Arai Y.T., Smith J.S., Hanlon C.A., Kameoka Y.,
RA   Rupprecht C.E.;
RT   "Bat lyssaviruses (Aravan and Khujand) from Central Asia: phylogenetic
RT   relationships according to N, P and G gene sequences.";
RL   Virus Res. 97:65-79(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=18514350; DOI=10.1016/j.virusres.2008.04.021;
RA   Kuzmin I.V., Wu X., Tordo N., Rupprecht C.E.;
RT   "Complete genomes of Aravan, Khujand, Irkut and West Caucasian bat viruses,
RT   with special attention to the polymerase gene and non-coding regions.";
RL   Virus Res. 136:81-90(2008).
CC   -!- FUNCTION: Plays a major role in assembly and budding of virion.
CC       Completely covers the ribonucleoprotein coil and keep it in condensed
CC       bullet-shaped form. Inhibits viral transcription and stimulates
CC       replication. Plays a major role in early induction of TRAIL-mediated
CC       apoptosis in infected neurons (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homomultimer. Interacts with nucleoprotein and with the
CC       cytoplasmic domain of glycoprotein (By 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. 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; EF614261; AAP86778.1; -; Genomic_RNA.
DR   RefSeq; YP_009094329.1; NC_025385.1.
DR   SMR; Q6X1D2; -.
DR   GeneID; 21011769; -.
DR   KEGG; vg:21011769; -.
DR   Proteomes; UP000136780; Genome.
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 membrane; Host-virus interaction; Membrane; Phosphoprotein;
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_0000295571"
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;  23022 MW;  ADEE48C4CCEC91A5 CRC64;
     MNFLRKIVKS CKDEEDQKPA LVSAPPDDDD LWLPPPESVP LTEISGKKNM RNFCINGEVK
     ICSPNGYSFK ILRHILKSFD GIYSGNRRMI GLVKVVIGLA LSGAPVPEGM NWVYKIRRTL
     VFQWAESRGP LDGEELEYSQ EITWDDDSEF IGLQIRVSAR QCHIQGRVWC INMNSRACQL
     WSDMSLKTQQ SDEDKNTSLL LE