MATRX_ARAV
ID MATRX_ARAV Reviewed; 202 AA.
AC Q6X1D6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Matrix protein;
DE AltName: Full=Phosphoprotein M2;
GN Name=M;
OS Aravan virus (ARAV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=211977;
OH NCBI_TaxID=109482; Myotis blythii (Lesser mouse-eared 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}.
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DR EMBL; EF614259; AAP86774.1; -; Genomic_RNA.
DR RefSeq; YP_007641394.1; NC_020808.1.
DR SMR; Q6X1D6; -.
DR GeneID; 14857927; -.
DR KEGG; vg:14857927; -.
DR Proteomes; UP000007445; 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_0000295569"
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; 23092 MW; 91AAEEEE581FE834 CRC64;
MNILRKIVKS CKDEEDQKPA LVSAPPDDDD LWLPPPEYVP LTEITGKKNM RNFCVNGEIK
ICSPNGYSFR ILRHILKSFD GVYSGNRRMI GLVKVVIGLA LSGAPVPEGM NWVYKIRRTL
VFQWAESRGP LDGEELEYSQ EITWDDDSEF IGLQIRVSAR QCHIQGRVWC INMNSRACQL
WSDMSLKTQQ SDEDKNTSLL LE