MATRX_ABLVB
ID MATRX_ABLVB Reviewed; 212 AA.
AC Q9QSP2;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 29-SEP-2021, entry version 65.
DE RecName: Full=Matrix protein;
DE AltName: Full=Phosphoprotein M2;
GN Name=M;
OS Australian bat lyssavirus (isolate Bat/AUS/1996) (ABLV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=446561;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9402; Pteropus alecto (Black flying fox).
OH NCBI_TaxID=328804; Pteropus conspicillatus (Spectacled flying fox).
OH NCBI_TaxID=9403; Pteropus poliocephalus (Grey-headed flying fox).
OH NCBI_TaxID=94117; Pteropus scapulatus (Little red flying fox).
OH NCBI_TaxID=446909; Saccolaimus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12367747; DOI=10.1016/s0168-1702(02)00056-4;
RA Gould A.R., Kattenbelt J.A., Gumley S.G., Lunt R.A.;
RT "Characterisation of an Australian bat lyssavirus variant isolated from an
RT insectivorous bat.";
RL Virus Res. 89:1-28(2002).
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 -!- CAUTION: It is uncertain whether Met-1 or Met-11 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AF081020; AAD47898.1; -; Genomic_RNA.
DR RefSeq; NP_478341.1; NC_003243.1.
DR SMR; Q9QSP2; -.
DR GeneID; 926732; -.
DR KEGG; vg:926732; -.
DR Proteomes; UP000006934; 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 Reference proteome; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral envelope protein;
KW Viral matrix protein; Viral release from host cell; Virion.
FT CHAIN 1..212
FT /note="Matrix protein"
FT /id="PRO_0000295567"
FT REGION 125..161
FT /note="Essential for glycoprotein binding"
FT /evidence="ECO:0000250"
FT MOTIF 45..48
FT /note="PPXY motif"
FT /evidence="ECO:0000255"
SQ SEQUENCE 212 AA; 24504 MW; 22BA5C658C189B68 CRC64;
MRKTVNTTDK MNFLRKIVRN CKDEDDQKPP LASTLPNDDD LWLPPPEYVP LTEITGKKNM
RNLCINGEVK VCSPNGYSFR ILRHILESLD EIYSGNHRMI GLVKVVMDLT LSGAPCPEGM
NWVYKLRRTL IFQWAESRGP LDGEELEYSQ EITWDDDSEF VGLQIRVSAR QCHIQGRIWC
INMNSRACQL WSDMSLKTQQ SEDHKNSSLL LE