MATRX_RABVA
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}.
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; 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