MATRX_RABVS
ID MATRX_RABVS Reviewed; 202 AA.
AC P16287; A3F5L7; A3F5R7; A3F5T2; P13616; Q6HA96;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 29-SEP-2021, entry version 90.
DE RecName: Full=Matrix protein;
DE AltName: Full=Phosphoprotein M2;
GN Name=M;
OS Rabies virus (strain SAD B19) (RABV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Lyssavirus.
OX NCBI_TaxID=11300;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=40674; Mammalia.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2139267; DOI=10.1016/0042-6822(90)90433-r;
RA Conzelmann K.-K., Cox J.H., Schneider L.G., Thiel H.-J.;
RT "Molecular cloning and complete nucleotide sequence of the attenuated
RT rabies virus SAD B19.";
RL Virology 175:485-499(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=SRV9;
RA Wang T., Zhang S., Hu R.;
RT "Analysis of the whole sequence of rabies virus vaccine strain SRV9.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate SAD B19, Isolate SAD Bern, Isolate SAD Bern original var 1,
RC Isolate SAD Bern original var 2, Isolate SAD Bern original var 3,
RC Isolate SAD Bern original var 4, Isolate SAD Bern original var 5,
RC Isolate SAD P5/88, Isolate SAD VA1, Isolate SAD1-3670 var 1,
RC Isolate SAD1-3670 var 2, and Isolate SAG 2;
RA Geue L., Schares S., Schnick C., Kliemt J., Beckert A., Hoffmann B.,
RA Freuling C., Marston D., McElhinney L., Fooks A., Zanoni R., Peterhans E.,
RA Cox J., Mueller T.;
RT "Complete nucleotide sequencing of SAD derivatives of attenuated rabies
RT virus vaccine strains.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP MUTAGENESIS OF ARG-58.
RX PubMed=14581544; DOI=10.1128/jvi.77.22.12074-12082.2003;
RA Finke S., Conzelmann K.-K.;
RT "Dissociation of rabies virus matrix protein functions in regulation of
RT viral RNA synthesis and virus assembly.";
RL J. Virol. 77:12074-12082(2003).
RN [5]
RP FUNCTION, AND INTERACTION WITH GLYCOPROTEIN.
RX PubMed=9847327; DOI=10.1128/jvi.73.1.242-250.1999;
RA Mebatsion T., Weiland F., Conzelmann K.K.;
RT "Matrix protein of rabies virus is responsible for the assembly and budding
RT of bullet-shaped particles and interacts with the transmembrane spike
RT glycoprotein G.";
RL J. Virol. 73:242-250(1999).
RN [6]
RP LATE-BUDDING DOMAIN, AND MUTAGENESIS OF TYR-38.
RX PubMed=10074141; DOI=10.1128/jvi.73.4.2921-2929.1999;
RA Harty R.N., Paragas J., Sudol M., Palese P.;
RT "A proline-rich motif within the matrix protein of vesicular stomatitis
RT virus and rabies virus interacts with WW domains of cellular proteins:
RT implications for viral budding.";
RL J. Virol. 73:2921-2929(1999).
RN [7]
RP FUNCTION.
RX PubMed=12771432; DOI=10.1099/vir.0.19128-0;
RA Finke S., Mueller-Waldeck R., Conzelmann K.K.;
RT "Rabies virus matrix protein regulates the balance of virus transcription
RT and replication.";
RL J. Gen. Virol. 84:1613-1621(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HOST ATP6V1A.
RX PubMed=33208464; DOI=10.1074/jbc.ra120.014190;
RA Liu X., Li F., Zhang J., Wang L., Wang J., Wen Z., Wang Z., Shuai L.,
RA Wang X., Ge J., Zhao D., Bu Z.;
RT "The ATPase ATP6V1A facilitates rabies virus replication by promoting
RT virion uncoating and interacting with the viral matrix protein.";
RL J. Biol. Chem. 296:100096-100096(2020).
CC -!- FUNCTION: Plays a major role in assembly, budding and uncoating of
CC virion after membrane fusion (PubMed:33208464). Completely covers the
CC ribonucleoprotein coil and keep it in condensed bullet-shaped form.
CC Inhibits viral transcription and stimulates replication. Plays a major
CC role in early induction of TRAIL-mediated apoptosis in infected neurons
CC (PubMed:12771432, PubMed:9847327). {ECO:0000269|PubMed:12771432,
CC ECO:0000269|PubMed:33208464, ECO:0000269|PubMed:9847327}.
CC -!- SUBUNIT: Homomultimer. Interacts with nucleoprotein and with the
CC cytoplasmic domain of glycoprotein (PubMed:9847327). Interacts with
CC host ATP6V1A; this interaction plays an important role in virion
CC uncoating after viral entry (PubMed:33208464).
CC {ECO:0000269|PubMed:33208464, ECO:0000269|PubMed:9847327}.
CC -!- SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein.
CC Host endomembrane system; Peripheral membrane protein. Host cytoplasm
CC {ECO:0000269|PubMed:33208464}.
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; M31046; AAA47201.1; -; Genomic_RNA.
DR EMBL; AF499686; AAT48625.1; -; Genomic_RNA.
DR EMBL; EF206708; ABN11298.1; -; Genomic_RNA.
DR EMBL; EF206709; ABN11303.1; -; Genomic_RNA.
DR EMBL; EF206710; ABN11308.1; -; Genomic_RNA.
DR EMBL; EF206711; ABN11313.1; -; Genomic_RNA.
DR EMBL; EF206712; ABN11318.1; -; Genomic_RNA.
DR EMBL; EF206713; ABN11323.1; -; Genomic_RNA.
DR EMBL; EF206714; ABN11328.1; -; Genomic_RNA.
DR EMBL; EF206715; ABN11333.1; -; Genomic_RNA.
DR EMBL; EF206716; ABN11338.1; -; Genomic_RNA.
DR EMBL; EF206717; ABN11343.1; -; Genomic_RNA.
DR EMBL; EF206718; ABN11348.1; -; Genomic_RNA.
DR EMBL; EF206719; ABN11353.1; -; Genomic_RNA.
DR EMBL; EF206720; ABN11358.1; -; Genomic_RNA.
DR PIR; C34746; MFVNSB.
DR SMR; P16287; -.
DR ELM; P16287; -.
DR TCDB; 9.A.73.3.1; the virus matrix protein (vmp) family.
DR Proteomes; UP000006363; Genome.
DR Proteomes; UP000007308; Genome.
DR Proteomes; UP000100286; Genome.
DR Proteomes; UP000107382; Genome.
DR Proteomes; UP000115894; Genome.
DR Proteomes; UP000118099; Genome.
DR Proteomes; UP000123862; Genome.
DR Proteomes; UP000132522; Genome.
DR Proteomes; UP000133682; Genome.
DR Proteomes; UP000142143; Genome.
DR Proteomes; UP000151156; Genome.
DR Proteomes; UP000167748; Genome.
DR Proteomes; UP000172072; Genome.
DR Proteomes; UP000174835; Genome.
DR Proteomes; UP000175378; 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:0032897; P:negative regulation of viral transcription; IMP:CACAO.
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 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..202
FT /note="Matrix protein"
FT /id="PRO_0000222851"
FT REGION 9..31
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 2
FT /note="N -> D (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 11
FT /note="R -> C (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 19
FT /note="S -> P (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 22
FT /note="A -> V (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 46
FT /note="G -> S (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 58
FT /note="R -> G (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 110
FT /note="L -> M (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 120
FT /note="F -> L (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 158
FT /note="I -> S (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT VARIANT 168
FT /note="V -> I (in strain: Isolate SAD1-3670 var 1 and
FT Isolate SAD1-3670 var 2)"
FT MUTAGEN 38
FT /note="Y->A: Complete loss of interaction with WW domain in
FT vitro."
FT /evidence="ECO:0000269|PubMed:10074141"
FT MUTAGEN 58
FT /note="R->G: Complete loss of viral transcription
FT inhibition."
FT /evidence="ECO:0000269|PubMed:14581544"
SQ SEQUENCE 202 AA; 23341 MW; 012A1C6C25237628 CRC64;
MNLLRKIVKN RRDEDTQKSS PASAPLDDDD LWLPPPEYVP LKELTGKKNM RNFCINGRVK
VCSPNGYSFR ILRHILKSFD EIYSGNHRMI GLVKVVIGLA LSGSPVPEGL NWVYKLRRTF
IFQWADSRGP LEGEELEYSQ EITWDDDTEF VGLQIRVIAK QCHIQGRVWC INMNPRACQL
WSDMSLQTQR SEEDKDSSLL LE
