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MATRX_EBLV2
ID   MATRX_EBLV2             Reviewed;         202 AA.
AC   A4UHQ5;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Matrix protein;
GN   Name=M;
OS   European bat lyssavirus 2 (strain Human/Scotland/RV1333/2002) (EBLV2).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Lyssavirus.
OX   NCBI_TaxID=453116;
OH   NCBI_TaxID=40674; Mammalia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=17374776; DOI=10.1099/vir.0.82692-0;
RA   Marston D.A., McElhinney L.M., Johnson N., Muller T., Conzelmann K.K.,
RA   Tordo N., Fooks A.R.;
RT   "Comparative analysis of the full genome sequence of European bat
RT   lyssavirus type 1 and type 2 with other lyssaviruses and evidence for a
RT   conserved transcription termination and polyadenylation motif in the G-L 3'
RT   non-translated region.";
RL   J. Gen. Virol. 88:1302-1314(2007).
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; EF157977; ABO65250.1; -; Genomic_RNA.
DR   RefSeq; YP_001285395.1; NC_009528.2.
DR   SMR; A4UHQ5; -.
DR   GeneID; 5219915; -.
DR   KEGG; vg:5219915; -.
DR   Proteomes; UP000007206; 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   Apoptosis; 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_0000299103"
FT   MOTIF           35..38
FT                   /note="PPXY motif"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   202 AA;  23139 MW;  90F17FA9D8CBAD95 CRC64;
     MNFLRKIVRG CRDEEDQKPA LVSAPPDDDD LWLPPPEYVP LTEITGRKNM RNFCVNGEVK
     VCSPNGYSFK ILRHILRSFD GVYSGNQRMR GLVKVVIGLA LSGGPIPEGM NWVYKVRRTL
     VFQWAESRGP LDGEELEYSQ EITWDDDSEF VGSQIRVSAR QCHIQGRIWC INMNSRACQL
     WSDMALKTQQ SDEDRNTSLL LE
 
 
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