GLYCO_EBLV2
ID GLYCO_EBLV2 Reviewed; 524 AA.
AC A4UHQ6; Q49IT8; Q49IT9; Q49IU1; Q49IU2; Q49LL3;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Glycoprotein;
DE Flags: Precursor;
GN Name=G;
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].
RC STRAIN=Isolate Holland/G9018/1987, Isolate Holland/G9375/1993,
RC Isolate Holland/G94112/1989, and Isolate Switzerland/G9337/1993;
RX PubMed=16051841; DOI=10.1128/jvi.79.16.10487-10497.2005;
RA Davis P.L., Holmes E.C., Larrous F., Van der Poel W.H., Tjornehoj K.,
RA Alonso W.J., Bourhy H.;
RT "Phylogeography, population dynamics, and molecular evolution of European
RT bat lyssaviruses.";
RL J. Virol. 79:10487-10497(2005).
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 7-524.
RC STRAIN=Isolate England/RV628/1996;
RX PubMed=15964478; DOI=10.1016/j.vaccine.2005.03.037;
RA Brookes S.M., Parsons G., Johnson N., McElhinney L.M., Fooks A.R.;
RT "Rabies human diploid cell vaccine elicits cross-neutralising and cross-
RT protecting immune responses against European and Australian bat
RT lyssaviruses.";
RL Vaccine 23:4101-4109(2005).
CC -!- FUNCTION: Attaches the virus to host cellular receptor, inducing
CC endocytosis of the virion. In the endosome, the acidic pH induces
CC conformational changes in the glycoprotein trimer, which trigger fusion
CC between virus and cell membrane (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer. Interacts with matrix protein (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: Glycosylated and palmitoylated by host. Glycosylation is crucial
CC for glycoprotein export at the cell surface (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Arg-352 is highly involved in rabies virus
CC pathogenicity. Its mutation dramatically attenuates the virus (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lyssavirus glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; AY863343; AAX62810.1; -; Genomic_RNA.
DR EMBL; AY863344; AAX62811.1; -; Genomic_RNA.
DR EMBL; AY863346; AAX62813.1; -; Genomic_RNA.
DR EMBL; AY863347; AAX62814.1; -; Genomic_RNA.
DR EMBL; EF157977; ABO65251.1; -; Genomic_RNA.
DR EMBL; AY721613; AAW50816.1; -; Genomic_RNA.
DR RefSeq; YP_001285396.1; NC_009528.2.
DR SMR; A4UHQ6; -.
DR GeneID; 5219916; -.
DR KEGG; vg:5219916; -.
DR Proteomes; UP000007206; Genome.
DR GO; GO:0016021; C:integral component of 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 InterPro; IPR001903; Rhabd_glycop.
DR Pfam; PF00974; Rhabdo_glycop; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral envelope protein; Virion.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..524
FT /note="Glycoprotein"
FT /id="PRO_0000299100"
FT TOPO_DOM 20..459
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..524
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 503..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 480
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000250"
FT VARIANT 5
FT /note="A -> T (in strain: Isolate Switzerland/G9337/1993)"
FT VARIANT 142
FT /note="R -> K (in strain: Isolate Holland/G9018/1987)"
FT VARIANT 148
FT /note="K -> Q (in strain: Isolate Holland/G9018/1987)"
FT VARIANT 151
FT /note="V -> L (in strain: Isolate Switzerland/G9337/1993)"
FT VARIANT 160
FT /note="D -> N (in strain: Isolate Switzerland/G9337/1993)"
FT VARIANT 212
FT /note="T -> A (in strain: Isolate Switzerland/G9337/1993)"
FT VARIANT 267
FT /note="E -> A (in strain: Isolate Holland/G9375/1993)"
FT VARIANT 321
FT /note="S -> T (in strain: Isolate England/RV628/1996)"
FT VARIANT 336
FT /note="I -> V (in strain: Isolate Holland/G9018/1987 and
FT Isolate Holland/G94112/1989)"
SQ SEQUENCE 524 AA; 58544 MW; 17DDA79747B16069 CRC64;
MPFQAVLSAL LSALTLCVGK FPIYTIPDKL GPWSPIDIHH LSCPNNIVVE DEGCTTLTVF
SYMELKVGYI TTIKVNGFTC TGVVTEAETY TNFVGYVTTT FKRKHFRPSP SACRDAYSWK
TAGDPRYEES LHNPYPDSHW LRTVTTTKES VLIISPSVAD MDAYDKTLYS KIFLNGKCSG
VSQVSPFCST NHDYTIWMPE NPNPGVSCDI FTTSKGKKAT KDGKLCGFVD ERGLYKSLKG
ACKLKLCGIS GMRLMDGSWV SIQNHDEAKW CSPDQLVNIH DFHSDEVEHL IAEELVKKRE
ECLDALESIM TTKSISFRRL SHLRKLVPGF GKAYTIINKT LMEADAHYKS IREWTDVIPS
KGCLMAGGRC YPHHNGVFFN GIILSPDGHV LIPEMQSAML QQHIELLESS VIPLMHPLAD
PSTIFKKDDG AEDFVEVHLP DVQKQISGID LGLPEWKRYF LIGVSALAFL ALMIFIAACC
RRVKRKKRAK PNPVELIRKV SVTSQSGRPI PSWESYKVET GGQS
