VGLG_BDVV
ID VGLG_BDVV Reviewed; 503 AA.
AC P52638; Q778R6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 23-FEB-2022, entry version 92.
DE RecName: Full=Envelope glycoprotein p57;
DE AltName: Full=gp84;
DE AltName: Full=gp94;
DE Contains:
DE RecName: Full=Envelope glycoprotein p27;
DE Contains:
DE RecName: Full=Envelope glycoprotein p29;
DE Flags: Precursor;
GN Name=G;
OS Borna disease virus (strain V) (BDV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Bornaviridae; unclassified Bornaviridae.
OX NCBI_TaxID=928296;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9352; Bradypodidae (three-fingered sloths).
OH NCBI_TaxID=9925; Capra hircus (Goat).
OH NCBI_TaxID=9850; Cervidae (deer).
OH NCBI_TaxID=109474; Crocidura leucodon (Bicoloured white-toothed shrew) (Celebes shrew).
OH NCBI_TaxID=9788; Equidae (horses).
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH NCBI_TaxID=56798; Hexaprotodon liberiensis (Pygmy hippopotamus) (Choeropsis liberiensis).
OH NCBI_TaxID=9844; Lama glama (Llama).
OH NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
OH NCBI_TaxID=9940; Ovis aries (Sheep).
OH NCBI_TaxID=8801; Struthio camelus (Common ostrich).
OH NCBI_TaxID=9455; Varecia variegata (Black-and-white ruffed lemur) (Lemur variegatus).
OH NCBI_TaxID=30538; Vicugna pacos (Alpaca) (Lama pacos).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8183914; DOI=10.1073/pnas.91.10.4362;
RA Briese T., Schneemann A., Lewis A.J., Park Y.-S., Kim S., Ludwig H.,
RA Lipkin W.I.;
RT "Genomic organization of Borna disease virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:4362-4366(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11602780; DOI=10.1099/0022-1317-82-11-2681;
RA Pleschka S., Staeheli P., Kolodziejek J., Richt J.A., Nowotny N.,
RA Schwemmle M.;
RT "Conservation of coding potential and terminal sequences in four different
RT isolates of Borna disease virus.";
RL J. Gen. Virol. 82:2681-2690(2001).
RN [3]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=9060684; DOI=10.1128/jvi.71.4.3208-3218.1997;
RA Gonzalez-Dunia D., Cubitt B., Grasser F.A., de la Torre J.C.;
RT "Characterization of Borna disease virus p56 protein, a surface
RT glycoprotein involved in virus entry.";
RL J. Virol. 71:3208-3218(1997).
RN [4]
RP REVIEW.
RX PubMed=11815287; DOI=10.2741/a789;
RA Ikuta K., Ibrahim M.S., Kobayashi T., Tomonaga K.;
RT "Borna disease virus and infection in humans.";
RL Front. Biosci. 7:470-495(2002).
CC -!- FUNCTION: Unprocessed envelope protein p57 is thought to be involved in
CC attachment of the virus to its cell surface receptor. This attachment
CC induces virion internalization predominantly through clathrin-dependent
CC endocytosis (By similarity). {ECO:0000250|UniProtKB:Q8BB27}.
CC -!- FUNCTION: Envelope protein p27 and p29 presumably linked by disulfide
CC bond are the viral type II fusion protein, involved in pH-dependent
CC fusion within early endosomes after internalization of the virion by
CC endocytosis. {ECO:0000250|UniProtKB:Q8BB27}.
CC -!- SUBCELLULAR LOCATION: [Envelope glycoprotein p57]: Host endoplasmic
CC reticulum membrane; Single-pass type I membrane protein.
CC Note=Accumulates in the endoplasmic reticulum when unprocessed, whereas
CC cleaved products reaches cell surface. {ECO:0000269|PubMed:9060684}.
CC -!- SUBCELLULAR LOCATION: [Envelope glycoprotein p27]: Virion. Host cell
CC membrane {ECO:0000269|PubMed:9060684}; Peripheral membrane protein.
CC Note=Appear to be associated with infectious virions.
CC {ECO:0000269|PubMed:9060684}.
CC -!- SUBCELLULAR LOCATION: [Envelope glycoprotein p29]: Virion. Host cell
CC membrane {ECO:0000269|PubMed:9060684}; Single-pass type I membrane
CC protein. Note=Appear to be associated with infectious virions.
CC {ECO:0000269|PubMed:9060684}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Envelope glycoprotein p57 precursor;
CC IsoId=P52638-1; Sequence=Displayed;
CC Name=Matrix protein;
CC IsoId=P0C795-1; Sequence=External;
CC Name=Large structural protein;
CC IsoId=P52639-1; Sequence=External;
CC -!- PTM: Glycosated; Stabilizes it.
CC -!- PTM: A portion of p57 is cleaved into p27 and p29. p27 and p29 are
CC called gp43 when glycosylated, as they seem to have the same molecular
CC weight. {ECO:0000250|UniProtKB:Q8BB27}.
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DR EMBL; U04608; AAA20227.1; -; Genomic_RNA.
DR EMBL; AJ311521; CAC70638.1; -; Genomic_RNA.
DR RefSeq; NP_042023.1; NC_001607.1.
DR GeneID; 26799166; -.
DR KEGG; vg:26799166; -.
DR Proteomes; UP000007804; Genome.
DR Proteomes; UP000124375; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR InterPro; IPR009344; BDV_G.
DR Pfam; PF06208; BDV_G; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Clathrin-mediated endocytosis of virus by host;
KW Cleavage on pair of basic residues;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host endoplasmic reticulum; Host membrane;
KW Host-virus interaction; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..503
FT /note="Envelope glycoprotein p57"
FT /id="PRO_0000045270"
FT CHAIN 23..249
FT /note="Envelope glycoprotein p27"
FT /id="PRO_0000045271"
FT CHAIN 250..503
FT /note="Envelope glycoprotein p29"
FT /id="PRO_0000045272"
FT TOPO_DOM 23..467
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 489..503
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 274..315
FT /note="Fusion peptide"
FT /evidence="ECO:0000255"
FT SITE 249..250
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000250"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 503 AA; 56652 MW; 081B55347DF91A08 CRC64;
MQPSMSFLIG FGTLVLVLSA RTFDLQGLSC NTDSTPGLID LEIRRLCHTP TENVISCEVS
YLNHTTISLP AVHTSCLKYH CKTYWGFFGS YSADRIINRY TGTVKGCLNN SAPEDPFECN
WFYCCSAITT EICRCSITNV TVAVQTFPPF MYCSFADCST VSQQELESGK AMLSDGSTLT
YTPYILQSEV VNKTLNGTIL CNSSSKIVSF DEFRRSYSLT NGSYQSSSIN VTCANYTSSC
RPRLKRRRRD TQQIEYLVHK LRPTLKDAWE DCEILQSLLL GVFGTGIASA SQFLRSWLNH
PDIIGYIVNG VGVVWQCHRV NVTFMAWNES TYYPPVDYNG RKYFLNDEGR LQTNTPEARP
GLKRVMWFGR YFLGTVGSGV KPRRIRYNKT SHDYHLEEFE ASLNMTPQTS IASGHETDPI
NHAYGTQADL LPYTRSSNIT STDTGSGWVH IGLPSFAFLN PLGWLRDLLA WAAWLGGVLY
LISLCVSLPA SFARRRRLGR WQE
