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   02-SEP-2026, entry version 100.
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; Borna disease virus.
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 macaco 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   AlphaFoldDB; P52638; -.
DR   GlyCosmos; P52638; 13 sites, No reported glycans.
DR   Proteomes; UP000007804; Segment.
DR   GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; EXP:UniProtKB.
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
//