VGLG_BDV1
ID VGLG_BDV1 Reviewed; 503 AA.
AC Q8BB27; Q88626;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 54.
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 1 (BoDV-1).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Bornaviridae; Orthobornavirus.
OX NCBI_TaxID=1714621;
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=7906311; DOI=10.1128/jvi.68.3.1382-1396.1994;
RA Cubitt B., Oldstone C., de la Torre J.C.;
RT "Sequence and genome organization of Borna disease virus.";
RL J. Virol. 68:1382-1396(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12208952; DOI=10.1128/jvi.76.19.9735-9743.2002;
RA Vahlenkamp T.W., Konrath A., Weber M., Muller H.;
RT "Persistence of Borna disease virus in naturally infected sheep.";
RL J. Virol. 76:9735-9743(2002).
RN [3]
RP CLEAVAGE BY HOST FURIN.
RC STRAIN=isolate H640;
RX PubMed=9557754; DOI=10.1128/jvi.72.5.4528-4533.1998;
RA Richt J.A., Furbringer T., Koch A., Pfeuffer I., Herden C.,
RA Bause-Niedrig I., Garten W.;
RT "Processing of the Borna disease virus glycoprotein gp94 by the subtilisin-
RT like endoprotease furin.";
RL J. Virol. 72:4528-4533(1998).
RN [4]
RP FUNCTION.
RC STRAIN=He80;
RX PubMed=19656886; DOI=10.1128/jvi.00990-09;
RA Clemente R., de la Torre J.C.;
RT "Cell entry of Borna disease virus follows a clathrin-mediated endocytosis
RT pathway that requires Rab5 and microtubules.";
RL J. Virol. 83:10406-10416(2009).
RN [5]
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. {ECO:0000269|PubMed:19656886}.
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:0000269|PubMed:19656886}.
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:0000250|UniProtKB:P52638}.
CC -!- SUBCELLULAR LOCATION: [Envelope glycoprotein p27]: Virion. Host cell
CC membrane; Peripheral membrane protein. Note=Appear to be associated
CC with infectious virions. {ECO:0000250|UniProtKB:P52638}.
CC -!- SUBCELLULAR LOCATION: [Envelope glycoprotein p29]: Virion. Host cell
CC membrane; Single-pass type I membrane protein. Note=Appear to be
CC associated with infectious virions. {ECO:0000250|UniProtKB:P52638}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Envelope glycoprotein p57 precursor;
CC IsoId=Q8BB27-1; Sequence=Displayed;
CC Name=Matrix protein;
CC IsoId=P0C794-1; Sequence=External;
CC Name=Large structural protein;
CC IsoId=Q8JMN0-1; 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:0000269|PubMed:9557754}.
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DR EMBL; L27077; AAA20666.1; -; Genomic_RNA.
DR EMBL; AY066023; AAL49985.1; -; Genomic_RNA.
DR Proteomes; UP000185272; 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 GO; GO:0019062; P:virion attachment to host cell; 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; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell; 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_0000405346"
FT CHAIN 23..249
FT /note="Envelope glycoprotein p27"
FT /id="PRO_0000405347"
FT CHAIN 250..503
FT /note="Envelope glycoprotein p29"
FT /id="PRO_0000405348"
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 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"
FT CONFLICT 242..245
FT /note="PRLK -> SKLR (in Ref. 2; AAA20666)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="V -> M (in Ref. 2; AAA20666)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 56704 MW; B3265E21197BB5BA CRC64;
MQLSMSFLIG FGTLVLALSA RTFDLQGLSC NTDSTPGLID LEIRRLCHTP TENVISCEVR
YLNHTTINLP AVHTSCLKYH CKTYWGFFGS YSADRIINRY TGTVKGCLNN SAPEDPFECN
WFYCCSAITT EICRCSITNV TVAVQTFPPF MYCSFADCST VSQQELESGK AMLSDGSTLT
YTPYILQSEV VNKTLNGTIL CNSSSKIVSF DEFRRSYSLA NGSYQSSSIN VTCVNYTSSC
RPRLKRRRRD TQQIEYLVHK LRPTLKDAWE DCEILQSLLL GVFGTGIASA SQFLRGWLNH
PDIIGYIVNG VGVVWQCHRV NVTFMAWNES TYYPPVDYNG RKYFLNDEGR LQTNTPEARP
GLKRVMWFGR YFLGTVGSGV KPRRIRYNKT SHDYHLEEFE ASLNMTPQTS IASGHETDPI
NHAYGTQADL LPYTRSSNIT STDTGSGWVH IGLPSFAFLN PLGWLRDLLA WAAWLGGVLY
LISLCVSLPA SFARRRRLGR WQE
