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Envelope glycoprotein p57 (gp84) (gp94) [Cleaved into: Envelope glycoprotein p27; Envelope glycoprotein p29]

 VGLG_BDV1               Reviewed;         503 AA.
Q8BB27; Q88626;
08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
23-MAY-2018, entry version 38.
RecName: Full=Envelope glycoprotein p57;
AltName: Full=gp84;
AltName: Full=gp94;
Contains:
RecName: Full=Envelope glycoprotein p27;
Contains:
RecName: Full=Envelope glycoprotein p29;
Flags: Precursor;
Name=G;
Borna disease virus 1 (BoDV-1).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Bornaviridae; Orthobornavirus.
NCBI_TaxID=1714621;
NCBI_TaxID=9913; Bos taurus (Bovine).
NCBI_TaxID=9352; Bradypodidae (three-fingered sloths).
NCBI_TaxID=9925; Capra hircus (Goat).
NCBI_TaxID=9850; Cervidae (deer).
NCBI_TaxID=109474; Crocidura leucodon (Bicoloured white-toothed shrew) (Celebes shrew).
NCBI_TaxID=9788; Equidae (horses).
NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
NCBI_TaxID=56798; Hexaprotodon liberiensis (Pygmy hippopotamus) (Choeropsis liberiensis).
NCBI_TaxID=9844; Lama glama (Llama).
NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
NCBI_TaxID=9940; Ovis aries (Sheep).
NCBI_TaxID=8801; Struthio camelus (Common ostrich).
NCBI_TaxID=9455; Varecia variegata (Black-and-white ruffed lemur) (Lemur variegatus).
NCBI_TaxID=30538; Vicugna pacos (Alpaca) (Lama pacos).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=7906311;
Cubitt B., Oldstone C., de la Torre J.C.;
"Sequence and genome organization of Borna disease virus.";
J. Virol. 68:1382-1396(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=12208952; DOI=10.1128/JVI.76.19.9735-9743.2002;
Vahlenkamp T.W., Konrath A., Weber M., Muller H.;
"Persistence of Borna disease virus in naturally infected sheep.";
J. Virol. 76:9735-9743(2002).
[3]
CLEAVAGE BY HOST FURIN.
STRAIN=isolate H640;
PubMed=9557754;
Richt J.A., Furbringer T., Koch A., Pfeuffer I., Herden C.,
Bause-Niedrig I., Garten W.;
"Processing of the Borna disease virus glycoprotein gp94 by the
subtilisin-like endoprotease furin.";
J. Virol. 72:4528-4533(1998).
[4]
FUNCTION.
STRAIN=He80;
PubMed=19656886; DOI=10.1128/JVI.00990-09;
Clemente R., de la Torre J.C.;
"Cell entry of Borna disease virus follows a clathrin-mediated
endocytosis pathway that requires Rab5 and microtubules.";
J. Virol. 83:10406-10416(2009).
[5]
REVIEW.
PubMed=11815287; DOI=10.2741/A789;
Ikuta K., Ibrahim M.S., Kobayashi T., Tomonaga K.;
"Borna disease virus and infection in humans.";
Front. Biosci. 7:470-495(2002).
-!- FUNCTION: Unprocessed envelope protein p57 is thought to be
involved in attachment of the virus to its cell surface receptor.
This attachment induces virion internalization predominantly
through clathrin-dependent endocytosis.
{ECO:0000269|PubMed:19656886}.
-!- FUNCTION: Envelope protein p27 and p29 presumably linked by
disulfide bond are the viral type II fusion protein, involved in
pH-dependent fusion within early endosomes after internalization
of the virion by endocytosis. {ECO:0000269|PubMed:19656886}.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein p57: Host endoplasmic
reticulum membrane; Single-pass type I membrane protein.
Note=Accumulates in the endoplasmic reticulum when unprocessed,
whereas cleaved products reaches cell surface.
{ECO:0000250|UniProtKB:P52638}.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein p27: Virion. Host cell
membrane; Peripheral membrane protein. Note=Appear to be
associated with infectious virions.
{ECO:0000250|UniProtKB:P52638}.
-!- SUBCELLULAR LOCATION: Envelope glycoprotein p29: Virion. Host cell
membrane; Single-pass type I membrane protein. Note=Appear to be
associated with infectious virions.
{ECO:0000250|UniProtKB:P52638}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Envelope glycoprotein p57 precursor;
IsoId=Q8BB27-1; Sequence=Displayed;
Name=Matrix protein;
IsoId=P0C794-1; Sequence=External;
Name=Large structural protein;
IsoId=Q8JMN0-1; Sequence=External;
-!- PTM: Glycosated; Stabilizes it.
-!- PTM: A portion of p57 is cleaved into p27 and p29. p27 and p29 are
called gp43 when glycosylated, as they seem to have the same
molecular weight. {ECO:0000269|PubMed:9557754}.
-----------------------------------------------------------------------
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EMBL; L27077; AAA20666.1; -; Genomic_RNA.
EMBL; AY066023; AAL49985.1; -; Genomic_RNA.
SMR; Q8BB27; -.
OrthoDB; VOG09000005; -.
Proteomes; UP000185272; Genome.
GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR009344; BDV_G.
Pfam; PF06208; BDV_G; 1.
1: Evidence at protein level;
Alternative splicing; Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Complete proteome;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host endoplasmic reticulum; Host membrane;
Host-virus interaction; Membrane; Signal; Transmembrane;
Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 503 Envelope glycoprotein p57.
/FTId=PRO_0000405346.
CHAIN 23 249 Envelope glycoprotein p27.
/FTId=PRO_0000405347.
CHAIN 250 503 Envelope glycoprotein p29.
/FTId=PRO_0000405348.
TOPO_DOM 23 467 Extracellular. {ECO:0000255}.
TRANSMEM 468 488 Helical. {ECO:0000255}.
TOPO_DOM 489 503 Cytoplasmic. {ECO:0000255}.
REGION 274 315 Fusion peptide. {ECO:0000255}.
COMPBIAS 246 249 Poly-Arg. {ECO:0000255}.
COMPBIAS 494 497 Poly-Arg. {ECO:0000255}.
SITE 249 250 Cleavage; by host furin.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 139 139 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 202 202 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 221 221 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 321 321 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 328 328 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 388 388 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 438 438 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CONFLICT 242 245 PRLK -> SKLR (in Ref. 2; AAA20666).
{ECO:0000305}.
CONFLICT 282 282 V -> M (in Ref. 2; AAA20666).
{ECO:0000305}.
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


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