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P52638 (VGLG_BDVV) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity.

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 By similarity.

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.

Envelope glycoprotein p27: Virion. Host cell membrane; Peripheral membrane protein. Note: Appear to be associated with infectious virions.

Envelope glycoprotein p29: Virion. Host cell membrane; Single-pass type I membrane protein. Note: Appear to be associated with infectious virions.

Post-translational modification

Glycosated; Stabilizes it.

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 By similarity.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Envelope glycoprotein p57 precursor (identifier: P52638-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Matrix protein (identifier: P0C795-1)

The sequence of this isoform can be found in the external entry P0C795.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Isoform Large structural protein (identifier: P52639-1)

The sequence of this isoform can be found in the external entry P52639.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 503481Envelope glycoprotein p57
PRO_0000045270
Chain23 – 249227Envelope glycoprotein p27
PRO_0000045271
Chain250 – 503254Envelope glycoprotein p29
PRO_0000045272

Regions

Topological domain23 – 467445Extracellular Potential
Transmembrane468 – 48821Helical; Potential
Topological domain489 – 50315Cytoplasmic Potential
Region274 – 31542Fusion peptide Potential

Sites

Site249 – 2502Cleavage; by host furin By similarity

Amino acid modifications

Glycosylation631N-linked (GlcNAc...); by host Potential
Glycosylation1091N-linked (GlcNAc...); by host Potential
Glycosylation1391N-linked (GlcNAc...); by host Potential
Glycosylation1921N-linked (GlcNAc...); by host Potential
Glycosylation1961N-linked (GlcNAc...); by host Potential
Glycosylation2021N-linked (GlcNAc...); by host Potential
Glycosylation2211N-linked (GlcNAc...); by host Potential
Glycosylation2301N-linked (GlcNAc...); by host Potential
Glycosylation2351N-linked (GlcNAc...); by host Potential
Glycosylation3211N-linked (GlcNAc...); by host Potential
Glycosylation3281N-linked (GlcNAc...); by host Potential
Glycosylation3881N-linked (GlcNAc...); by host Potential
Glycosylation4381N-linked (GlcNAc...); by host Potential

Sequences

Sequence LengthMass (Da)Tools
Isoform Envelope glycoprotein p57 precursor [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 081B55347DF91A08

FASTA50356,652
        10         20         30         40         50         60 
MQPSMSFLIG FGTLVLVLSA RTFDLQGLSC NTDSTPGLID LEIRRLCHTP TENVISCEVS 

        70         80         90        100        110        120 
YLNHTTISLP AVHTSCLKYH CKTYWGFFGS YSADRIINRY TGTVKGCLNN SAPEDPFECN 

       130        140        150        160        170        180 
WFYCCSAITT EICRCSITNV TVAVQTFPPF MYCSFADCST VSQQELESGK AMLSDGSTLT 

       190        200        210        220        230        240 
YTPYILQSEV VNKTLNGTIL CNSSSKIVSF DEFRRSYSLT NGSYQSSSIN VTCANYTSSC 

       250        260        270        280        290        300 
RPRLKRRRRD TQQIEYLVHK LRPTLKDAWE DCEILQSLLL GVFGTGIASA SQFLRSWLNH 

       310        320        330        340        350        360 
PDIIGYIVNG VGVVWQCHRV NVTFMAWNES TYYPPVDYNG RKYFLNDEGR LQTNTPEARP 

       370        380        390        400        410        420 
GLKRVMWFGR YFLGTVGSGV KPRRIRYNKT SHDYHLEEFE ASLNMTPQTS IASGHETDPI 

       430        440        450        460        470        480 
NHAYGTQADL LPYTRSSNIT STDTGSGWVH IGLPSFAFLN PLGWLRDLLA WAAWLGGVLY 

       490        500 
LISLCVSLPA SFARRRRLGR WQE

« Hide

Isoform Matrix protein [UniParc].

See P0C795.

––
Isoform Large structural protein [UniParc].

See P52639.

––

References

[1]"Genomic organization of Borna disease virus."
Briese T., Schneemann A., Lewis A.J., Park Y.-S., Kim S., Ludwig H., Lipkin W.I.
Proc. Natl. Acad. Sci. U.S.A. 91:4362-4366(1994) [PubMed: 8183914] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Conservation of coding potential and terminal sequences in four different isolates of Borna disease virus."
Pleschka S., Staeheli P., Kolodziejek J., Richt J.A., Nowotny N., Schwemmle M.
J. Gen. Virol. 82:2681-2690(2001) [PubMed: 11602780] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[3]"Characterization of Borna disease virus p56 protein, a surface glycoprotein involved in virus entry."
Gonzalez-Dunia D., Cubitt B., Grasser F.A., de la Torre J.C.
J. Virol. 71:3208-3218(1997) [PubMed: 9060684] [Abstract]
Cited for: CHARACTERIZATION.
[4]"Borna disease virus and infection in humans."
Ikuta K., Ibrahim M.S., Kobayashi T., Tomonaga K.
Front. Biosci. 7:470-495(2002) [PubMed: 11815287] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U04608 Genomic RNA. Translation: AAA20227.1.
AJ311521 Genomic RNA. Translation: CAC70638.1.
RefSeqNP_042023.1. NC_001607.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1494401.

Family and domain databases

InterProIPR009344. BDV_G.
[Graphical view]
PfamPF06208. BDV_G. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PMAP-CutDBP52638.

Entry information

Entry nameVGLG_BDVV
AccessionPrimary (citable) accession number: P52638
Secondary accession number(s): Q778R6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 21, 2011
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info