Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q66800 (VSGP_EBORR) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pre-small/secreted glycoprotein

Short name=pre-sGP

Cleaved into the following 2 chains:

  1. Small/secreted glycoprotein
    Short name=sGP
  2. Delta-peptide
Gene names
Name:GP
OrganismReston ebolavirus (strain Reston-89) (REBOV) (Reston Ebola virus) [Complete proteome]
Taxonomic identifier386032 [NCBI]
Taxonomic lineageVirusesssRNA negative-strand virusesMononegaviralesFiloviridaeEbolavirus
Virus hostEpomops franqueti (Franquet's epauleted fruit bat) [TaxID: 77231]
Homo sapiens (Human) [TaxID: 9606]
Myonycteris torquata (Little collared fruit bat) [TaxID: 77243]
Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

sGP seems to possess an anti-inflammatory activity as it can reverse the barrier-decreasing effects of TNF alpha. Might therefore contribute to the lack of inflammatory reaction seen during infection in spite the of extensive necrosis and massive virus production. Does not seem to be involved in activation of primary macrophages. Does not seem to interact specifically with neutrophils By similarity.

Delta-peptide does not seem to be involved in activation of primary macrophages By similarity.

Subunit structure

sGP is a homodimer; disulfide-linked. The homodimers are linked by two disulfide bonds in a parallel orientation. Delta-peptide is a monomer By similarity.

Subcellular location

Small/secreted glycoprotein: Secreted.

Delta-peptide: Secreted By similarity.

Post-translational modification

Pre-sGP is N-glycosylated. This precursor is processed into mature sGP and delta-peptide by host furin or furin-like proteases. The cleavage site corresponds to the furin optimal cleavage sequence [KR]-X-[KR]-R. Both cleavage fragments contain sialic acid, but only the delta-peptide is O-glycosylated By similarity.

Sequence similarities

Belongs to the filoviruses glycoprotein family.

RNA editing

Edited at position 296.
Partially edited. RNA editing at this position consists of an insertion of one or two adenine nucleotides. The sequence displayed here is the full-length transmembrane glycoprotein GP, derived from the +1A edited RNA. The unedited RNA gives rise to the small secreted glycoprotein sGP (AC Q66799), the +2A edited RNA gives rise to the super small secreted glycoprotein ssGP (AC P0C771). Ref.1

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityRNA editing
   DomainSignal
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 367334Pre-small/secreted glycoprotein By similarity
PRO_0000037497
Chain34 – 325292Small/secreted glycoprotein By similarity
PRO_0000037498
Chain326 – 36742Delta-peptide By similarity
PRO_0000037499

Sites

Site325 – 3262Cleavage; by host furin By similarity

Amino acid modifications

Glycosylation411N-linked (GlcNAc...); by host Potential
Glycosylation2051N-linked (GlcNAc...); by host Potential
Glycosylation2291N-linked (GlcNAc...); by host Potential
Glycosylation2391N-linked (GlcNAc...); by host Potential
Glycosylation2581N-linked (GlcNAc...); by host Potential
Glycosylation2691N-linked (GlcNAc...); by host Potential
Disulfide bond54Interchain By similarity
Disulfide bond109 ↔ 136 By similarity
Disulfide bond122 ↔ 148 By similarity
Disulfide bond307Interchain By similarity

Natural variations

Natural variant3121Y → H.

Sequences

Sequence LengthMass (Da)Tools
Q66800 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F3953243F5420C40

FASTA36741,771
        10         20         30         40         50         60 
MGSGYQLLQL PRERFRKTSF LVWVIILFQR AISMPLGIVT NSTLKATEID QLVCRDKLSS 

        70         80         90        100        110        120 
TSQLKSVGLN LEGNGIATDV PSATKRWGFR SGVPPKVVSY EAGEWAENCY NLEIKKSDGS 

       130        140        150        160        170        180 
ECLPLPPDGV RGFPRCRYVH KVQGTGPCPG DLAFHKNGAF FLYDRLASTV IYRGTTFAEG 

       190        200        210        220        230        240 
VVAFLILSEP KKHFWKATPA HEPVNTTDDS TSYYMTLTLS YEMSNFGGNE SNTLFKVDNH 

       250        260        270        280        290        300 
TYVQLDRPHT PQFLVQLNET LRRNNRLSNS TGRLTWTLDP KIEPDVGEWA FWETKKTFPN 

       310        320        330        340        350        360 
NFMEKTCISK FYQPTPTTPQ IRARRELSKE KLATTHPPTT PSWFQRIPLQ WFQCSLQDGQ 


RKCRPKV 

« Hide

References

[1]"The virion glycoproteins of Ebola viruses are encoded in two reading frames and are expressed through transcriptional editing."
Sanchez A., Trappier S.G., Mahy B.W.J., Peters C.J., Nichol S.T.
Proc. Natl. Acad. Sci. U.S.A. 93:3602-3607(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], RNA EDITING.
[2]Volchkov V.E.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]"Molecular characterization of an isolate from the 1989/90 epizootic of Ebola virus Reston among macaques imported into the United States."
Groseth A., Stroeher U., Theriault S., Feldmann H.
Virus Res. 87:155-163(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[4]"A reconstituted replication and transcription system for Ebola virus Reston and comparison with Ebola virus Zaire."
Boehmann Y., Enterlein S., Randolf A., Muehlberger E.I.
Virology 332:406-417(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Isolate Pennsylvania-89.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U23152 Genomic RNA. Translation: AAC54884.1.
AF034645 Genomic RNA. Translation: AAC24345.1.
AF522874 Genomic RNA. Translation: AAN04451.1.
AY769362 Genomic RNA. Translation: AAV48578.1.
RefSeqNP_690584.1. NC_004161.1.

3D structure databases

ProteinModelPortalQ66800.
SMRQ66800. Positions 33-285.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID955190.

Family and domain databases

InterProIPR014625. GPC_FiloV.
IPR002561. GPC_filovir-type_extra_dom.
[Graphical view]
PfamPF01611. Filo_glycop. 1 hit.
[Graphical view]
PIRSFPIRSF036874. GPC_FiloV. 1 hit.
ProtoNetSearch...

Entry information

Entry nameVSGP_EBORR
AccessionPrimary (citable) accession number: Q66800
Secondary accession number(s): Q5UAK7, Q8JPX7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: December 11, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families