Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q66811 (VSGP_EBOIC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 54. 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
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
OrganismIvory Coast ebolavirus (strain Cote d'Ivoire-94) (CIEBOV) (Cote d'Ivoire Ebola virus)
Taxonomic identifier128999 [NCBI]
Taxonomic lineageViruses › ssRNA negative-strand viruses › Mononegavirales › Filoviridae › Ebolavirus ›
Virus hostEpomops franqueti (Franquet's epauleted fruit bat) [TaxID: 77231]
Homo sapiens (Human) [TaxID: 9606]
Myonycteris torquata (Little collared fruit bat) [TaxID: 77243]

Protein attributes

Sequence length365 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 295.
Partially edited. RNA editing at this position consists of an insertion of one adenine nucleotide. The sequence displayed here is the small secreted glycoprotein, derived from the unedited RNA. The edited RNA gives rise to the full-length transmembrane glycoprotein (AC Q66810). Ref.1

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityRNA editing
   DomainSignal
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
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 – 3232 Potential
Chain33 – 365333Pre-small/secreted glycoprotein By similarity
PRO_0000037494
Chain33 – 324292Small/secreted glycoprotein By similarity
PRO_0000037495
Chain325 – 36541Delta-peptide By similarity
PRO_0000037496

Sites

Site324 – 3252Cleavage; by host furin By similarity

Amino acid modifications

Glycosylation401N-linked (GlcNAc...); by host Potential
Glycosylation2041N-linked (GlcNAc...); by host Potential
Glycosylation2281N-linked (GlcNAc...); by host Potential
Glycosylation2571N-linked (GlcNAc...); by host Potential
Glycosylation2681N-linked (GlcNAc...); by host Potential
Disulfide bond53Interchain By similarity
Disulfide bond108 ↔ 135 By similarity
Disulfide bond121 ↔ 147 By similarity
Disulfide bond306Interchain By similarity

Sequences

Sequence LengthMass (Da)Tools
Q66811 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D2D39579392F9C28

FASTA36541,690
        10         20         30         40         50         60 
MGASGILQLP RERFRKTSFF VWVIILFHKV FSIPLGVVHN NTLQVSDIDK FVCRDKLSST 

        70         80         90        100        110        120 
SQLKSVGLNL EGNGVATDVP TATKRWGFRA GVPPKVVNYE AGEWAENCYN LAIKKVDGSE 

       130        140        150        160        170        180 
CLPEAPEGVR DFPRCRYVHK VSGTGPCPGG LAFHKEGAFF LYDRLASTII YRGTTFAEGV 

       190        200        210        220        230        240 
IAFLILPKAR KDFFQSPPLH EPANMTTDPS SYYHTTTINY VVDNFGTNTT EFLFQVDHLT 

       250        260        270        280        290        300 
YVQLEARFTP QFLVLLNETI YSDNRRSNTT GKLIWKINPT VDTSMGEWAF WENKKTSQKP 

       310        320        330        340        350        360 
FQVKSCLSYL YQKPRTRSLT RQRRSLLPSP PTTTQAKTTK NWFQRIPLQW FRCKTSRERT 


QCQPQ

« 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U28006 Genomic RNA. Translation: AAB37092.1.

3D structure databases

ProteinModelPortalQ66811.
SMRQ66811. Positions 32-278.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_EBOIC
AccessionPrimary (citable) accession number: Q66811
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: April 3, 2013
This is version 54 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents