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P60172 (VSGP_EBOSB) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 43. 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
OrganismSudan ebolavirus (strain Boniface-76) (SEBOV) (Sudan Ebola virus)
Taxonomic identifier128948 [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]

Protein attributes

Sequence length372 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 Q66814). 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 – 372340Pre-small/secreted glycoprotein By similarity
PRO_0000037503
Chain33 – 324292Small/secreted glycoprotein By similarity
PRO_0000037504
Chain325 – 37248Delta-peptide By similarity
PRO_0000037505

Sites

Site324 – 3252Cleavage; by host furin By similarity

Amino acid modifications

Glycosylation401N-linked (GlcNAc...); by host Potential
Glycosylation2041N-linked (GlcNAc...); by host Potential
Glycosylation2081N-linked (GlcNAc...); by host Potential
Glycosylation2381N-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
P60172 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: ACD3E582EA6A9210

FASTA37242,547
        10         20         30         40         50         60 
MEGLSLLQLP RDKFRKSSFF VWVIILFQKA FSMPLGVVTN STLEVTEIDQ LVCKDHLAST 

        70         80         90        100        110        120 
DQLKSVGLNL EGSGVSTDIP SATKRWGFRS GVPPQVVSYE AGEWAENCYN LEIKKPDGSE 

       130        140        150        160        170        180 
CLPPPPDGVR GFPRCRYVHK AQGTGPCPGD YAFHKDGAFF LYDRLASTVI YRGVNFAEGV 

       190        200        210        220        230        240 
IAFLILAKPK ETFLQSPPIR EAANYTENTS SYYATSYLEY EIENFGAQHS TTLFKINNNT 

       250        260        270        280        290        300 
FVLLDRPHTP QFLFQLNDTI QLHQQLSNTT GKLIWTLDAN INADIGEWAF WENKKISPNN 

       310        320        330        340        350        360 
YVEKSCLSKL YRSTRQKTMM RHRRELQREE SPTGPPGSIR TWFQRIPLGW FHCTYQKGKQ 

       370 
HCRLRIRQKV EE 

« 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
U28134 Genomic RNA. Translation: AAB37097.1.

3D structure databases

ProteinModelPortalP60172.
SMRP60172. Positions 32-284.
ModBaseSearch...
MobiDBSearch...

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_EBOSB
AccessionPrimary (citable) accession number: P60172
Secondary accession number(s): Q89455
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: December 11, 2013
This is version 43 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