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P60171 (VSGP_EBOZ5) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 48. 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
OrganismZaire ebolavirus (strain Kikwit-95) (ZEBOV) (Zaire Ebola virus) [Complete proteome]
Taxonomic identifier128951 [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 length364 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 or two adenine nucleotides. The sequence displayed here is the small secreted glycoprotein, derived from the unedited RNA. The sequence derived from the +1A edited gives rise to the full-length transmembrane glycoprotein GP (AC P87666), the +2A edited RNA gives rise to the super small secreted glycoprotein ssGP (AC P0C773). 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 – 3232 Potential
Chain33 – 364332Pre-small/secreted glycoprotein By similarity
PRO_0000037509
Chain33 – 324292Small/secreted glycoprotein By similarity
PRO_0000037510
Chain325 – 36440Delta-peptide By similarity
PRO_0000037511

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
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

Natural variations

Natural variant471D → E in strain: Isolate Chain.

Sequences

Sequence LengthMass (Da)Tools
P60171 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 67376A454CE5F362

FASTA36441,175
        10         20         30         40         50         60 
MGVTGILQLP RDRFKRTSFF LWVIILFQRT FSIPLGVIHN STLQVSDVDK LVCRDKLSST 

        70         80         90        100        110        120 
NQLRSVGLNL EGNGVATDVP SATKRWGFRS GVPPKVVNYE AGEWAENCYN LEIKKPDGSE 

       130        140        150        160        170        180 
CLPAAPDGIR GFPRCRYVHK VSGTGPCAGD FAFHKEGAFF LYDRLASTVI YRGTTFAEGV 

       190        200        210        220        230        240 
VAFLILPQAK KDFFSSHPLR EPVNATEDPS SGYYSTTIRY QATGFGTNET EYLFEVDNLT 

       250        260        270        280        290        300 
YVQLESRFTP QFLLQLNETI YTSGKRSNTT GKLIWKVNPE IDTTIGEWAF WETKKTSLEK 

       310        320        330        340        350        360 
FAVKSCLSQL YQTEPKTSVV RVRRELLPTQ GPTQQLKTTK SWLQKIPLQW FKCTVKEGKL 


QCRI 

« 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]Chain P.S.G., Ichou M.A., Malfatti S.A., Hajjaj A., Vergez L.M., Paragas J., Do L.H., Jahrling P.B., Smith K.L., McCready P.M., Ibrahim M.S.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Isolate Chain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28077 Genomic RNA. Translation: AAB37094.1.
AY354458 Genomic RNA. Translation: AAQ55049.1.

3D structure databases

ProteinModelPortalP60171.
SMRP60171. Positions 32-281.
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_EBOZ5
AccessionPrimary (citable) accession number: P60171
Secondary accession number(s): O12421 expand/collapse secondary AC list , O12717, Q66801, Q66819, Q6V1Q6, Q9YMG3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: December 11, 2013
This is version 48 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