P60173 (VSGP_EBOSM) Reviewed, UniProtKB/Swiss-Prot
Last modified December 11, 2013. Version 43. History...
Names and origin
|Protein names||Recommended name:|
|Organism||Sudan ebolavirus (strain Maleo-79) (SEBOV) (Sudan Ebola virus)|
|Taxonomic identifier||128949 [NCBI]|
|Taxonomic lineage||Viruses › ssRNA negative-strand viruses › Mononegavirales › Filoviridae › Ebolavirus ›|
|Virus host||Epomops franqueti (Franquet's epauleted fruit bat) [TaxID: 77231]|
Homo sapiens (Human) [TaxID: 9606]
Myonycteris torquata (Little collared fruit bat) [TaxID: 77243]
|Sequence length||372 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at transcript level|
General annotation (Comments)
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.
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.
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.
Belongs to the filoviruses glycoprotein family.
Edited at position 295.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Signal peptide||1 – 32||32||Potential|
|Chain||33 – 372||340||Pre-small/secreted glycoprotein By similarity||PRO_0000037506|
|Chain||33 – 324||292||Small/secreted glycoprotein By similarity||PRO_0000037507|
|Chain||325 – 372||48||Delta-peptide By similarity||PRO_0000037508|
|Site||324 – 325||2||Cleavage; by host furin By similarity|
Amino acid modifications
|Glycosylation||40||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||204||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||208||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||238||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||257||1||N-linked (GlcNAc...); by host Potential|
|Glycosylation||268||1||N-linked (GlcNAc...); by host Potential|
|Disulfide bond||53||Interchain By similarity|
|Disulfide bond||108 ↔ 135||By similarity|
|Disulfide bond||121 ↔ 147||By similarity|
|Disulfide bond||306||Interchain By similarity|
|||"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.
|U23069 Genomic RNA. Translation: AAC54883.1.|
3D structure databases
|SMR||P60173. Positions 32-284. |
Protocols and materials databases
Family and domain databases
|InterPro||IPR014625. GPC_FiloV. |
|Pfam||PF01611. Filo_glycop. 1 hit. |
|PIRSF||PIRSF036874. GPC_FiloV. 1 hit. |
|Accession||Primary (citable) accession number: P60173|
Secondary accession number(s): Q89455
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families