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P60172

- VSGP_EBOSB

UniProt

P60172 - VSGP_EBOSB

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Protein

Pre-small/secreted glycoprotein

Gene
GP
Organism
Sudan ebolavirus (strain Boniface-76) (SEBOV) (Sudan Ebola virus)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei324 – 3252Cleavage; by host furin By similarity

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-small/secreted glycoprotein
Short name:
pre-sGP
Cleaved into the following 2 chains:
Gene namesi
Name:GP
OrganismiSudan ebolavirus (strain Boniface-76) (SEBOV) (Sudan Ebola virus)
Taxonomic identifieri128948 [NCBI]
Taxonomic lineageiVirusesssRNA negative-strand virusesMononegaviralesFiloviridaeEbolavirus
Virus hostiEpomops franqueti (Franquet's epauleted fruit bat) [TaxID: 77231]
Homo sapiens (Human) [TaxID: 9606]
Myonycteris torquata (Little collared fruit bat) [TaxID: 77243]

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232 Reviewed predictionAdd
BLAST
Chaini33 – 372340Pre-small/secreted glycoprotein By similarityPRO_0000037503Add
BLAST
Chaini33 – 324292Small/secreted glycoprotein By similarityPRO_0000037504Add
BLAST
Chaini325 – 37248Delta-peptide By similarityPRO_0000037505Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi53 – 53Interchain By similarity
Disulfide bondi108 ↔ 135 By similarity
Disulfide bondi121 ↔ 147 By similarity
Glycosylationi204 – 2041N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi208 – 2081N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi238 – 2381N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi257 – 2571N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi268 – 2681N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi306 – 306Interchain By similarity

Post-translational modificationi

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.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

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.

Structurei

3D structure databases

ProteinModelPortaliP60172.
SMRiP60172. Positions 32-284.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR014625. GPC_FiloV.
IPR002561. GPC_filovir-type_extra_dom.
[Graphical view]
PfamiPF01611. Filo_glycop. 1 hit.
[Graphical view]
PIRSFiPIRSF036874. GPC_FiloV. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P60172-1 [UniParc]FASTAAdd to Basket

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MEGLSLLQLP RDKFRKSSFF VWVIILFQKA FSMPLGVVTN STLEVTEIDQ    50
LVCKDHLAST DQLKSVGLNL EGSGVSTDIP SATKRWGFRS GVPPQVVSYE 100
AGEWAENCYN LEIKKPDGSE CLPPPPDGVR GFPRCRYVHK AQGTGPCPGD 150
YAFHKDGAFF LYDRLASTVI YRGVNFAEGV IAFLILAKPK ETFLQSPPIR 200
EAANYTENTS SYYATSYLEY EIENFGAQHS TTLFKINNNT FVLLDRPHTP 250
QFLFQLNDTI QLHQQLSNTT GKLIWTLDAN INADIGEWAF WENKKISPNN 300
YVEKSCLSKL YRSTRQKTMM RHRRELQREE SPTGPPGSIR TWFQRIPLGW 350
FHCTYQKGKQ HCRLRIRQKV EE 372
Length:372
Mass (Da):42,547
Last modified:December 15, 2003 - v1
Checksum:iACD3E582EA6A9210
GO

RNA editingi

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).1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U28134 Genomic RNA. Translation: AAB37097.1.

Keywords - Coding sequence diversityi

RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U28134 Genomic RNA. Translation: AAB37097.1 .

3D structure databases

ProteinModelPortali P60172.
SMRi P60172. Positions 32-284.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR014625. GPC_FiloV.
IPR002561. GPC_filovir-type_extra_dom.
[Graphical view ]
Pfami PF01611. Filo_glycop. 1 hit.
[Graphical view ]
PIRSFi PIRSF036874. GPC_FiloV. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiVSGP_EBOSB
AccessioniPrimary (citable) accession number: P60172
Secondary accession number(s): Q89455
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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