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Protein

Pre-small/secreted glycoprotein

Gene

GP

Organism
Sudan ebolavirus (strain Maleo-79) (SEBOV) (Sudan Ebola virus)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

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: Viroporin that permeabilizes mammalian cell plasma membranes. It acts by altering permeation of ionic compounds and small molecules. This activity may leads to viral enterotoxic activity.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIon channel, Viral ion channel
Biological processIon transport, Transport

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 Maleo-79) (SEBOV) (Sudan Ebola virus)
Taxonomic identifieri128949 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA 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

Delta-peptide :

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32Sequence analysisAdd BLAST32
ChainiPRO_000003750633 – 372Pre-small/secreted glycoproteinBy similarityAdd BLAST340
ChainiPRO_000003750733 – 324Small/secreted glycoproteinBy similarityAdd BLAST292
ChainiPRO_0000037508325 – 372Delta-peptideBy similarityAdd BLAST48

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi40N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi53InterchainBy similarity
Disulfide bondi108 ↔ 135By similarity
Disulfide bondi121 ↔ 147By similarity
Glycosylationi204N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi208N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi238N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi257N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Glycosylationi268N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi306InterchainBy 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).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei324 – 325Cleavage; by host furinBy similarity2

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).By similarity

Structurei

3D structure databases

ProteinModelPortaliP60173
SMRiP60173
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the filoviruses glycoprotein family.Curated

Keywords - Domaini

Signal

Family and domain databases

InterProiView protein in InterPro
IPR014625 GPC_FiloV
IPR002561 GPC_filovir-type_extra_dom
PfamiView protein in Pfam
PF01611 Filo_glycop, 1 hit
PIRSFiPIRSF036874 GPC_FiloV, 1 hit

Sequencei

Sequence statusi: Complete.

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

P60173-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGLSLLQLP RDKFRKSSFF VWVIILFQKA FSMPLGVVTN STLEVTEIDQ
60 70 80 90 100
LVCKDHLAST DQLKSVGLNL EGSGVSTDIP SATKRWGFRS GVPPQVVSYE
110 120 130 140 150
AGEWAENCYN LEIKKPDGSE CLPPPPDGVR GFPRCRYVHK AQGTGPCPGD
160 170 180 190 200
YAFHKDGAFF LYDRLASTVI YRGVNFAEGV IAFLILAKPK ETFLQSPPIR
210 220 230 240 250
EAANYTENTS SYYATSYLEY EIENFGAQHS TTLFKINNNT FVLLDRPHTP
260 270 280 290 300
QFLFQLNDTI QLHQQLSNTT GKLIWTLDAN INADIGEWAF WENKKISPNN
310 320 330 340 350
YVEKSCLSKL YRSTRQKTMM RHRRELQREE SPTGPPGSIR TWFQRIPLGW
360 370
FHCTYQKGKQ HCRLRIRQKV EE
Length:372
Mass (Da):42,547
Last modified:December 15, 2003 - v1
Checksum:iACD3E582EA6A9210
GO

RNA editingi

Edited at position 295.1 Publication
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 Q66798).

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23069 Genomic RNA Translation: AAC54883.1

Keywords - Coding sequence diversityi

RNA editing

Similar proteinsi

Entry informationi

Entry nameiVSGP_EBOSM
AccessioniPrimary (citable) accession number: P60173
Secondary accession number(s): Q89455
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: May 23, 2018
This is version 56 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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