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P60171

- VSGP_EBOZ5

UniProt

P60171 - VSGP_EBOZ5

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Protein

Pre-small/secreted glycoprotein

Gene

GP

Organism
Zaire ebolavirus (strain Kikwit-95) (ZEBOV) (Zaire Ebola virus)
Status
Reviewed - Annotation score: 3 out of 5- 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).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 furinBy 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
OrganismiZaire ebolavirus (strain Kikwit-95) (ZEBOV) (Zaire Ebola virus)
Taxonomic identifieri128951 [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]
ProteomesiUP000007208: Genome

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence AnalysisAdd
BLAST
Chaini33 – 364332Pre-small/secreted glycoproteinBy similarityPRO_0000037509Add
BLAST
Chaini33 – 324292Small/secreted glycoproteinBy similarityPRO_0000037510Add
BLAST
Chaini325 – 36440Delta-peptideBy similarityPRO_0000037511Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi40 – 401N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi53 – 53InterchainBy similarity
Disulfide bondi108 ↔ 135By similarity
Disulfide bondi121 ↔ 147By similarity
Glycosylationi204 – 2041N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi228 – 2281N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi238 – 2381N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi257 – 2571N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi268 – 2681N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi306 – 306InterchainBy 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

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

ProteinModelPortaliP60171.
SMRiP60171. Positions 32-281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the filoviruses glycoprotein family.Curated

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.

P60171-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGVTGILQLP RDRFKRTSFF LWVIILFQRT FSIPLGVIHN STLQVSDVDK
60 70 80 90 100
LVCRDKLSST NQLRSVGLNL EGNGVATDVP SATKRWGFRS GVPPKVVNYE
110 120 130 140 150
AGEWAENCYN LEIKKPDGSE CLPAAPDGIR GFPRCRYVHK VSGTGPCAGD
160 170 180 190 200
FAFHKEGAFF LYDRLASTVI YRGTTFAEGV VAFLILPQAK KDFFSSHPLR
210 220 230 240 250
EPVNATEDPS SGYYSTTIRY QATGFGTNET EYLFEVDNLT YVQLESRFTP
260 270 280 290 300
QFLLQLNETI YTSGKRSNTT GKLIWKVNPE IDTTIGEWAF WETKKTSLEK
310 320 330 340 350
FAVKSCLSQL YQTEPKTSVV RVRRELLPTQ GPTQQLKTTK SWLQKIPLQW
360
FKCTVKEGKL QCRI
Length:364
Mass (Da):41,175
Last modified:December 15, 2003 - v1
Checksum:i67376A454CE5F362
GO

RNA editingi

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).

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti47 – 471D → E in strain: Isolate Chain.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28077 Genomic RNA. Translation: AAB37094.1.
AY354458 Genomic RNA. Translation: AAQ55049.1.
RefSeqiNP_066247.1. NC_002549.1.

Genome annotation databases

GeneIDi911829.

Keywords - Coding sequence diversityi

RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28077 Genomic RNA. Translation: AAB37094.1 .
AY354458 Genomic RNA. Translation: AAQ55049.1 .
RefSeqi NP_066247.1. NC_002549.1.

3D structure databases

ProteinModelPortali P60171.
SMRi P60171. Positions 32-281.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 911829.

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.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate Chain.

Entry informationi

Entry nameiVSGP_EBOZ5
AccessioniPrimary (citable) accession number: P60171
Secondary accession number(s): O12421
, O12717, Q66801, Q66819, Q6V1Q6, Q9YMG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: October 29, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3