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Q66800

- VSGP_EBORR

UniProt

Q66800 - VSGP_EBORR

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Protein
Pre-small/secreted glycoprotein
Gene
GP
Organism
Reston ebolavirus (strain Reston-89) (REBOV) (Reston 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
Sitei325 – 3262Cleavage; 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
OrganismiReston ebolavirus (strain Reston-89) (REBOV) (Reston Ebola virus)
Taxonomic identifieri386032 [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]
Sus scrofa (Pig) [TaxID: 9823]
ProteomesiUP000007207: Genome

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 – 3333 Reviewed prediction
Add
BLAST
Chaini34 – 367334Pre-small/secreted glycoprotein By similarity
PRO_0000037497Add
BLAST
Chaini34 – 325292Small/secreted glycoprotein By similarity
PRO_0000037498Add
BLAST
Chaini326 – 36742Delta-peptide By similarity
PRO_0000037499Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi41 – 411N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi54 – 54Interchain By similarity
Disulfide bondi109 ↔ 136 By similarity
Disulfide bondi122 ↔ 148 By similarity
Glycosylationi205 – 2051N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi229 – 2291N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi239 – 2391N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi258 – 2581N-linked (GlcNAc...); by host Reviewed prediction
Glycosylationi269 – 2691N-linked (GlcNAc...); by host Reviewed prediction
Disulfide bondi307 – 307Interchain 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

ProteinModelPortaliQ66800.
SMRiQ66800. Positions 33-285.

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.

Q66800-1 [UniParc]FASTAAdd to Basket

« Hide

MGSGYQLLQL PRERFRKTSF LVWVIILFQR AISMPLGIVT NSTLKATEID    50
QLVCRDKLSS TSQLKSVGLN LEGNGIATDV PSATKRWGFR SGVPPKVVSY 100
EAGEWAENCY NLEIKKSDGS ECLPLPPDGV RGFPRCRYVH KVQGTGPCPG 150
DLAFHKNGAF FLYDRLASTV IYRGTTFAEG VVAFLILSEP KKHFWKATPA 200
HEPVNTTDDS TSYYMTLTLS YEMSNFGGNE SNTLFKVDNH TYVQLDRPHT 250
PQFLVQLNET LRRNNRLSNS TGRLTWTLDP KIEPDVGEWA FWETKKTFPN 300
NFMEKTCISK FYQPTPTTPQ IRARRELSKE KLATTHPPTT PSWFQRIPLQ 350
WFQCSLQDGQ RKCRPKV 367
Length:367
Mass (Da):41,771
Last modified:November 1, 1996 - v1
Checksum:iF3953243F5420C40
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 full-length transmembrane glycoprotein GP, derived from the +1A edited RNA. The unedited RNA gives rise to the small secreted glycoprotein sGP (AC Q66799), the +2A edited RNA gives rise to the super small secreted glycoprotein ssGP (AC P0C771).1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti312 – 3121Y → H.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U23152 Genomic RNA. Translation: AAC54884.1.
AF034645 Genomic RNA. Translation: AAC24345.1.
AF522874 Genomic RNA. Translation: AAN04451.1.
AY769362 Genomic RNA. Translation: AAV48578.1.
RefSeqiNP_690584.1. NC_004161.1.

Genome annotation databases

GeneIDi955190.

Keywords - Coding sequence diversityi

RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U23152 Genomic RNA. Translation: AAC54884.1 .
AF034645 Genomic RNA. Translation: AAC24345.1 .
AF522874 Genomic RNA. Translation: AAN04451.1 .
AY769362 Genomic RNA. Translation: AAV48578.1 .
RefSeqi NP_690584.1. NC_004161.1.

3D structure databases

ProteinModelPortali Q66800.
SMRi Q66800. Positions 33-285.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 955190.

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. Volchkov V.E.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "Molecular characterization of an isolate from the 1989/90 epizootic of Ebola virus Reston among macaques imported into the United States."
    Groseth A., Stroeher U., Theriault S., Feldmann H.
    Virus Res. 87:155-163(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  4. "A reconstituted replication and transcription system for Ebola virus Reston and comparison with Ebola virus Zaire."
    Boehmann Y., Enterlein S., Randolf A., Muehlberger E.I.
    Virology 332:406-417(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Strain: Isolate Pennsylvania-89.

Entry informationi

Entry nameiVSGP_EBORR
AccessioniPrimary (citable) accession number: Q66800
Secondary accession number(s): Q5UAK7, Q8JPX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: December 11, 2013
This is version 61 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

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