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P87670

- VSGP_EBOEC

UniProt

P87670 - VSGP_EBOEC

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Protein
Pre-small/secreted glycoprotein
Gene
GP
Organism
Zaire ebolavirus (strain Eckron-76) (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.
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
OrganismiZaire ebolavirus (strain Eckron-76) (ZEBOV) (Zaire Ebola virus)
Taxonomic identifieri129000 [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 prediction
Add
BLAST
Chaini33 – 364332Pre-small/secreted glycoprotein By similarity
PRO_0000037488Add
BLAST
Chaini33 – 324292Small/secreted glycoprotein By similarity
PRO_0000037489Add
BLAST
Chaini325 – 36440Delta-peptide By similarity
PRO_0000037490Add
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
Glycosylationi228 – 2281N-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

ProteinModelPortaliP87670.
SMRiP87670. Positions 32-281.

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.

P87670-1 [UniParc]FASTAAdd to Basket

« Hide

MGVTGILQLP RDRFKRTSFF LWVIILFQRT FSIPLGVIHN STLQVNDVDK    50
LVCRDKLSST NQLRSVGLNL EGNGVATDVP SATKRWGFRS GVPPKVVNYE 100
AGEWAENCYN LEIKKPDGSE CLPAAPDGIR GFPRCRYVHK VSGTGPCAGD 150
FAFHKEGAFF LYDRLASTVI YRGTTFAEGV VAFLILPQAK KDFFSSHPLR 200
EPVNATEDPS SGYYSTTIRY QATGFGTNET EYLFEVDNLT YVQLESRFTP 250
QFLLQLNETI YTSGKRSNTT GKLIWKVNPE IDTTIGEWAF WETKKTSLEK 300
FAVKSCLSQL YQTEPKTSVV RVRRELLPTQ GPTQQLKTTK SWLQKIPLQW 350
FKCTVKEGKL QCRI 364
Length:364
Mass (Da):41,202
Last modified:May 1, 1997 - v1
Checksum:i5D034F8DA5EE2695
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 P87671) By similarity.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U81161 Genomic RNA. Translation: AAC57993.1.

Keywords - Coding sequence diversityi

RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U81161 Genomic RNA. Translation: AAC57993.1 .

3D structure databases

ProteinModelPortali P87670.
SMRi P87670. Positions 32-281.
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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiVSGP_EBOEC
AccessioniPrimary (citable) accession number: P87670
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1997
Last modified: December 11, 2013
This is version 59 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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