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Pre-small/secreted glycoprotein (pre-sGP) [Cleaved into: Small/secreted glycoprotein (sGP); Delta-peptide]

 VSGP_EBOZM              Reviewed;         364 AA.
P60170; O12421; O12717; Q66801; Q66819; Q77LU4; Q8JS61; Q9YMG3;
15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
15-DEC-2003, sequence version 1.
22-NOV-2017, entry version 69.
RecName: Full=Pre-small/secreted glycoprotein;
Short=pre-sGP;
Contains:
RecName: Full=Small/secreted glycoprotein;
Short=sGP;
Contains:
RecName: Full=Delta-peptide;
Flags: Precursor;
Name=GP;
Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Filoviridae; Ebolavirus.
NCBI_TaxID=128952;
NCBI_TaxID=77231; Epomops franqueti (Franquet's epauleted fruit bat).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA / MRNA], AND RNA EDITING.
PubMed=8553543; DOI=10.1006/viro.1995.0052;
Volchkov V.E., Becker S., Volchkova V.A., Ternovoj V.A., Kotov A.N.,
Netesov S.V., Klenk H.-D.;
"GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by
T7 and vaccinia virus polymerases.";
Virology 214:421-430(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
PubMed=8622982; DOI=10.1073/pnas.93.8.3602;
Sanchez A., Trappier S.G., Mahy B.W.J., Peters C.J., Nichol S.T.;
"The virion glycoproteins of Ebola viruses are encoded in two reading
frames and are expressed through transcriptional editing.";
Proc. Natl. Acad. Sci. U.S.A. 93:3602-3607(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate guinea pig-adapted;
PubMed=11062045; DOI=10.1006/viro.2000.0572;
Volchkov V.E., Chepurnov A.A., Volchkova V.A., Ternovoj V.A.,
Klenk H.D.;
"Molecular characterization of guinea pig-adapted variants of Ebola
virus.";
Virology 277:147-155(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Volchkov V.E.;
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate mouse-adapted;
Wilson J.A., Kondig J.P., Kuehne A.I., Hart M.K.;
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF ARG-324.
PubMed=10603327; DOI=10.1006/viro.1999.0034;
Volchkova V.A., Klenk H.-D., Volchkov V.E.;
"Delta-peptide is the carboxy-terminal cleavage fragment of the
nonstructural small glycoprotein sGP of Ebola virus.";
Virology 265:164-171(1999).
[7]
DISULFIDE BONDS.
PubMed=15369806; DOI=10.1016/j.bbrc.2004.08.148;
Barrientos L.G., Martin A.M., Rollin P.E., Sanchez A.;
"Disulfide bond assignment of the Ebola virus secreted glycoprotein
SGP.";
Biochem. Biophys. Res. Commun. 323:696-702(2004).
[8]
FUNCTION OF SGP.
PubMed=11152533; DOI=10.1128/JVI.75.3.1576-1580.2001;
Ito H., Watanabe S., Takada A., Kawaoka Y.;
"Ebola virus glycoprotein: proteolytic processing, acylation, cell
tropism, and detection of neutralizing antibodies.";
J. Virol. 75:1576-1580(2001).
[9]
FUNCTION OF SGP.
PubMed=12482654; DOI=10.1006/viro.2002.1715;
Sui J., Marasco W.A.;
"Evidence against Ebola virus sGP binding to human neutrophils by a
specific receptor.";
Virology 303:9-14(2002).
[10]
FUNCTION OF SGP.
PubMed=16051836; DOI=10.1128/JVI.79.16.10442-10450.2005;
Wahl-Jensen V.M., Afanasieva T.A., Seebach J., Stroeher U.,
Feldmann H., Schnittler H.J.;
"Effects of Ebola virus glycoproteins on endothelial cell activation
and barrier function.";
J. Virol. 79:10442-10450(2005).
[11]
FUNCTION.
PubMed=15681442; DOI=10.1128/JVI.79.4.2413-2419.2005;
Wahl-Jensen V., Kurz S.K., Hazelton P.R., Schnittler H.J.,
Stroeher U., Burton D.R., Feldmann H.;
"Role of Ebola virus secreted glycoproteins and virus-like particles
in activation of human macrophages.";
J. Virol. 79:2413-2419(2005).
[12]
FUNCTION (DELTA-PEPTIDE).
PubMed=25609303; DOI=10.3390/v7010285;
Gallaher W.R., Garry R.F.;
"Modeling of the Ebola virus delta peptide reveals a potential lytic
sequence motif.";
Viruses 7:285-305(2015).
[13]
FUNCTION (DELTA-PEPTIDE).
STRAIN=Zaire ebolavirus Makona;
PubMed=28539454; DOI=10.1128/JVI.00438-17;
He J., Melnik L.I., Komin A., Wiedman G., Fuselier T., Morris C.F.,
Starr C.G., Searson P.C., Gallaher W.R., Hristova K., Garry R.F.,
Wimley W.C.;
"Ebola virus delta peptide is a viroporin.";
J. Virol. 0:0-0(2017).
-!- FUNCTION: 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.
-!- FUNCTION: 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. {ECO:0000269|PubMed:28539454,
ECO:0000305|PubMed:25609303}.
-!- SUBUNIT: sGP is a homodimer; disulfide-linked. The homodimers are
linked by two disulfide bonds in a parallel orientation. Delta-
peptide is a monomer. {ECO:0000269|PubMed:15369806}.
-!- SUBCELLULAR LOCATION: Small/secreted glycoprotein: Secreted.
-!- SUBCELLULAR LOCATION: Delta-peptide: Secreted.
-!- PTM: 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.
{ECO:0000269|PubMed:10603327}.
-!- RNA EDITING: Modified_positions=295 {ECO:0000269|PubMed:8553543,
ECO:0000269|PubMed:8622982}; Note=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 Q05320), the +2A edited RNA gives rise to the
super small secreted glycoprotein ssGP (AC Q9YMG2).;
-!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; U31033; AAA96745.1; -; Genomic_RNA.
EMBL; U23187; AAC54886.1; -; Genomic_RNA.
EMBL; AF272001; AAG40167.1; -; Genomic_RNA.
EMBL; AY142960; AAN37508.1; -; Genomic_RNA.
EMBL; AF086833; AAD14584.1; -; Genomic_RNA.
EMBL; AF499101; AAM76035.1; -; Genomic_RNA.
RefSeq; NP_066247.1; NC_002549.1.
ProteinModelPortal; P60170; -.
SMR; P60170; -.
ELM; P60170; -.
GeneID; 911829; -.
OrthoDB; VOG090000CW; -.
Proteomes; UP000007209; Genome.
Proteomes; UP000149419; Genome.
Proteomes; UP000150973; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
InterPro; IPR014625; GPC_FiloV.
InterPro; IPR002561; GPC_filovir-type_extra_dom.
Pfam; PF01611; Filo_glycop; 1.
PIRSF; PIRSF036874; GPC_FiloV; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Glycoprotein; Ion channel; Ion transport; Reference proteome;
RNA editing; Secreted; Signal; Transport; Viral ion channel.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 364 Pre-small/secreted glycoprotein.
/FTId=PRO_0000037512.
CHAIN 33 324 Small/secreted glycoprotein.
/FTId=PRO_0000037513.
CHAIN 325 364 Delta-peptide.
/FTId=PRO_0000037514.
SITE 324 325 Cleavage; by host furin.
CARBOHYD 40 40 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 228 228 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 238 238 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 257 257 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 268 268 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 53 53 Interchain.
{ECO:0000269|PubMed:15369806}.
DISULFID 108 135 {ECO:0000269|PubMed:15369806}.
DISULFID 121 147 {ECO:0000269|PubMed:15369806}.
DISULFID 306 306 Interchain.
{ECO:0000269|PubMed:15369806}.
VARIANT 65 65 S -> P (in strain: Isolate mouse-
adapted).
VARIANT 246 246 S -> P (in strain: Isolate mouse-
adapted).
MUTAGEN 324 324 R->S: Loss of cleavage.
{ECO:0000269|PubMed:10603327}.
SEQUENCE 364 AA; 41175 MW; 67376A454CE5F362 CRC64;
MGVTGILQLP RDRFKRTSFF LWVIILFQRT FSIPLGVIHN STLQVSDVDK LVCRDKLSST
NQLRSVGLNL EGNGVATDVP SATKRWGFRS GVPPKVVNYE AGEWAENCYN LEIKKPDGSE
CLPAAPDGIR GFPRCRYVHK VSGTGPCAGD FAFHKEGAFF LYDRLASTVI YRGTTFAEGV
VAFLILPQAK KDFFSSHPLR EPVNATEDPS SGYYSTTIRY QATGFGTNET EYLFEVDNLT
YVQLESRFTP QFLLQLNETI YTSGKRSNTT GKLIWKVNPE IDTTIGEWAF WETKKTSLEK
FAVKSCLSQL YQTEPKTSVV RVRRELLPTQ GPTQQLKTTK SWLQKIPLQW FKCTVKEGKL
QCRI


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