VSGP_EBOZM
ID VSGP_EBOZM Reviewed; 364 AA.
AC P60170; O12421; O12717; Q66801; Q66819; Q77LU4; Q8JS61; Q9YMG3;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 02-JUN-2021, entry version 79.
DE RecName: Full=Pre-small/secreted glycoprotein;
DE Short=pre-sGP;
DE Contains:
DE RecName: Full=Small/secreted glycoprotein;
DE Short=sGP;
DE Contains:
DE RecName: Full=Delta-peptide;
DE Flags: Precursor;
GN Name=GP;
OS Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=128952;
OH NCBI_TaxID=77231; Epomops franqueti (Franquet's epauleted fruit bat).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA / MRNA], AND RNA EDITING.
RX PubMed=8553543; DOI=10.1006/viro.1995.0052;
RA Volchkov V.E., Becker S., Volchkova V.A., Ternovoj V.A., Kotov A.N.,
RA Netesov S.V., Klenk H.-D.;
RT "GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by T7
RT and vaccinia virus polymerases.";
RL Virology 214:421-430(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
RX PubMed=8622982; DOI=10.1073/pnas.93.8.3602;
RA Sanchez A., Trappier S.G., Mahy B.W.J., Peters C.J., Nichol S.T.;
RT "The virion glycoproteins of Ebola viruses are encoded in two reading
RT frames and are expressed through transcriptional editing.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:3602-3607(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate guinea pig-adapted;
RX PubMed=11062045; DOI=10.1006/viro.2000.0572;
RA Volchkov V.E., Chepurnov A.A., Volchkova V.A., Ternovoj V.A., Klenk H.D.;
RT "Molecular characterization of guinea pig-adapted variants of Ebola
RT virus.";
RL Virology 277:147-155(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Volchkov V.E.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate mouse-adapted;
RA Wilson J.A., Kondig J.P., Kuehne A.I., Hart M.K.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF ARG-324.
RX PubMed=10603327; DOI=10.1006/viro.1999.0034;
RA Volchkova V.A., Klenk H.-D., Volchkov V.E.;
RT "Delta-peptide is the carboxy-terminal cleavage fragment of the
RT nonstructural small glycoprotein sGP of Ebola virus.";
RL Virology 265:164-171(1999).
RN [7]
RP DISULFIDE BONDS.
RX PubMed=15369806; DOI=10.1016/j.bbrc.2004.08.148;
RA Barrientos L.G., Martin A.M., Rollin P.E., Sanchez A.;
RT "Disulfide bond assignment of the Ebola virus secreted glycoprotein SGP.";
RL Biochem. Biophys. Res. Commun. 323:696-702(2004).
RN [8]
RP FUNCTION OF SGP.
RX PubMed=11152533; DOI=10.1128/jvi.75.3.1576-1580.2001;
RA Ito H., Watanabe S., Takada A., Kawaoka Y.;
RT "Ebola virus glycoprotein: proteolytic processing, acylation, cell tropism,
RT and detection of neutralizing antibodies.";
RL J. Virol. 75:1576-1580(2001).
RN [9]
RP FUNCTION OF SGP.
RX PubMed=12482654; DOI=10.1006/viro.2002.1715;
RA Sui J., Marasco W.A.;
RT "Evidence against Ebola virus sGP binding to human neutrophils by a
RT specific receptor.";
RL Virology 303:9-14(2002).
RN [10]
RP FUNCTION OF SGP.
RX PubMed=16051836; DOI=10.1128/jvi.79.16.10442-10450.2005;
RA Wahl-Jensen V.M., Afanasieva T.A., Seebach J., Stroeher U., Feldmann H.,
RA Schnittler H.J.;
RT "Effects of Ebola virus glycoproteins on endothelial cell activation and
RT barrier function.";
RL J. Virol. 79:10442-10450(2005).
RN [11]
RP FUNCTION.
RX PubMed=15681442; DOI=10.1128/jvi.79.4.2413-2419.2005;
RA Wahl-Jensen V., Kurz S.K., Hazelton P.R., Schnittler H.J., Stroeher U.,
RA Burton D.R., Feldmann H.;
RT "Role of Ebola virus secreted glycoproteins and virus-like particles in
RT activation of human macrophages.";
RL J. Virol. 79:2413-2419(2005).
RN [12]
RP FUNCTION (DELTA-PEPTIDE).
RX PubMed=25609303; DOI=10.3390/v7010285;
RA Gallaher W.R., Garry R.F.;
RT "Modeling of the Ebola virus delta peptide reveals a potential lytic
RT sequence motif.";
RL Viruses 7:285-305(2015).
RN [13]
RP FUNCTION (DELTA-PEPTIDE).
RC STRAIN=Zaire ebolavirus Makona;
RX PubMed=28539454; DOI=10.1128/jvi.00438-17;
RA He J., Melnik L.I., Komin A., Wiedman G., Fuselier T., Morris C.F.,
RA Starr C.G., Searson P.C., Gallaher W.R., Hristova K., Garry R.F.,
RA Wimley W.C.;
RT "Ebola virus delta peptide is a viroporin.";
RL J. Virol. 0:0-0(2017).
CC -!- FUNCTION: sGP seems to possess an anti-inflammatory activity as it can
CC reverse the barrier-decreasing effects of TNF alpha. Might therefore
CC contribute to the lack of inflammatory reaction seen during infection
CC in spite the of extensive necrosis and massive virus production. Does
CC not seem to be involved in activation of primary macrophages. Does not
CC seem to interact specifically with neutrophils.
CC -!- FUNCTION: [Delta-peptide]: Viroporin that permeabilizes mammalian cell
CC plasma membranes. It acts by altering permeation of ionic compounds and
CC small molecules. This activity may lead to viral enterotoxic activity.
CC {ECO:0000269|PubMed:28539454, ECO:0000305|PubMed:25609303}.
CC -!- SUBUNIT: sGP is a homodimer; disulfide-linked. The homodimers are
CC linked by two disulfide bonds in a parallel orientation. Delta-peptide
CC is a monomer. {ECO:0000269|PubMed:15369806}.
CC -!- SUBCELLULAR LOCATION: [Small/secreted glycoprotein]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Delta-peptide]: Secreted.
CC -!- PTM: Pre-sGP is N-glycosylated. This precursor is processed into mature
CC sGP and delta-peptide by host furin or furin-like proteases. The
CC cleavage site corresponds to the furin optimal cleavage sequence [KR]-
CC X-[KR]-R. Both cleavage fragments contain sialic acid, but only the
CC delta-peptide is O-glycosylated. {ECO:0000269|PubMed:10603327}.
CC -!- RNA EDITING: Modified_positions=295 {ECO:0000269|PubMed:8553543,
CC ECO:0000269|PubMed:8622982}; Note=Partially edited. RNA editing at this
CC position consists of an insertion of one or two adenine nucleotides.
CC The sequence displayed here is the small secreted glycoprotein, derived
CC from the unedited RNA. The sequence derived from the +1A edited gives
CC rise to the full-length transmembrane glycoprotein GP (AC Q05320), the
CC +2A edited RNA gives rise to the super small secreted glycoprotein ssGP
CC (AC Q9YMG2).;
CC -!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; U31033; AAA96745.1; -; Genomic_RNA.
DR EMBL; U23187; AAC54886.1; -; Genomic_RNA.
DR EMBL; AF272001; AAG40167.1; -; Genomic_RNA.
DR EMBL; AY142960; AAN37508.1; -; Genomic_RNA.
DR EMBL; AF086833; AAD14584.1; -; Genomic_RNA.
DR EMBL; AF499101; AAM76035.1; -; Genomic_RNA.
DR RefSeq; NP_066247.1; NC_002549.1.
DR SMR; P60170; -.
DR ELM; P60170; -.
DR DNASU; 911829; -.
DR GeneID; 911829; -.
DR Proteomes; UP000007209; Genome.
DR Proteomes; UP000149419; Genome.
DR Proteomes; UP000150973; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR InterPro; IPR014625; GPC_FiloV.
DR InterPro; IPR002561; GPC_filovir-type_extra_dom.
DR Pfam; PF01611; Filo_glycop; 1.
DR PIRSF; PIRSF036874; GPC_FiloV; 1.
PE 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Reference proteome; RNA editing; Secreted;
KW Signal; Transport; Viral ion channel.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..364
FT /note="Pre-small/secreted glycoprotein"
FT /id="PRO_0000037512"
FT CHAIN 33..324
FT /note="Small/secreted glycoprotein"
FT /id="PRO_0000037513"
FT CHAIN 325..364
FT /note="Delta-peptide"
FT /id="PRO_0000037514"
FT SITE 324..325
FT /note="Cleavage; by host furin"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 53
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:15369806"
FT DISULFID 108..135
FT /evidence="ECO:0000269|PubMed:15369806"
FT DISULFID 121..147
FT /evidence="ECO:0000269|PubMed:15369806"
FT DISULFID 306
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:15369806"
FT VARIANT 65
FT /note="S -> P (in strain: Isolate mouse-adapted)"
FT VARIANT 246
FT /note="S -> P (in strain: Isolate mouse-adapted)"
FT MUTAGEN 324
FT /note="R->S: Loss of cleavage."
FT /evidence="ECO:0000269|PubMed:10603327"
SQ 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
