ID   VSGP_EBOG4              Reviewed;         364 AA.
AC   O11458;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   24-JAN-2024, entry version 87.
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 Gabon-94) (ZEBOV) (Zaire Ebola virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Orthoebolavirus;
OC   Orthoebolavirus zairense; Zaire ebolavirus.
OX   NCBI_TaxID=128947;
OH   NCBI_TaxID=77231; Epomops franqueti (Franquet's epauletted fruit bat) (Epomophorus franqueti).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=9185597; DOI=10.1006/viro.1997.8529;
RA   Volchkov V., Volchkova V., Eckel C., Klenk H.-D., Bouloy M., Leguenno B.,
RA   Feldmann H.;
RT   "Emergence of subtype Zaire Ebola virus in Gabon.";
RL   Virology 232:139-144(1997).
CC   -!- FUNCTION: [Small/secreted glycoprotein]: Seems to possess an anti-
CC       inflammatory activity as it can reverse the barrier-decreasing effects
CC       of TNF alpha. Might therefore contribute to the lack of inflammatory
CC       reaction seen during infection in spite the of extensive necrosis and
CC       massive virus production. Does not seem to be involved in activation of
CC       primary macrophages. Does not seem to interact specifically with
CC       neutrophils. {ECO:0000250|UniProtKB:P60170}.
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:0000250|UniProtKB:P60170}.
CC   -!- SUBUNIT: [Small/secreted glycoprotein]: Homodimer; disulfide-linked (By
CC       similarity). The homodimers are linked by two disulfide bonds in a
CC       parallel orientation (By similarity). {ECO:0000250|UniProtKB:P60170}.
CC   -!- SUBUNIT: [Delta-peptide]: Monomer.
CC   -!- SUBCELLULAR LOCATION: [Small/secreted glycoprotein]: Secreted
CC       {ECO:0000250|UniProtKB:P60170}.
CC   -!- SUBCELLULAR LOCATION: [Delta-peptide]: Secreted
CC       {ECO:0000250|UniProtKB:P60170}.
CC   -!- PTM: [Pre-small/secreted glycoprotein]: This precursor is processed
CC       into mature sGP and delta-peptide by host furin or furin-like
CC       proteases. The cleavage site corresponds to the furin optimal cleavage
CC       sequence [KR]-X-[KR]-R. {ECO:0000250|UniProtKB:P60170}.
CC   -!- PTM: [Small/secreted glycoprotein]: N-glycosylated.
CC       {ECO:0000250|UniProtKB:P60170}.
CC   -!- PTM: [Delta-peptide]: O-glycosylated. {ECO:0000250|UniProtKB:P60170}.
CC   -!- RNA EDITING: Modified_positions=295 {ECO:0000250}; Note=Partially
CC       edited. RNA editing at this position consists of an insertion of one
CC       adenine nucleotide. The sequence displayed here is the small secreted
CC       glycoprotein, derived from the unedited RNA. The edited RNA gives rise
CC       to the full-length transmembrane glycoprotein (AC O11457) (By
CC       similarity). {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U77384; AAC57990.1; -; Genomic_RNA.
DR   SMR; O11458; -.
DR   GlyCosmos; O11458; 6 sites, No reported glycans.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR   GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; 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   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; RNA editing; Secreted; Signal; Transport;
KW   Viral ion channel.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..364
FT                   /note="Pre-small/secreted glycoprotein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037491"
FT   CHAIN           33..324
FT                   /note="Small/secreted glycoprotein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037492"
FT   CHAIN           325..364
FT                   /note="Delta-peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037493"
FT   SITE            324..325
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000250"
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:0000250"
FT   DISULFID        108..135
FT                   /evidence="ECO:0000250"
FT   DISULFID        121..147
FT                   /evidence="ECO:0000250"
FT   DISULFID        306
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   364 AA;  41218 MW;  7B46B128FA3E82A5 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 QFLLQLNETR YTSGKRSNTT GKLIWKVNPE IDTTIGEWAF WETKKTSLEK
     FAVKSCLSQL YQTEPKTSVV RVRRELLPTQ GPTQQLKTTK SWLQKIPLQW FKCTVKEGKL
     QCRI
//