ID   VSGP_EBORR              Reviewed;         367 AA.
AC   Q66800; Q5UAK7; Q8JPX7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 95.
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   Reston ebolavirus (strain Reston-89) (REBOV) (Reston Ebola virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX   NCBI_TaxID=386032;
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).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Volchkov V.E.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12191779; DOI=10.1016/s0168-1702(02)00087-4;
RA   Groseth A., Stroeher U., Theriault S., Feldmann H.;
RT   "Molecular characterization of an isolate from the 1989/90 epizootic of
RT   Ebola virus Reston among macaques imported into the United States.";
RL   Virus Res. 87:155-163(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Pennsylvania-89;
RX   PubMed=15661171; DOI=10.1016/j.virol.2004.11.018;
RA   Boehmann Y., Enterlein S., Randolf A., Muehlberger E.I.;
RT   "A reconstituted replication and transcription system for Ebola virus
RT   Reston and comparison with Ebola virus Zaire.";
RL   Virology 332:406-417(2005).
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       {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: 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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Small/secreted glycoprotein]: Secreted.
CC   -!- SUBCELLULAR LOCATION: [Delta-peptide]: Secreted {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- RNA EDITING: Modified_positions=296 {ECO:0000269|PubMed:8622982};
CC       Note=Partially edited. RNA editing at this position consists of an
CC       insertion of one or two adenine nucleotides. The sequence displayed
CC       here is the full-length transmembrane glycoprotein GP, derived from the
CC       +1A edited RNA. The unedited RNA gives rise to the small secreted
CC       glycoprotein sGP (AC Q66799), the +2A edited RNA gives rise to the
CC       super small secreted glycoprotein ssGP (AC P0C771).;
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; U23152; AAC54884.1; -; Genomic_RNA.
DR   EMBL; AF034645; AAC24345.1; -; Genomic_RNA.
DR   EMBL; AF522874; AAN04451.1; -; Genomic_RNA.
DR   EMBL; AY769362; AAV48578.1; -; Genomic_RNA.
DR   RefSeq; NP_690584.1; NC_004161.1.
DR   SMR; Q66800; -.
DR   GeneID; 955190; -.
DR   Proteomes; UP000007207; Genome.
DR   Proteomes; UP000138664; 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   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..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..367
FT                   /note="Pre-small/secreted glycoprotein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037497"
FT   CHAIN           34..325
FT                   /note="Small/secreted glycoprotein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037498"
FT   CHAIN           326..367
FT                   /note="Delta-peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037499"
FT   SITE            325..326
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        109..136
FT                   /evidence="ECO:0000250"
FT   DISULFID        122..148
FT                   /evidence="ECO:0000250"
FT   DISULFID        307
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   VARIANT         312
FT                   /note="Y -> H"
SQ   SEQUENCE   367 AA;  41771 MW;  F3953243F5420C40 CRC64;
     MGSGYQLLQL PRERFRKTSF LVWVIILFQR AISMPLGIVT NSTLKATEID QLVCRDKLSS
     TSQLKSVGLN LEGNGIATDV PSATKRWGFR SGVPPKVVSY EAGEWAENCY NLEIKKSDGS
     ECLPLPPDGV RGFPRCRYVH KVQGTGPCPG DLAFHKNGAF FLYDRLASTV IYRGTTFAEG
     VVAFLILSEP KKHFWKATPA HEPVNTTDDS TSYYMTLTLS YEMSNFGGNE SNTLFKVDNH
     TYVQLDRPHT PQFLVQLNET LRRNNRLSNS TGRLTWTLDP KIEPDVGEWA FWETKKTFPN
     NFMEKTCISK FYQPTPTTPQ IRARRELSKE KLATTHPPTT PSWFQRIPLQ WFQCSLQDGQ
     RKCRPKV