ID   VSGP_EBORE              Reviewed;         367 AA.
AC   Q91DD7;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 71.
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 Philippines-96) (REBOV) (Reston Ebola virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Orthoebolavirus;
OC   Orthoebolavirus restonense; Reston ebolavirus.
OX   NCBI_TaxID=129003;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9541; Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OH   NCBI_TaxID=77225; Pteropodinae.
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11722021; DOI=10.1007/s007050170049;
RA   Ikegami T., Calaor A.B., Miranda M.E., Niikura M., Saijo M., Kurane I.,
RA   Yoshikawa Y., Morikawa S.;
RT   "Genome structure of Ebola virus subtype Reston: differences among Ebola
RT   subtypes.";
RL   Arch. Virol. 146:2021-2027(2001).
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=296; Note=Partially edited. RNA editing
CC       at this position consists of an insertion of one or two adenine
CC       nucleotides. The sequence displayed here is the small secreted
CC       glycoprotein, derived from the unedited RNA. The sequence derived from
CC       the +1A edited gives rise to the full-length transmembrane glycoprotein
CC       GP (AC Q91DD8), the +2A edited RNA gives rise to the super small
CC       secreted glycoprotein ssGP (AC P0C770).;
CC   -!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AB050936; BAB69007.1; -; Genomic_RNA.
DR   SMR; Q91DD7; -.
DR   GlyCosmos; Q91DD7; 5 sites, No reported glycans.
DR   Proteomes; UP000002322; Genome.
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..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..367
FT                   /note="Pre-small/secreted glycoprotein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000245084"
FT   CHAIN           34..325
FT                   /note="Small/secreted glycoprotein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000245085"
FT   CHAIN           326..367
FT                   /note="Delta-peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000245086"
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        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"
SQ   SEQUENCE   367 AA;  41786 MW;  EDA51204CF8298FA CRC64;
     MGSGYQLLQL PRERFRKTSF LVWVIILFQR AISMPLGIVT NSTLKATEID QLVCRDKLSS
     TSQLKSVGLN LEGNGIATDV PSATKRWGFR SGVPPKVVSY EAGEWAENCY NLEIKKSDGS
     ECLPLPPDGV RGFPRCRYVH KVQGTGPCPG DLAFHKNGAF FLYDRLASTV IYRGTTFAEG
     VIAFLILSEP KKHFWKATPA HEPVNTTDDS TSYYMTLTLS YEMSNFGGEE SNTLFKVDNH
     TYVQLDRPHT PQFLVQLNET LRRNNRLSNS TGRLTWTVDP KIEPDVGEWA FWETKKTFPN
     NFMEKTCISK FYQPTPTTPQ IRARRELSKE KLATTHPPTT PSWFQRIPLQ WFQCSLQDGQ
     RKCRPKV
//