VSGP_EBORE
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 23-FEB-2022, entry version 65.
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; 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: 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; 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}.
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; AB050936; BAB69007.1; -; Genomic_RNA.
DR SMR; Q91DD7; -.
DR Proteomes; UP000002322; 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_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
