ID   VSGP_EBOSU              Reviewed;         372 AA.
AC   Q7T9E0;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=SGP; Synonyms=GP;
OS   Sudan ebolavirus (strain Human/Uganda/Gulu/2000) (SEBOV) (Sudan Ebola
OS   virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX   NCBI_TaxID=386033;
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].
RX   PubMed=15367603; DOI=10.1128/jvi.78.19.10370-10377.2004;
RA   Sanchez A., Lukwiya M., Bausch D., Mahanty S., Sanchez A.J., Wagoner K.D.,
RA   Rollin P.E.;
RT   "Analysis of human peripheral blood samples from fatal and nonfatal cases
RT   of Ebola (Sudan) hemorrhagic fever: cellular responses, virus load, and
RT   nitric oxide levels.";
RL   J. Virol. 78:10370-10377(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15047846; DOI=10.1128/jvi.78.8.4330-4341.2004;
RA   Towner J.S., Rollin P.E., Bausch D.G., Sanchez A., Crary S.M., Vincent M.,
RA   Lee W.F., Spiropoulou C.F., Ksiazek T.G., Lukwiya M., Kaducu F.,
RA   Downing R., Nichol S.T.;
RT   "Rapid diagnosis of Ebola hemorrhagic fever by reverse transcription-PCR in
RT   an outbreak setting and assessment of patient viral load as a predictor of
RT   outcome.";
RL   J. Virol. 78:4330-4341(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=16139097; DOI=10.1016/j.virusres.2005.03.028;
RA   Sanchez A., Rollin P.E.;
RT   "Complete genome sequence of an Ebola virus (Sudan species) responsible for
RT   a 2000 outbreak of human disease in Uganda.";
RL   Virus Res. 113:16-25(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=295; 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 Q7T9D9), the +2A edited RNA gives rise to the super small
CC       secreted glycoprotein ssGP (AC P0C772).;
CC   -!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AY316199; AAP88030.1; -; Genomic_RNA.
DR   EMBL; AY344234; AAR11464.1; -; Genomic_RNA.
DR   EMBL; AY729654; AAU43886.1; -; Genomic_RNA.
DR   RefSeq; YP_138524.1; NC_006432.1.
DR   SMR; Q7T9E0; -.
DR   DNASU; 3160774; -.
DR   GeneID; 3160774; -.
DR   Proteomes; UP000000277; 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..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..372
FT                   /note="Pre-small/secreted glycoprotein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000245090"
FT   CHAIN           33..324
FT                   /note="Small/secreted glycoprotein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000245091"
FT   CHAIN           325..372
FT                   /note="Delta-peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000245092"
FT   REGION          320..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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        208
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   372 AA;  42584 MW;  19307E2085FBC6A4 CRC64;
     MGGLSLLQLP RDKFRKSSFF VWVIILFQKA FSMPLGVVTN STLEVTEIDQ LVCKDHLAST
     DQLKSVGLNL EGSGVSTDIP SATKRWGFRS GVPPKVVSYE AGEWAENCYN LEIKKPDGSE
     CLPPPPDGVR GFPRCRYVHK AQGTGPCPGD YAFHKDGAFF LYDRLASTVI YRGVNFAEGV
     IAFLILAKPK ETFLQSPPIR EAVNYTENTS SYYATSYLEY EIENFGAQHS TTLFKIDNNT
     FVRLDRPHTP QFLFQLNDTI HLHQQLSNTT GRLIWTLDAN INADIGEWAF WENKKISPNN
     YVEKSCLSKL YRSTRQKTMM RHRRELQREE SPTGPPGSIR TWFQRIPLGW FHCTYQKGKQ
     HCRLRIRQKV EE