VSGP_EBOSM
ID VSGP_EBOSM Reviewed; 372 AA.
AC P60173; Q89455;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 29-SEP-2021, 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 Sudan ebolavirus (strain Maleo-79) (SEBOV) (Sudan Ebola virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=128949;
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], 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).
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 {ECO:0000269|PubMed:8622982};
CC Note=Partially edited. RNA editing at this position consists of an
CC insertion of one adenine nucleotide. The sequence displayed here is the
CC small secreted glycoprotein, derived from the unedited RNA. The edited
CC RNA gives rise to the full-length transmembrane glycoprotein (AC
CC Q66798).;
CC -!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; U23069; AAC54883.1; -; Genomic_RNA.
DR SMR; P60173; -.
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_0000037506"
FT CHAIN 33..324
FT /note="Small/secreted glycoprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037507"
FT CHAIN 325..372
FT /note="Delta-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037508"
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; 42547 MW; ACD3E582EA6A9210 CRC64;
MEGLSLLQLP RDKFRKSSFF VWVIILFQKA FSMPLGVVTN STLEVTEIDQ LVCKDHLAST
DQLKSVGLNL EGSGVSTDIP SATKRWGFRS GVPPQVVSYE AGEWAENCYN LEIKKPDGSE
CLPPPPDGVR GFPRCRYVHK AQGTGPCPGD YAFHKDGAFF LYDRLASTVI YRGVNFAEGV
IAFLILAKPK ETFLQSPPIR EAANYTENTS SYYATSYLEY EIENFGAQHS TTLFKINNNT
FVLLDRPHTP QFLFQLNDTI QLHQQLSNTT GKLIWTLDAN INADIGEWAF WENKKISPNN
YVEKSCLSKL YRSTRQKTMM RHRRELQREE SPTGPPGSIR TWFQRIPLGW FHCTYQKGKQ
HCRLRIRQKV EE
