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VSGP_EBOZ5
ID   VSGP_EBOZ5              Reviewed;         364 AA.
AC   P60171; O12421; O12717; Q66801; Q66819; Q6V1Q6; Q9YMG3;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 73.
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   Zaire ebolavirus (strain Kikwit-95) (ZEBOV) (Zaire Ebola virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX   NCBI_TaxID=128951;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Chain;
RA   Chain P.S.G., Ichou M.A., Malfatti S.A., Hajjaj A., Vergez L.M.,
RA   Paragas J., Do L.H., Jahrling P.B., Smith K.L., McCready P.M.,
RA   Ibrahim M.S.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
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 or two adenine nucleotides. The sequence displayed
CC       here is the small secreted glycoprotein, derived from the unedited RNA.
CC       The sequence derived from the +1A edited gives rise to the full-length
CC       transmembrane glycoprotein GP (AC P87666), the +2A edited RNA gives
CC       rise to the super small secreted glycoprotein ssGP (AC P0C773).;
CC   -!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; U28077; AAB37094.1; -; Genomic_RNA.
DR   EMBL; AY354458; AAQ55049.1; -; Genomic_RNA.
DR   RefSeq; NP_066247.1; NC_002549.1.
DR   SMR; P60171; -.
DR   DNASU; 911829; -.
DR   GeneID; 911829; -.
DR   Proteomes; UP000007208; 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; Reference proteome; RNA editing; Secreted;
KW   Signal; Transport; Viral ion channel.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..364
FT                   /note="Pre-small/secreted glycoprotein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037509"
FT   CHAIN           33..324
FT                   /note="Small/secreted glycoprotein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037510"
FT   CHAIN           325..364
FT                   /note="Delta-peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000037511"
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        228
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"
FT   VARIANT         47
FT                   /note="D -> E (in strain: Isolate Chain)"
SQ   SEQUENCE   364 AA;  41175 MW;  67376A454CE5F362 CRC64;
     MGVTGILQLP RDRFKRTSFF LWVIILFQRT FSIPLGVIHN STLQVSDVDK LVCRDKLSST
     NQLRSVGLNL EGNGVATDVP SATKRWGFRS GVPPKVVNYE AGEWAENCYN LEIKKPDGSE
     CLPAAPDGIR GFPRCRYVHK VSGTGPCAGD FAFHKEGAFF LYDRLASTVI YRGTTFAEGV
     VAFLILPQAK KDFFSSHPLR EPVNATEDPS SGYYSTTIRY QATGFGTNET EYLFEVDNLT
     YVQLESRFTP QFLLQLNETI YTSGKRSNTT GKLIWKVNPE IDTTIGEWAF WETKKTSLEK
     FAVKSCLSQL YQTEPKTSVV RVRRELLPTQ GPTQQLKTTK SWLQKIPLQW FKCTVKEGKL
     QCRI
 
 
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