VSGP_TAFVC
ID VSGP_TAFVC Reviewed; 365 AA.
AC Q66811;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 78.
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 Tai Forest ebolavirus (strain Cote d'Ivoire-94) (TAFV) (Cote d'Ivoire Ebola
OS virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=128999;
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 Q66810).;
CC -!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; U28006; AAB37092.1; -; Genomic_RNA.
DR SMR; Q66811; -.
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..365
FT /note="Pre-small/secreted glycoprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037494"
FT CHAIN 33..324
FT /note="Small/secreted glycoprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037495"
FT CHAIN 325..365
FT /note="Delta-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037496"
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 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 365 AA; 41690 MW; D2D39579392F9C28 CRC64;
MGASGILQLP RERFRKTSFF VWVIILFHKV FSIPLGVVHN NTLQVSDIDK FVCRDKLSST
SQLKSVGLNL EGNGVATDVP TATKRWGFRA GVPPKVVNYE AGEWAENCYN LAIKKVDGSE
CLPEAPEGVR DFPRCRYVHK VSGTGPCPGG LAFHKEGAFF LYDRLASTII YRGTTFAEGV
IAFLILPKAR KDFFQSPPLH EPANMTTDPS SYYHTTTINY VVDNFGTNTT EFLFQVDHLT
YVQLEARFTP QFLVLLNETI YSDNRRSNTT GKLIWKINPT VDTSMGEWAF WENKKTSQKP
FQVKSCLSYL YQKPRTRSLT RQRRSLLPSP PTTTQAKTTK NWFQRIPLQW FRCKTSRERT
QCQPQ
