VSGP_EBOG4
ID VSGP_EBOG4 Reviewed; 364 AA.
AC O11458;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 Gabon-94) (ZEBOV) (Zaire Ebola virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=128947;
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=9185597; DOI=10.1006/viro.1997.8529;
RA Volchkov V., Volchkova V., Eckel C., Klenk H.-D., Bouloy M., Leguenno B.,
RA Feldmann H.;
RT "Emergence of subtype Zaire Ebola virus in Gabon.";
RL Virology 232:139-144(1997).
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:0000250}; Note=Partially
CC edited. RNA editing at this position consists of an insertion of one
CC adenine nucleotide. The sequence displayed here is the small secreted
CC glycoprotein, derived from the unedited RNA. The edited RNA gives rise
CC to the full-length transmembrane glycoprotein (AC O11457) (By
CC similarity). {ECO:0000250};
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; U77384; AAC57990.1; -; Genomic_RNA.
DR PDB; 7SWD; EM; 3.59 A; A/C/E=33-188.
DR PDBsum; 7SWD; -.
DR SMR; O11458; -.
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 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; RNA editing; Secreted; Signal;
KW 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_0000037491"
FT CHAIN 33..324
FT /note="Small/secreted glycoprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037492"
FT CHAIN 325..364
FT /note="Delta-peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037493"
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"
SQ SEQUENCE 364 AA; 41218 MW; 7B46B128FA3E82A5 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 QFLLQLNETR YTSGKRSNTT GKLIWKVNPE IDTTIGEWAF WETKKTSLEK
FAVKSCLSQL YQTEPKTSVV RVRRELLPTQ GPTQQLKTTK SWLQKIPLQW FKCTVKEGKL
QCRI
