ID   VSSGP_EBORE             Reviewed;         332 AA.
AC   P0C770;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   23-FEB-2022, entry version 32.
DE   RecName: Full=Super small secreted glycoprotein;
DE            Short=SsGP;
DE   Flags: Precursor;
GN   Name=GP;
OS   Reston ebolavirus (strain Philippines-96) (REBOV) (Reston Ebola virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX   NCBI_TaxID=129003;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9541; Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OH   NCBI_TaxID=77225; Pteropodinae.
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11722021; DOI=10.1007/s007050170049;
RA   Ikegami T., Calaor A.B., Miranda M.E., Niikura M., Saijo M., Kurane I.,
RA   Yoshikawa Y., Morikawa S.;
RT   "Genome structure of Ebola virus subtype Reston: differences among Ebola
RT   subtypes.";
RL   Arch. Virol. 146:2021-2027(2001).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- RNA EDITING: Modified_positions=296; 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 super small secreted
CC       glycoprotein ssGP, derived from the +2A edited RNA. The unedited RNA
CC       gives rise to the small secreted glycoprotein sGP (AC Q91DD7), the +1A
CC       edited RNA gives rise to the full-length transmembrane glycoprotein GP
CC       (AC Q91DD8).;
CC   -!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AB050936; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   SMR; P0C770; -.
DR   Proteomes; UP000002322; Genome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Disulfide bond; Glycoprotein; RNA editing; Secreted; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..332
FT                   /note="Super small secreted glycoprotein"
FT                   /id="PRO_0000391495"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        109..136
FT                   /evidence="ECO:0000250"
FT   DISULFID        122..148
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   332 AA;  37496 MW;  D1AFC1BD29D68F35 CRC64;
     MGSGYQLLQL PRERFRKTSF LVWVIILFQR AISMPLGIVT NSTLKATEID QLVCRDKLSS
     TSQLKSVGLN LEGNGIATDV PSATKRWGFR SGVPPKVVSY EAGEWAENCY NLEIKKSDGS
     ECLPLPPDGV RGFPRCRYVH KVQGTGPCPG DLAFHKNGAF FLYDRLASTV IYRGTTFAEG
     VIAFLILSEP KKHFWKATPA HEPVNTTDDS TSYYMTLTLS YEMSNFGGEE SNTLFKVDNH
     TYVQLDRPHT PQFLVQLNET LRRNNRLSNS TGRLTWTVDP KIEPDVGEWA FWETKKKLFP
     TTSWRKLAFP NSINPHQQLL RSEPGGNCPR KN