GLYCO_PIRYV
ID GLYCO_PIRYV Reviewed; 529 AA.
AC Q85213;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 29-SEP-2021, entry version 78.
DE RecName: Full=Glycoprotein;
DE Flags: Precursor;
GN Name=G;
OS Piry virus (PIRYV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=11274;
OH NCBI_TaxID=126289; Gracilinanus microtarsus (Brazilian gracile mouse opossum).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1454546; DOI=10.1093/nar/20.21.5843;
RA Barik S.;
RT "The phosphoprotein (P) gene of the rhabdovirus Piry: its cloning,
RT sequencing, and expression in Escherichia coli.";
RL Nucleic Acids Res. 20:5843-5843(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8724858; DOI=10.1159/000150451;
RA Brun G., Bao X., Prevec L.;
RT "The relationship of Piry virus to other vesiculoviruses: a re-evaluation
RT based on the glycoprotein gene sequence.";
RL Intervirology 38:274-282(1995).
CC -!- FUNCTION: Attaches the virus to host cellular receptor, inducing
CC endocytosis of the virion. In the endosome, the acidic pH induces
CC conformational changes in the glycoprotein trimer, which trigger fusion
CC between virus and cell membrane (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- PTM: Glycosylated by host. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the vesiculovirus glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; D26175; BAA05163.1; -; Genomic_RNA.
DR SMR; Q85213; -.
DR PRIDE; Q85213; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR001903; Rhabd_glycop.
DR Pfam; PF00974; Rhabdo_glycop; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Host-virus interaction; Lipoprotein;
KW Membrane; Palmitate; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..529
FT /note="Glycoprotein"
FT /id="PRO_0000287248"
FT TOPO_DOM 19..469
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..529
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 42..304
FT /evidence="ECO:0000250"
FT DISULFID 77..110
FT /evidence="ECO:0000250"
FT DISULFID 86..132
FT /evidence="ECO:0000250"
FT DISULFID 171..176
FT /evidence="ECO:0000250"
FT DISULFID 195..240
FT /evidence="ECO:0000250"
FT DISULFID 235..273
FT /evidence="ECO:0000250"
SQ SEQUENCE 529 AA; 59771 MW; 9343868D5B67CA9F CRC64;
MDLFPILVVV LMTDTVLGKF QIVFPDQNEL EWRPVVGDSR HCPQSSEMQF DGSRSQTILT
GKAPVGITPS KSDGFICHAA KWVTTCDFRW YGPKYITHSI HHLRPTTSDC ETALQRYKDG
SLINLGFPPE SCGYATVTDS EAMLVQVTPH HVGVDDYRGH WIDPLFPGGE CSTNFCDTVH
NSSVWIPKSQ KTDICAQSFK NIKMTASYPS EGALVSDRFA FHSAYHPNMP GSTVCIMDFC
EQKGLRFTNG EWMGLNVEQS IREKKISAIF PNCVAGTEIR ATLESEGART LTWETQRMLD
YSLCQNTWDK VSRKEPLSPL DLSYLSPRAP GKGMAYTVIN GTLHSAHAKY IRTWIDYGEM
KEIKGGRGEY SKAPELLWSQ WFDFGPFKIG PNGLLHTGKT FKFPLYLIGA GIIDEDLHEL
DEAAPIDHPQ MPDAKSVLPE DEEIFFGDTG VSKNPIELIQ GWFSNWRESV MAIVGIVLLI
VVTFLAIKTV RVLNCLWRPR KKRIVRQEVD VESRLNHFEM RGFPEYVKR