ID   GLYCO_TUPVT             Reviewed;         531 AA.
AC   Q4VKV3;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   23-FEB-2022, entry version 34.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Tupaia virus (isolate Tupaia/Thailand/-/1986) (TUPV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Tupavirus.
OX   NCBI_TaxID=1560034;
OH   NCBI_TaxID=9394; Tupaia.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=15890917; DOI=10.1128/jvi.79.11.6781-6790.2005;
RA   Springfeld C., Darai G., Cattaneo R.;
RT   "Characterization of the Tupaia rhabdovirus genome reveals a long open
RT   reading frame overlapping with P and a novel gene encoding a small
RT   hydrophobic protein.";
RL   J. Virol. 79:6781-6790(2005).
CC   -!- FUNCTION: Attaches the virus to host receptors, inducing clathrin-
CC       dependent endocytosis of the virion. {ECO:0000250|UniProtKB:P03522}.
CC   -!- FUNCTION: In the endosome, the acidic pH induces conformational changes
CC       in the glycoprotein trimer, which trigger fusion between virus and
CC       endosomal membrane. {ECO:0000250|UniProtKB:P03522}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P03522}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250|UniProtKB:P03522};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:P03522}.
CC       Host membrane {ECO:0000250|UniProtKB:P03522}; Single-pass type I
CC       membrane protein {ECO:0000250|UniProtKB:P03522}.
CC   -!- PTM: Glycosylated by host. {ECO:0000250|UniProtKB:P03522}.
CC   -!- SIMILARITY: Belongs to the vesiculovirus glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AY840978; AAX47601.1; -; Genomic_RNA.
DR   RefSeq; YP_238533.1; NC_007020.1.
DR   SMR; Q4VKV3; -.
DR   GeneID; 3416614; -.
DR   KEGG; vg:3416614; -.
DR   Proteomes; UP000029771; Genome.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
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:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; 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   Clathrin-mediated endocytosis of virus by host; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein; Host membrane;
KW   Host-virus interaction; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW   Viral attachment to host cell; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW   Virus entry into host cell.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..531
FT                   /note="Glycoprotein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000432049"
FT   TOPO_DOM        22..492
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        514..531
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   DISULFID        44..318
FT                   /evidence="ECO:0000250"
FT   DISULFID        77..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        86..132
FT                   /evidence="ECO:0000250"
FT   DISULFID        171..177
FT                   /evidence="ECO:0000250"
FT   DISULFID        235..287
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   531 AA;  59336 MW;  BF8C7D085F5571BB CRC64;
     MAPQTISLLW AMVCVSVYTR ANRVVAPIHE PQNWKPATVD DFTCRTGFNL DFDSKFIKTK
     ALVLKRVGQA KVKGYLCMKN RWTTTCETNW LYSKSVSHHI THVAVSAEEC YNKIRDDASG
     NLKIESYPNP QCAWSSTVSR EEDFIHISTS DVGYDMYTDT VLSPSFPGGT CKLKTCCKTI
     YPNIVWVPET PAQTQVRDAL FDETMVTVTV EAKKVVKDSW VTGATITPSV MEGSCKKTLG
     SKSGILLPNG QWFSIVETGQ ITIQPKGSVE EKETWVNLIN DLNLSDCAET QEAKVPTAEF
     TVYKTESMVF NILNYHLCLE TVAKARSGKN LTRLDLARLA PEIPGVAHVY QLTSDGVRVG
     STRYEIIAWK PTMGLDKTLG LTIVPSGNRN SETIKWIEWT RTDDGLLNGP NGIFIADGKE
     IVHPNLKMVS FELETYLISE HSTQLVPHPV IHSISDEIYP ENYTIGGKNS YIKIHTPTAY
     FWSGIHWIEG AVQKLFIVVV ATALIGLFIL VVWLCCGCCS KSRPVRNQKW E