ID   GLYCO_VSIVG             Reviewed;         511 AA.
AC   P04883;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Vesicular stomatitis Indiana virus (strain Glasgow) (VSIV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Vesiculovirus.
OX   NCBI_TaxID=11278;
OH   NCBI_TaxID=7158; Aedes.
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
OH   NCBI_TaxID=58271; Culicoides.
OH   NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
OH   NCBI_TaxID=9796; Equus caballus (Horse).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=252607; Lutzomyia.
OH   NCBI_TaxID=7370; Musca domestica (House fly).
OH   NCBI_TaxID=7190; Simuliidae (black flies).
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3005478; DOI=10.1099/0022-1317-67-3-441;
RA   Vandepol S.B., Holland J.J.;
RT   "Evolution of vesicular stomatitis virus in athymic nude mice: mutations
RT   associated with natural killer cell selection.";
RL   J. Gen. Virol. 67:441-451(1986).
CC   -!- FUNCTION: Attaches the virus to host cellular receptor, inducing
CC       clathrin-dependent endocytosis of the virion. In the endosome, the
CC       acidic pH induces conformational changes in the glycoprotein trimer,
CC       which trigger fusion between virus and endosomal membrane. In neurons,
CC       neo-synthesized glycoproteins are sorted to the dendrites, where the
CC       virus buds (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane
CC       protein. Host membrane; Single-pass type I membrane protein. Note=The
CC       cytoplasmic domain sorts the protein to neurons dentrites instead of
CC       axons. When expressed in ex vivo polarized cells like epithelial cells,
CC       it sorts the protein to the basolateral side (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Glycosylated by host. {ECO:0000250}.
CC   -!- BIOTECHNOLOGY: Used to pseudotype many virus-like particles like
CC       lentiviral vector, because of its broad spectrum of host cell tropism.
CC       Also used in viral vectors studies in cancer therapy.
CC   -!- SIMILARITY: Belongs to the vesiculovirus glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; X03633; CAA27283.1; -; Genomic_RNA.
DR   SMR; P04883; -.
DR   Proteomes; UP000007544; 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   1: Evidence at protein level;
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; Membrane; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW   Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW   Virus endocytosis by host; Virus entry into host cell.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..511
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000041002"
FT   TOPO_DOM        17..467
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        468..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        489..511
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   MOTIF           496..506
FT                   /note="basolateral targeting ex vivo"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        40..300
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..108
FT                   /evidence="ECO:0000250"
FT   DISULFID        84..130
FT                   /evidence="ECO:0000250"
FT   DISULFID        169..174
FT                   /evidence="ECO:0000250"
FT   DISULFID        193..240
FT                   /evidence="ECO:0000250"
FT   DISULFID        235..269
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   511 AA;  57692 MW;  0DA18842E427C509 CRC64;
     MKCFLYLAFL FIGVNCKFTI VFPHNQKGNW KNVPSNYHYC PSSSDLNWHN DLIGTGLQVK
     MPKSHKAIQA DGWMCHASKW VTTCDFRWYG PKYITHSIRS FTPSVEQCKE SIEQTKQGTW
     LNPGFPPQSC GYATVTDAEA VIVQVTPHHV LVDEYTGEWV DSQFINGKCS NDICPTVHNS
     TTWHSDYKVK GLCDSNLIST DITFFSEDRE LSSLGKEGTG FRSNYFAYET GDKACKMQYC
     KHWGVRLPSG VWFEMADKDL FAAARFPECP EGSSISAPSQ TSVDVSLIQD VERILDYSLC
     QETWSKIRAG LPISPVDLSY LAPKNPGTGP AFTIINGTLK YFETRYIRVD IAAPILSRMV
     GMISGTTTER ELWDDWAPYE DVEIGPNGVL RTSSGYKFPL YMIGHGMLDS GLHLSSKAQV
     FEHPHIQDAA SQLPDDEILF FGDTGLSKNP IDFVEGWFSS WKSSIASFFF IIGLIIGLFL
     VLRVGIYLYI KLKHTKKRQI YTDIEMNRLG R