GLYCO_VSIVO
ID GLYCO_VSIVO Reviewed; 511 AA.
AC P04884;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 23-FEB-2022, entry version 93.
DE RecName: Full=Glycoprotein;
DE Flags: Precursor;
GN Name=G;
OS Vesicular stomatitis Indiana virus (strain Orsay) (VSIV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=11284;
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 [MRNA], AND PALMITOYLATION AT CYS-489.
RX PubMed=2985803; DOI=10.1128/jvi.54.2.374-382.1985;
RA Gallione C.J., Rose J.K.;
RT "A single amino acid substitution in a hydrophobic domain causes
RT temperature-sensitive cell-surface transport of a mutant viral
RT glycoprotein.";
RL J. Virol. 54:374-382(1985).
RN [2]
RP FUNCTION.
RX PubMed=20921141; DOI=10.1083/jcb.201006116;
RA Libersou S., Albertini A.A., Ouldali M., Maury V., Maheu C., Raux H.,
RA de Haas F., Roche S., Gaudin Y., Lepault J.;
RT "Distinct structural rearrangements of the VSV glycoprotein drive membrane
RT fusion.";
RL J. Cell Biol. 191:199-210(2010).
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. {ECO:0000269|PubMed:20921141}.
CC -!- SUBUNIT: Homotrimer.
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. Palmitoylated by host on Cys-489 (By
CC similarity). {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; M11048; AAA48438.1; -; mRNA.
DR SMR; P04884; -.
DR IntAct; P04884; 2.
DR MINT; P04884; -.
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; Lipoprotein; Membrane; Palmitate; 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 CHAIN 17..511
FT /note="Glycoprotein"
FT /id="PRO_0000041004"
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 LIPID 489
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:2985803"
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"
FT VARIANT 204
FT /note="F -> S (in temperature-sensitive mutant TSO45, which
FT exhibits temperature-sensitive cell-surface transport)"
SQ SEQUENCE 511 AA; 57571 MW; A10E67B6F8138179 CRC64;
MKCLLYLAFL FIGVNCKFTI VFPHNQKGNW KNVPSNYHYC PSSSDLNWHN DLIGTALQVK
MPKSHKAIQA DGWMCHASKW VTTCDFRWYG PKYITHSIRS FTPSVEQCKE SIEQTKQGTW
LNPGFPPQSC GYATVTDAEA AIVQVTPHHV LVDEYTGEWV DSQFINGKCS NDICPTVHNS
TTWHSDYKVK GLCDSNLIST DITFFSEDGE LSSLGKEGTG FRSNYFAYET GDKACKMQYC
KHWGVRLPSG VWFEMADKDL FAAARFPECP EGSSISAPSQ TSVDVSLIQD VERILDYSLC
QETWSKIRAG LPISPVDLSY LAPKNPGTGP VFTIINGTLK YFETRYIRVD IAAPILSRMV
GMISGTTTER ELWDDWAPYE DVEIGPNGVL RTSLGYKFPL YMIGHGMLDS DLHLSSKAQV
FEHPHIQDAA SQLPDDETLF FGDTGLSKNP IEFVEGWFSS WKSSIASFFF IIGLIIGLFL
VLRVGIYLCI KLKHTKKRQI YTDIEMNRLG K
