ID   GLYCO_VSNJO             Reviewed;         517 AA.
AC   P04882;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Glycoprotein;
DE   Flags: Precursor;
GN   Name=G;
OS   Vesicular stomatitis New Jersey virus (strain Ogden subtype Concan)
OS   (VSNJV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC   Vesiculovirus.
OX   NCBI_TaxID=11283;
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=6298453; DOI=10.1128/jvi.46.1.162-169.1983;
RA   Gallione C.J., Rose J.K.;
RT   "Nucleotide sequence of a cDNA clone encoding the entire glycoprotein from
RT   the New Jersey serotype of vesicular stomatitis virus.";
RL   J. Virol. 46:162-169(1983).
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.
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   -!- MISCELLANEOUS: The Ogden glycoprotein is missing the basolateral
CC       targeting signal in the cytoplasmic domain, therefore this protein
CC       should not be targeted correctly to the neurons dendrites as the other
CC       VSV G. Palmitoylation site is also missing on this domain.
CC   -!- SIMILARITY: Belongs to the vesiculovirus glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; V01214; CAA24525.1; -; Unassigned_RNA.
DR   PIR; A04118; VGVNVJ.
DR   SMR; P04882; -.
DR   PRIDE; P04882; -.
DR   Proteomes; UP000007626; Genome.
DR   GO; GO:0044177; C:host cell Golgi apparatus; IDA:UniProtKB.
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; Signal; Transmembrane;
KW   Transmembrane helix; 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..16
FT   CHAIN           17..517
FT                   /note="Glycoprotein"
FT                   /id="PRO_0000041003"
FT   TOPO_DOM        17..474
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        475..495
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        496..517
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        179
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        40..304
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..273
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   517 AA;  58230 MW;  A5F0B008B3490194 CRC64;
     MLSYLIFALA VSPILGKIEI VFPQHTTGDW KRVPHEYNYC PTSADKNSHG TQTGIPVELT
     MPKGLTTHQV EGFMCHSALW MTTCDFRWYG PKYITHSIHN EEPTDYQCLE AIKSYKDGVS
     FNPGFPPQSC GYGTVTDAEA HIVTVTPHSV KVDEYTGEWI DPHFIGGRCK GQICETVHNS
     TKWFTSSDGE SVCSQLFTLV GGIFFSDSEE ITSMGLPETG IRSNYFPYIS TEGICKMPFC
     RKQGYKLKND LWFQIMDPDL DKTVRDLPHI KDCDLSSSII TPGEHATDIS LISDVERILD
     YALCQNTWSK IESGEPITPV DLSYLGPKNP GVGPVFTIIN GSLHYFTSKY LRVELESPVI
     PRMEGKVAGT RIVRQLWDQW FPFGEVEIGP NGVLKTKQGY KFPLHIIGTG EVDSDIKMER
     VVKHWEHPHI EAAQTFLKKD DTGEVLYYGD TGVSKNPVEL VEGWFSGWRS SLMGVLAVII
     GFVILMFLIK LIGVLSSLFR PKRRPIYKSD VEMAHFR