GLYCO_VSIVA
ID GLYCO_VSIVA Reviewed; 511 AA.
AC P03522;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Glycoprotein;
DE Flags: Precursor;
GN Name=G;
OS Vesicular stomatitis Indiana virus (strain San Juan) (VSIV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Rhabdoviridae; Alpharhabdovirinae;
OC Vesiculovirus.
OX NCBI_TaxID=11285;
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=6268840; DOI=10.1128/jvi.39.2.519-528.1981;
RA Rose J.K., Gallione C.J.;
RT "Nucleotide sequences of the mRNA's encoding the vesicular stomatitis virus
RT G and M proteins determined from cDNA clones containing the complete coding
RT regions.";
RL J. Virol. 39:519-528(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=San Juan 56-NM-B;
RX PubMed=2168974; DOI=10.1128/jvi.64.10.4873-4883.1990;
RA Bilsel P.A., Nichol S.T.;
RT "Polymerase errors accumulating during natural evolution of the
RT glycoprotein gene of vesicular stomatitis virus Indiana serotype
RT isolates.";
RL J. Virol. 64:4873-4883(1990).
RN [3]
RP PALMITOYLATION AT CYS-489, AND MUTAGENESIS OF CYS-489.
RX PubMed=6326102; DOI=10.1073/pnas.81.7.2050;
RA Rose J.K., Adams G.A., Gallione C.J.;
RT "The presence of cysteine in the cytoplasmic domain of the vesicular
RT stomatitis virus glycoprotein is required for palmitate addition.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:2050-2054(1984).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=1850035; DOI=10.1128/jvi.65.5.2622-2628.1991;
RA Rigaut K.D., Birk D.E., Lenard J.;
RT "Intracellular distribution of input vesicular stomatitis virus proteins
RT after uncoating.";
RL J. Virol. 65:2622-2628(1991).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=8144707; DOI=10.1242/jcs.1993.supplement_17.13;
RA de Hoop M.J., Dotti C.G.;
RT "Membrane traffic in polarized neurons in culture.";
RL J. Cell Sci. Suppl. 17:85-92(1993).
RN [6]
RP MUTAGENESIS OF LYS-496; LYS-497; ARG-498; GLN-499; ILE-500; TYR-501;
RP THR-502; ASP-503; ILE-504; GLU-505 AND MET-506.
RX PubMed=8195226; DOI=10.1016/s0021-9258(17)40742-3;
RA Thomas D.C., Roth M.G.;
RT "The basolateral targeting signal in the cytoplasmic domain of glycoprotein
RT G from vesicular stomatitis virus resembles a variety of intracellular
RT targeting motifs related by primary sequence but having diverse targeting
RT activities.";
RL J. Biol. Chem. 269:15732-15739(1994).
RN [7]
RP TROPISM.
RX PubMed=11773406; DOI=10.1128/jvi.76.3.1309-1327.2002;
RA van den Pol A.N., Dalton K.P., Rose J.K.;
RT "Relative neurotropism of a recombinant rhabdovirus expressing a green
RT fluorescent envelope glycoprotein.";
RL J. Virol. 76:1309-1327(2002).
RN [8]
RP BIOTECHNOLOGY.
RX PubMed=16101513; DOI=10.2174/1566523054546224;
RA Cronin J., Zhang X.Y., Reiser J.;
RT "Altering the tropism of lentiviral vectors through pseudotyping.";
RL Curr. Gene Ther. 5:387-398(2005).
RN [9]
RP FUNCTION.
RX PubMed=20941355; DOI=10.1371/journal.ppat.1001127;
RA Cureton D.K., Massol R.H., Whelan S.P., Kirchhausen T.;
RT "The length of vesicular stomatitis virus particles dictates a need for
RT actin assembly during clathrin-dependent endocytosis.";
RL PLoS Pathog. 6:E1001127-E1001127(2010).
RN [10]
RP FUNCTION.
RC STRAIN=Orsay;
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).
RN [11]
RP FUNCTION.
RX PubMed=22383886; DOI=10.1371/journal.ppat.1002556;
RA Albertini A.A., Merigoux C., Libersou S., Madiona K., Bressanelli S.,
RA Roche S., Lepault J., Melki R., Vachette P., Gaudin Y.;
RT "Characterization of monomeric intermediates during VSV glycoprotein
RT structural transition.";
RL PLoS Pathog. 8:E1002556-E1002556(2012).
RN [12]
RP FUNCTION, AND INTERACTION WITH HOST LDLR.
RX PubMed=23589850; DOI=10.1073/pnas.1214441110;
RA Finkelshtein D., Werman A., Novick D., Barak S., Rubinstein M.;
RT "LDL receptor and its family members serve as the cellular receptors for
RT vesicular stomatitis virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:7306-7311(2013).
RN [13] {ECO:0007744|PDB:3EGD}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 499-508.
RX PubMed=18843296; DOI=10.1038/emboj.2008.208;
RA Mancias J.D., Goldberg J.;
RT "Structural basis of cargo membrane protein discrimination by the human
RT COPII coat machinery.";
RL EMBO J. 27:2918-2928(2008).
CC -!- FUNCTION: Attaches the virus to host LDL receptors, inducing clathrin-
CC dependent endocytosis of the virion. {ECO:0000269|PubMed:20941355,
CC ECO:0000269|PubMed:23589850}.
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:0000269|PubMed:20921141,
CC ECO:0000269|PubMed:22383886}.
CC -!- SUBUNIT: Homotrimer. Interacts with host LDL at target cell surface
CC (PubMed:23589850). {ECO:0000269|PubMed:23589850}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:1850035,
CC ECO:0000269|PubMed:8144707}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:8144707}. Host membrane
CC {ECO:0000269|PubMed:8144707}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:8144707}. Note=The cytoplasmic domain sorts the
CC protein to neurons dentrites instead of axons. When expressed in ex
CC vivo polarized cells like epithelial cells, it sorts the protein to the
CC basolateral side.
CC -!- PTM: Glycosylated by host. {ECO:0000269|PubMed:6326102}.
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 {ECO:0000269|PubMed:16101513}.
CC -!- SIMILARITY: Belongs to the vesiculovirus glycoprotein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J02428; AAA48370.1; -; Genomic_RNA.
DR EMBL; M35219; AAA48389.1; -; Genomic_RNA.
DR RefSeq; NP_041715.1; NC_001560.1.
DR PDB; 3EGD; X-ray; 2.70 A; D=499-508.
DR PDBsum; 3EGD; -.
DR SMR; P03522; -.
DR ELM; P03522; -.
DR ChEMBL; CHEMBL4295565; -.
DR GeneID; 1489834; -.
DR KEGG; vg:1489834; -.
DR EvolutionaryTrace; P03522; -.
DR Proteomes; UP000002327; 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 3D-structure; Clathrin-mediated endocytosis of virus by host;
KW Disulfide bond; 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..16
FT CHAIN 17..511
FT /note="Glycoprotein"
FT /id="PRO_0000041005"
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 LIPID 489
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:6326102"
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 MUTAGEN 489
FT /note="C->S: Complete loss of palmitoylation."
FT /evidence="ECO:0000269|PubMed:6326102"
FT MUTAGEN 496
FT /note="K->A: No effect on basolateral targeting ex vivo."
FT /evidence="ECO:0000269|PubMed:8195226"
FT MUTAGEN 497
FT /note="K->A: No effect on basolateral targeting ex vivo."
FT /evidence="ECO:0000269|PubMed:8195226"
FT MUTAGEN 498
FT /note="R->A: No effect on basolateral targeting ex vivo."
FT /evidence="ECO:0000269|PubMed:8195226"
FT MUTAGEN 499
FT /note="Q->A: No effect on basolateral targeting ex vivo."
FT /evidence="ECO:0000269|PubMed:8195226"
FT MUTAGEN 500
FT /note="I->A: No effect on basolateral targeting ex vivo."
FT /evidence="ECO:0000269|PubMed:8195226"
FT MUTAGEN 501
FT /note="Y->A: Complete loss of basolateral targeting ex
FT vivo."
FT /evidence="ECO:0000269|PubMed:8195226"
FT MUTAGEN 502
FT /note="T->A: No effect on basolateral targeting ex vivo."
FT /evidence="ECO:0000269|PubMed:8195226"
FT MUTAGEN 503
FT /note="D->A: No effect on basolateral targeting ex vivo."
FT /evidence="ECO:0000269|PubMed:8195226"
FT MUTAGEN 504
FT /note="I->A: Complete loss of basolateral targeting ex
FT vivo."
FT /evidence="ECO:0000269|PubMed:8195226"
FT MUTAGEN 505
FT /note="E->A: No effect on basolateral targeting ex vivo."
FT /evidence="ECO:0000269|PubMed:8195226"
FT MUTAGEN 506
FT /note="M->A: No effect on basolateral targeting ex vivo."
FT /evidence="ECO:0000269|PubMed:8195226"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:3EGD"
SQ SEQUENCE 511 AA; 57482 MW; 26E94F713AC0B8E6 CRC64;
MKCLLYLAFL FIGVNCKFTI VFPHNQKGNW KNVPSNYHYC PSSSDLNWHN DLIGTAIQVK
MPKSHKAIQA DGWMCHASKW VTTCDFRWYG PKYITQSIRS FTPSVEQCKE SIEQTKQGTW
LNPGFPPQSC GYATVTDAEA VIVQVTPHHV LVDEYTGEWV DSQFINGKCS NYICPTVHNS
TTWHSDYKVK GLCDSNLISM DITFFSEDGE LSSLGKEGTG FRSNYFAYET GGKACKMQYC
KHWGVRLPSG VWFEMADKDL FAAARFPECP EGSSISAPSQ TSVDVSLIQD VERILDYSLC
QETWSKIRAG LPISPVDLSY LAPKNPGTGP AFTIINGTLK YFETRYIRVD IAAPILSRMV
GMISGTTTER ELWDDWAPYE DVEIGPNGVL RTSSGYKFPL YMIGHGMLDS DLHLSSKAQV
FEHPHIQDAA SQLPDDESLF FGDTGLSKNP IELVEGWFSS WKSSIASFFF IIGLIIGLFL
VLRVGIHLCI KLKHTKKRQI YTDIEMNRLG K
