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Glycoprotein

 GLYCO_VSIVN             Reviewed;         511 AA.
Q8B0I1;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
16-JAN-2019, entry version 59.
RecName: Full=Glycoprotein;
Flags: Precursor;
Name=G;
Vesicular stomatitis Indiana virus (strain 98COE North America)
(VSIV).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Rhabdoviridae; Vesiculovirus.
NCBI_TaxID=434488;
NCBI_TaxID=7158; Aedes.
NCBI_TaxID=9913; Bos taurus (Bovine).
NCBI_TaxID=58271; Culicoides.
NCBI_TaxID=9793; Equus asinus (Donkey) (Equus africanus asinus).
NCBI_TaxID=9796; Equus caballus (Horse).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=252607; Lutzomyia.
NCBI_TaxID=7370; Musca domestica (House fly).
NCBI_TaxID=7190; Simuliidae (black flies).
NCBI_TaxID=9823; Sus scrofa (Pig).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=12237430;
Rodriguez L.L., Pauszek S.J., Bunch T.A., Schumann K.R.;
"Full-length genome analysis of natural isolates of vesicular
stomatitis virus (Indiana 1 serotype) from North, Central and South
America.";
J. Gen. Virol. 83:2475-2483(2002).
-!- FUNCTION: Attaches the virus to host cellular receptor, inducing
clathrin-dependent endocytosis of the virion. In the endosome, the
acidic pH induces conformational changes in the glycoprotein
trimer, which trigger fusion between virus and endosomal membrane.
In neurons, neo-synthesized glycoproteins are sorted to the
dendrites, where the virus buds (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homotrimer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Virion membrane; Single-pass type I membrane
protein. Host membrane; Single-pass type I membrane protein.
Note=The cytoplasmic domain sorts the protein to neurons dentrites
instead of axons. When expressed in ex vivo polarized cells like
epithelial cells, it sorts the protein to the basolateral side (By
similarity). {ECO:0000250}.
-!- PTM: Glycosylated by host. Palmitoylated by host on Cys-489 (By
similarity). {ECO:0000250}.
-!- BIOTECHNOLOGY: Used to pseudotype many virus-like particles like
lentiviral vector, because of its broad spectrum of host cell
tropism. Also used in viral vectors studies in cancer therapy.
-!- SIMILARITY: Belongs to the vesiculovirus glycoprotein family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AF473864; AAN16983.1; -; Genomic_RNA.
ProteinModelPortal; Q8B0I1; -.
SMR; Q8B0I1; -.
Proteomes; UP000007624; Genome.
GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR001903; Rhabd_glycop.
Pfam; PF00974; Rhabdo_glycop; 1.
1: Evidence at protein level;
Clathrin-mediated endocytosis of virus by host; Complete proteome;
Disulfide bond; Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host membrane; Host-virus interaction; Lipoprotein; Membrane;
Palmitate; Signal; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral envelope protein;
Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 511 Glycoprotein.
/FTId=PRO_0000287252.
TOPO_DOM 17 467 Virion surface. {ECO:0000255}.
TRANSMEM 468 488 Helical. {ECO:0000255}.
TOPO_DOM 489 511 Intravirion. {ECO:0000255}.
MOTIF 496 506 basolateral targeting ex vivo.
{ECO:0000250}.
LIPID 489 489 S-palmitoyl cysteine; by host.
{ECO:0000250}.
CARBOHYD 179 179 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 336 336 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 40 300 {ECO:0000250}.
DISULFID 75 108 {ECO:0000250}.
DISULFID 84 130 {ECO:0000250}.
DISULFID 169 174 {ECO:0000250}.
DISULFID 193 240 {ECO:0000250}.
DISULFID 235 269 {ECO:0000250}.
SEQUENCE 511 AA; 57340 MW; 0DBEFB1C90B297F6 CRC64;
MKCLLYLAFL SIGVNCKFTI VFPHNQKGTW KNVPSNYHYC PSSSDLNWHN DLIGTALQVK
MPKSHKAIQA DGWMCHASKW VTTCDFRWYG PKYITHSIRS FTPSVEQCRE SIEQTKQGTW
LNPGFPPQSC GYATVTDAEA VIVQVTPHHV LVDEYTGEWV DSQFINGKCS NDICPTVHNS
TTWHSDYKVK GLCDSNLISM DITFFSEDGE LSSLGKEGTG FRSNHFAYET GDKACKMQYC
KHWGVRLPSG VWFEMADQDL FAAARFPECP EGSSISAPSQ TSVDVSLIQD VERILDYSLC
QETWSKIGAG LPISPVDLSY LAPKNPGTGP AFTIINGTLK YFETRYIRVD IAAPILSRMV
GMISGTTTER ELWDDWAPYE DVEIGPNGVL RTSSGYKFPL YMIGHGMLDS DLHLSSKAQV
FEHPHIQDAA SQLPDDETLF FGDTGLSKNP IELVEGWFSG WKSSIASFFF IIGLIIGLFL
VLRVGIYLCI KLKHTKKRQI YTDIEMNRLG K


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Kits Elisa; taq POLYMERASE

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Pathways :
WP1970: Glycoprotein VI platelet signaling

Related Genes :
[GP] Envelopment polyprotein (Glycoprotein precursor) (M polyprotein) [Cleaved into: Glycoprotein N (Gn) (Glycoprotein G2); Glycoprotein C (Gc) (Glycoprotein G1)]
[RHAG RH50] Ammonium transporter Rh type A (Erythrocyte membrane glycoprotein Rh50) (Erythrocyte plasma membrane 50 kDa glycoprotein) (Rh50A) (Rhesus blood group family type A glycoprotein) (Rh family type A glycoprotein) (Rh type A glycoprotein) (Rhesus blood group-associated ammonia channel) (Rhesus blood group-associated glycoprotein) (CD antigen CD241)
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p110) [Cleaved into: Capsid protein (Coat protein) (C); Spike glycoprotein E2 (E2 envelope glycoprotein); Spike glycoprotein E1 (E1 envelope glycoprotein)]
[GP] Envelopment polyprotein (M polyprotein) [Cleaved into: NSm-Gn protein (p78 protein); Glycoprotein N (Gn) (Glycoprotein G1); Glycoprotein C (Gc) (Glycoprotein G2)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]
[] Structural polyprotein (p130) [Cleaved into: Capsid protein (EC 3.4.21.90) (Coat protein) (C); Precursor of protein E3/E2 (p62) (pE2); Assembly protein E3; Spike glycoprotein E2 (E2 envelope glycoprotein); 6K protein; Spike glycoprotein E1 (E1 envelope glycoprotein)]

Bibliography :
[30897421] Probing and pressing surfaces of hepatitis C virus-like particles.
[30897325] Discovery and Mechanistic Study of Tailor-Made Quinoline Derivatives as Topoisomerase 1 Poisons with Potent Anticancer Activity.
[30897286] Brain region-specific regulation of histone acetylation and efflux transporters in mice.
[30897192] Zinc alpha 2 glycoprotein as an early biomarker of diabetic nephropathy in patients with type 2 diabetes mellitus.
[30897171] Expanding the watch list for potential Ebola virus antibody escape mutations.
[30896677] Exposure of von Willebrand factor on isolated hepatocytes promotes tethering of platelets to the cell surface.
[30896652] Prognositic significance of P-cadherin expression in breast cancer: Protocol for a meta-analysis.
[30896502] Knockdown of long noncoding RNA-taurine-upregulated gene 1 inhibits tumor angiogenesis in ovarian cancer by regulating leucine-rich α-2-glycoprotein-1.
[30895150] Abundant proteins in platelet-rich fibrin and their potential contribution to wound healing: An explorative proteomics study and review of the literature.
[30894498] OR14I1 is a receptor for the human cytomegalovirus pentameric complex and defines viral epithelial cell tropism.
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