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Envelope glycoprotein (GP1,2) (GP) [Cleaved into: GP1; GP2; GP2-delta]

 VGP_EBOZM               Reviewed;         676 AA.
Q05320; Q66818; Q77LU5; Q8B9S1; Q8JS62;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
05-DEC-2018, entry version 132.
RecName: Full=Envelope glycoprotein;
AltName: Full=GP1,2;
Short=GP;
Contains:
RecName: Full=Shed GP;
AltName: Full=GP1,2-delta;
Contains:
RecName: Full=GP1;
Contains:
RecName: Full=GP2;
Flags: Precursor;
Name=GP;
Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus).
Viruses; ssRNA viruses; ssRNA negative-strand viruses;
Mononegavirales; Filoviridae; Ebolavirus.
NCBI_TaxID=128952;
NCBI_TaxID=77231; Epomops franqueti (Franquet's epauleted fruit bat).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=8237108; DOI=10.1016/0168-1702(93)90063-S;
Sanchez A., Kiley M.P., Holloway B.P., Auperin D.D.;
"Sequence analysis of the Ebola virus genome: organization, genetic
elements, and comparison with the genome of Marburg virus.";
Virus Res. 29:215-240(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA / MRNA], AND RNA EDITING.
PubMed=8553543; DOI=10.1006/viro.1995.0052;
Volchkov V.E., Becker S., Volchkova V.A., Ternovoj V.A., Kotov A.N.,
Netesov S.V., Klenk H.-D.;
"GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by
T7 and vaccinia virus polymerases.";
Virology 214:421-430(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
PubMed=8622982; DOI=10.1073/pnas.93.8.3602;
Sanchez A., Trappier S.G., Mahy B.W.J., Peters C.J., Nichol S.T.;
"The virion glycoproteins of Ebola viruses are encoded in two reading
frames and are expressed through transcriptional editing.";
Proc. Natl. Acad. Sci. U.S.A. 93:3602-3607(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate guinea pig-adapted;
PubMed=11062045; DOI=10.1006/viro.2000.0572;
Volchkov V.E., Chepurnov A.A., Volchkova V.A., Ternovoj V.A.,
Klenk H.D.;
"Molecular characterization of guinea pig-adapted variants of Ebola
virus.";
Virology 277:147-155(2000).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Volchkov V.E.;
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Isolate mouse-adapted;
Wilson J.A., Kondig J.P., Kuehne A.I., Hart M.K.;
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 359-676.
PubMed=1299611; DOI=10.1016/0014-5793(92)80662-Z;
Volchkov V.E., Blinov V.M., Netesov S.V.;
"The envelope glycoprotein of Ebola virus contains an
immunosuppressive-like domain similar to oncogenic retroviruses.";
FEBS Lett. 305:181-184(1992).
[8]
PROTEOLYTIC PROCESSING OF ENVELOPE GLYCOPROTEIN, AND TOPOLOGY.
PubMed=9576958; DOI=10.1073/pnas.95.10.5762;
Volchkov V.E., Feldmann H., Volchkova V.A., Klenk H.-D.;
"Processing of the Ebola virus glycoprotein by the proprotein
convertase furin.";
Proc. Natl. Acad. Sci. U.S.A. 95:5762-5767(1998).
[9]
PROTEOLYTIC PROCESSING OF ENVELOPE GLYCOPROTEIN.
PubMed=9614872; DOI=10.1006/viro.1998.9143;
Volchkov V.E., Volchkova V.A., Slenczka W., Klenk H.-D., Feldmann H.;
"Release of viral glycoproteins during Ebola virus infection.";
Virology 245:110-119(1998).
[10]
DOMAIN FUSION PEPTIDE.
PubMed=9499027;
Ruiz-Arguello M.B., Goni F.M., Pereira F.B., Nieva J.L.;
"Phosphatidylinositol-dependent membrane fusion induced by a putative
fusogenic sequence of Ebola virus.";
J. Virol. 72:1775-1781(1998).
[11]
DOMAIN FUSION PEPTIDE, AND MUTAGENESIS OF GLY-528; LEU-529; ILE-532;
PHE-535; GLY-536 AND PRO-537.
PubMed=10482652;
Ito H., Watanabe S., Sanchez A., Whitt M.A., Kawaoka Y.;
"Mutational analysis of the putative fusion domain of Ebola virus
glycoprotein.";
J. Virol. 73:8907-8912(1999).
[12]
PROTEOLYTIC PROCESSING OF ENVELOPE GLYCOPROTEIN, AND MUTAGENESIS OF
498-ARG--ARG-501.
PubMed=9882347;
Wool-Lewis R.J., Bates P.;
"Endoproteolytic processing of the ebola virus envelope glycoprotein:
cleavage is not required for function.";
J. Virol. 73:1419-1426(1999).
[13]
FUNCTION, AND DOMAIN MUCIN/LIKE REGION.
PubMed=10932225; DOI=10.1038/78645;
Yang Z.-Y., Duckers H.J., Sullivan N.J., Sanchez A., Nabel E.G.,
Nabel G.J.;
"Identification of the Ebola virus glycoprotein as the main viral
determinant of vascular cell cytotoxicity and injury.";
Nat. Med. 6:886-889(2000).
[14]
FUNCTION.
PubMed=11112476; DOI=10.1006/viro.2000.0601;
Takada A., Watanabe S., Ito H., Okazaki K., Kida H., Kawaoka Y.;
"Downregulation of beta1 integrins by Ebola virus glycoprotein:
implication for virus entry.";
Virology 278:20-26(2000).
[15]
PROTEOLYTIC PROCESSING OF ENVELOPE GLYCOPROTEIN, PALMITOYLATION AT
CYS-670 AND CYS-672, AND MUTAGENESIS OF 497-ARG--ARG-501; CYS-670 AND
CYS-672.
PubMed=11152533; DOI=10.1128/JVI.75.3.1576-1580.2001;
Ito H., Watanabe S., Takada A., Kawaoka Y.;
"Ebola virus glycoprotein: proteolytic processing, acylation, cell
tropism, and detection of neutralizing antibodies.";
J. Virol. 75:1576-1580(2001).
[16]
COILED-COIL DOMAIN.
PubMed=11024148; DOI=10.1128/JVI.74.21.10194-10201.2000;
Watanabe S., Takada A., Watanabe T., Ito H., Kida H., Kawaoka Y.;
"Functional importance of the coiled-coil of the Ebola virus
glycoprotein.";
J. Virol. 74:10194-10201(2000).
[17]
INTERACTION WITH HUMAN FOLR1.
PubMed=11461707; DOI=10.1016/S0092-8674(01)00418-4;
Chan S.Y., Empig C.J., Welte F.J., Speck R.F., Schmaljohn A.,
Kreisberg J.F., Goldsmith M.A.;
"Folate receptor-alpha is a cofactor for cellular entry by Marburg and
Ebola viruses.";
Cell 106:117-126(2001).
[18]
DISULFIDE BONDS, GLYCOSYLATION, AND MUTAGENESIS OF ASN-40; CYS-53;
CYS-108; CYS-121; CYS-135; CYS-147; ASN-204; ASN-238; ASN-257;
ASN-296; CYS-511; CYS-556; ASN-563; CYS-601; CYS-608; CYS-609;
ASN-618; CYS-670 AND CYS-672.
PubMed=12438572; DOI=10.1128/JVI.76.24.12463-12472.2002;
Jeffers S.A., Sanders D.A., Sanchez A.;
"Covalent modifications of the ebola virus glycoprotein.";
J. Virol. 76:12463-12472(2002).
[19]
DOWN-MODULATION OF HOST MHC-I; ALPHA/BETA INTEGRINS AND EGFR.
PubMed=11836430; DOI=10.1128/jvi.76.5.2518-2528.2002;
Simmons G., Wool-Lewis R.J., Baribaud F., Netter R.C., Bates P.;
"Ebola virus glycoproteins induce global surface protein down-
modulation and loss of cell adherence.";
J. Virol. 76:2518-2528(2002).
[20]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-670 AND CYS-672.
PubMed=11877482; DOI=10.1084/jem.20011500;
Bavari S., Bosio C.M., Wiegand E., Ruthel G., Will A.B.,
Geisbert T.W., Hevey M., Schmaljohn C., Schmaljohn A., Aman M.J.;
"Lipid raft microdomains: a gateway for compartmentalized trafficking
of Ebola and Marburg viruses.";
J. Exp. Med. 195:593-602(2002).
[21]
INTERACTION WITH HUMAN CD209 AND CLEC4M, AND ROLE IN TRANS INFECTION.
PubMed=12050398; DOI=10.1128/JVI.76.13.6841-6844.2002;
Alvarez C.P., Lasala F., Carrillo J., Muniz O., Corbi A.L.,
Delgado R.;
"C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola
virus in cis and in trans.";
J. Virol. 76:6841-6844(2002).
[22]
PUTATIVE ROLE OF FOLR1 IN VIRUS ENTRY INTO THE CELL.
PubMed=14645601; DOI=10.1128/JVI.77.24.13433-13438.2003;
Simmons G., Rennekamp A.J., Chai N., Vandenberghe L.H., Riley J.L.,
Bates P.;
"Folate receptor alpha and caveolae are not required for Ebola virus
glycoprotein-mediated viral infection.";
J. Virol. 77:13433-13438(2003).
[23]
INTERACTION WITH HUMAN CD209 AND CLEC4M.
PubMed=12504546; DOI=10.1006/viro.2002.1730;
Simmons G., Reeves J.D., Grogan C.C., Vandenberghe L.H., Baribaud F.,
Whitbeck J.C., Burke E., Buchmeier M.J., Soilleux E.J., Riley J.L.,
Doms R.W., Bates P., Poehlmann S.;
"DC-SIGN and DC-SIGNR bind ebola glycoproteins and enhance infection
of macrophages and endothelial cells.";
Virology 305:115-123(2003).
[24]
CLEAVAGE BY HOST ADAM17, MUTAGENESIS OF ASP-632; LYS-633; THR-634;
LEU-635; ASP-637; GLN-638; GLY-639; ASP-640; ASN-641; ASP-642 AND
ASN-643, AND SUBCELLULAR LOCATION.
PubMed=15103332; DOI=10.1038/sj.emboj.7600219;
Dolnik O., Volchkova V., Garten W., Carbonnelle C., Becker S.,
Kahnt J., Stroeher U., Klenk H.-D., Volchkov V.;
"Ectodomain shedding of the glycoprotein GP of Ebola virus.";
EMBO J. 23:2175-2184(2004).
[25]
INTERACTION WITH HUMAN CLEC10A.
PubMed=14990712; DOI=10.1128/JVI.78.6.2943-2947.2004;
Takada A., Fujioka K., Tsuiji M., Morikawa A., Higashi N., Ebihara H.,
Kobasa D., Feldmann H., Irimura T., Kawaoka Y.;
"Human macrophage C-type lectin specific for galactose and N-
acetylgalactosamine promotes filovirus entry.";
J. Virol. 78:2943-2947(2004).
[26]
FUNCTION IN ENDOTHELIAL CELLS ACTIVATION.
PubMed=16051836; DOI=10.1128/JVI.79.16.10442-10450.2005;
Wahl-Jensen V.M., Afanasieva T.A., Seebach J., Stroeher U.,
Feldmann H., Schnittler H.J.;
"Effects of Ebola virus glycoproteins on endothelial cell activation
and barrier function.";
J. Virol. 79:10442-10450(2005).
[27]
PROTEOLYSIS OF GP1.
PubMed=15831716; DOI=10.1126/science.1110656;
Chandran K., Sullivan N.J., Felbor U., Whelan S.P., Cunningham J.M.;
"Endosomal proteolysis of the Ebola virus glycoprotein is necessary
for infection.";
Science 308:1643-1645(2005).
[28]
FUNCTION OF GP1,2DELTA.
PubMed=15681442; DOI=10.1128/JVI.79.4.2413-2419.2005;
Wahl-Jensen V., Kurz S.K., Hazelton P.R., Schnittler H.J.,
Stroeher U., Burton D.R., Feldmann H.;
"Role of Ebola virus secreted glycoproteins and virus-like particles
in activation of human macrophages.";
J. Virol. 79:2413-2419(2005).
[29]
DOWN-MODULATION OF HOST INTEGRIN DIMER ALPHA-V/BETA-3, AND INTERACTION
WITH HUMAN INTEGRIN ITGAV.
PubMed=15596847; DOI=10.1128/JVI.79.1.547-553.2005;
Sullivan N.J., Peterson M., Yang Z.-Y., Kong W.-P., Duckers H.,
Nabel E., Nabel G.J.;
"Ebola virus glycoprotein toxicity is mediated by a dynamin-dependent
protein-trafficking pathway.";
J. Virol. 79:547-553(2005).
[30]
PROTEOLYSIS OF GP1.
PubMed=16571833; DOI=10.1128/JVI.80.8.4174-4178.2006;
Schornberg K., Matsuyama S., Kabsch K., Delos S., Bouton A., White J.;
"Role of endosomal cathepsins in entry mediated by the Ebola virus
glycoprotein.";
J. Virol. 80:4174-4178(2006).
[31]
FUNCTION.
PubMed=16603527; DOI=10.1099/vir.0.81361-0;
Alazard-Dany N., Volchkova V., Reynard O., Carbonnelle C., Dolnik O.,
Ottmann M., Khromykh A., Volchkov V.E.;
"Ebola virus glycoprotein GP is not cytotoxic when expressed
constitutively at a moderate level.";
J. Gen. Virol. 87:1247-1257(2006).
[32]
FUNCTION OF SIGNAL PEPTIDE.
PubMed=16775318; DOI=10.1128/JVI.02545-05;
Marzi A., Akhavan A., Simmons G., Gramberg T., Hofmann H., Bates P.,
Lingappa V.R., Poehlmann S.;
"The signal peptide of the ebolavirus glycoprotein influences
interaction with the cellular lectins DC-SIGN and DC-SIGNR.";
J. Virol. 80:6305-6317(2006).
[33]
RECEPTOR-BINDING REGION.
PubMed=16595665; DOI=10.1074/jbc.M601796200;
Kuhn J.H., Radoshitzky S.R., Guth A.C., Warfield K.L., Li W.,
Vincent M.J., Towner J.S., Nichol S.T., Bavari S., Choe H., Aman M.J.,
Farzan M.;
"Conserved receptor-binding domains of Lake Victoria marburgvirus and
Zaire ebolavirus bind a common receptor.";
J. Biol. Chem. 281:15951-15958(2006).
[34]
FUNCTION.
PubMed=20862315; DOI=10.1371/journal.ppat.1001110;
Saeed M.F., Kolokoltsov A.A., Albrecht T., Davey R.A.;
"Cellular entry of ebola virus involves uptake by a macropinocytosis-
like mechanism and subsequent trafficking through early and late
endosomes.";
PLoS Pathog. 6:0-0(2010).
[35]
FUNCTION.
PubMed=20202662; DOI=10.1016/j.virol.2010.02.015;
Bhattacharyya S., Warfield K.L., Ruthel G., Bavari S., Aman M.J.,
Hope T.J.;
"Ebola virus uses clathrin-mediated endocytosis as an entry pathway.";
Virology 401:18-28(2010).
[36]
INTERACTION WITH HOST NPC1, AND FUNCTION.
PubMed=21866103; DOI=10.1038/nature10348;
Carette J.E., Raaben M., Wong A.C., Herbert A.S., Obernosterer G.,
Mulherkar N., Kuehne A.I., Kranzusch P.J., Griffin A.M., Ruthel G.,
Dal Cin P., Dye J.M., Whelan S.P., Chandran K., Brummelkamp T.R.;
"Ebola virus entry requires the cholesterol transporter Niemann-Pick
C1.";
Nature 477:340-343(2011).
[37]
FUNCTION, AND PROTEOLYTIC CLEAVAGE OF GP1.
PubMed=22031933; DOI=10.1128/JVI.05708-11;
Brecher M., Schornberg K.L., Delos S.E., Fusco M.L., Saphire E.O.,
White J.M.;
"Cathepsin cleavage potentiates the Ebola virus glycoprotein to
undergo a subsequent fusion-relevant conformational change.";
J. Virol. 86:364-372(2012).
[38]
FUNCTION (SHED GP), SUBCELLULAR LOCATION (SHED GP), AND GLYCOSYLATION
(SHED GP).
PubMed=25412102; DOI=10.1371/journal.ppat.1004509;
Escudero-Perez B., Volchkova V.A., Dolnik O., Lawrence P.,
Volchkov V.E.;
"Shed GP of Ebola virus triggers immune activation and increased
vascular permeability.";
PLoS Pathog. 10:E1004509-E1004509(2014).
[39]
FUNCTION (ENVELOPE GLYCOPROTEIN).
PubMed=26516900; DOI=10.3390/v7102888;
Vande Burgt N.H., Kaletsky R.L., Bates P.;
"Requirements within the Ebola viral glycoprotein for tetherin
antagonism.";
Viruses 7:5587-5602(2015).
[40]
FUNCTION (SHED GP), AND MUTAGENESIS OF LEU-635 AND ASP-637.
PubMed=26092855; DOI=10.1093/infdis/jiv268;
Dolnik O., Volchkova V.A., Escudero-Perez B., Lawrence P., Klenk H.D.,
Volchkov V.E.;
"Shedding of Ebola Virus Surface Glycoprotein Is a Mechanism of Self-
regulation of Cellular Cytotoxicity and Has a Direct Effect on Virus
Infectivity.";
J. Infect. Dis. 212:S322-S328(2015).
[41]
FUNCTION (ENVELOPE GLYCOPROTEIN), INTERACTION WITH HOST BST2 (ENVELOPE
GLYCOPROTEIN), AND MUTAGENESIS OF PHE-88; LEU-111 AND LEU-122.
PubMed=27707924; DOI=10.1128/JVI.01563-16;
Brinkmann C., Nehlmeier I., Walendy-Gnirss K., Nehls J.,
Gonzalez Hernandez M., Hoffmann M., Qiu X., Takada A., Schindler M.,
Poehlmann S.;
"The Tetherin Antagonism of the Ebola Virus Glycoprotein Requires an
Intact Receptor-Binding Domain and Can Be Blocked by GP1-Specific
Antibodies.";
J. Virol. 90:11075-11086(2016).
[42]
INTERACTION WITH HOST FCN1 (ENVELOPE GLYCOPROTEIN).
PubMed=26984723; DOI=10.1128/JVI.00232-16;
Favier A.L., Gout E., Reynard O., Ferraris O., Kleman J.P.,
Volchkov V., Peyrefitte C., Thielens N.M.;
"Enhancement of Ebola Virus Infection via Ficolin-1 Interaction with
the Mucin Domain of GP Glycoprotein.";
J. Virol. 90:5256-5269(2016).
[43]
FUNCTION (ENVELOPE GLYCOPROTEIN), AND INTERACTION WITH HOST TLR4
(ENVELOPE GLYCOPROTEIN).
PubMed=28542576; DOI=10.1371/journal.ppat.1006397;
Iampietro M., Younan P., Nishida A., Dutta M., Lubaki N.M.,
Santos R.I., Koup R.A., Katze M.G., Bukreyev A.;
"Ebola virus glycoprotein directly triggers T lymphocyte death despite
of the lack of infection.";
PLoS Pathog. 13:E1006397-E1006397(2017).
[44]
FUNCTION (ENVELOPE GLYCOPROTEIN).
PubMed=28878074; DOI=10.1128/JVI.01308-17;
Rizk M.G., Basler C.F., Guatelli J.;
"Cooperation of the Ebola Virus Proteins VP40 and GP1,2 with BST2 To
Activate NF-kappaB Independently of Virus-Like Particle Trapping.";
J. Virol. 91:0-0(2017).
[45]
FUNCTION (ENVELOPE GLYCOPROTEIN), MOTIF, AND MUTAGENESIS OF GLY-660
AND ALA-664.
PubMed=29669839; DOI=10.1128/JVI.00403-18;
Gonzalez-Hernandez M., Hoffmann M., Brinkmann C., Nehls J.,
Winkler M., Schindler M., Poehlmann S.;
"A GXXXA Motif in the Transmembrane Domain of the Ebola Virus
Glycoprotein Is Required for Tetherin Antagonism.";
J. Virol. 92:0-0(2018).
[46]
FUNCTION (ENVELOPE GLYCOPROTEIN).
PubMed=30013549; DOI=10.3389/fimmu.2018.01428;
Edri A., Shemesh A., Iraqi M., Matalon O., Brusilovsky M., Hadad U.,
Radinsky O., Gershoni-Yahalom O., Dye J.M., Mandelboim O.,
Barda-Saad M., Lobel L., Porgador A.;
"The Ebola-Glycoprotein Modulates the Function of Natural Killer
Cells.";
Front. Immunol. 9:1428-1428(2018).
[47]
FUNCTION (SHED GP), AND SUBCELLULAR LOCATION (SHED GP).
PubMed=30085081; DOI=10.1093/infdis/jiy406;
Iampietro M., Santos R.I., Lubaki N.M., Bukreyev A.;
"Ebola Virus Shed Glycoprotein Triggers Differentiation, Infection,
and Death of Monocytes Through Toll-Like Receptor 4 Activation.";
J. Infect. Dis. 0:0-0(2018).
[48]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 557-630.
PubMed=10077567; DOI=10.1073/pnas.96.6.2662;
Malashkevich V.N., Schneider B.J., McNally M.L., Milhollen M.A.,
Pang J.X., Kim P.S.;
"Core structure of the envelope glycoprotein GP2 from Ebola virus at
1.9-A resolution.";
Proc. Natl. Acad. Sci. U.S.A. 96:2662-2667(1999).
-!- FUNCTION: Envelope glycoprotein: Trimeric GP1,2 complexes form the
virion surface spikes and mediate the viral entry processes, with
GP1 acting as the receptor-binding subunit and GP2 as the membrane
fusion subunit. At later times of infection, downregulates the
expression of various host cell surface molecules that are
essential for immune surveillance and cell adhesion. Down-
modulates several integrins including ITGA1, ITGA2, ITGA3, ITGA4,
ITGA5, ITGA6, ITGAV and ITGB1. This decrease in cell adhesion
molecules may lead to cell detachment, contributing to the
disruption of blood vessel integrity and hemorrhages developed
during infection (cytotoxicity). Interacts with host TLR4 and
thereby stimulates the differentiation and activation of monocytes
leading to bystander death of T-lymphocytes (PubMed:28542576).
Downregulates as well the function of host natural killer cells
(PubMed:30013549). Counteracts the antiviral effect of host
BST2/tetherin that restricts release of progeny virions from
infected cells. However, cooperates with VP40 and host BST2 to
activate canonical NF-kappa-B pathway in a manner dependent on
neddylation. {ECO:0000269|PubMed:26516900,
ECO:0000269|PubMed:27707924, ECO:0000269|PubMed:28542576,
ECO:0000269|PubMed:28878074, ECO:0000269|PubMed:29669839,
ECO:0000269|PubMed:30013549}.
-!- FUNCTION: Shed GP: Functions as a decoy for anti-GP1,2 antibodies
therby contributing to viral immune evasion. Interacts and
activates host macrophages and dendritic cells inducing up-
regulation of cytokine transcription. This effect is mediated
throught activation of host TLR4. {ECO:0000269|PubMed:25412102,
ECO:0000269|PubMed:26092855, ECO:0000269|PubMed:30085081}.
-!- FUNCTION: GP1: responsible for binding to the receptor(s) on
target cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR
which act as cofactors for virus entry into dendritic cells (DCs)
and endothelial cells. Binding to the macrophage specific lectin
CLEC10A also seem to enhance virus infectivity. Interaction with
FOLR1/folate receptor alpha may be a cofactor for virus entry in
some cell types, although results are contradictory. Members of
the Tyro3 receptor tyrosine kinase family also seem to be cell
entry factors in filovirus infection. Once attached, the virions
are internalized through clathrin-dependent endocytosis and/or
macropinocytosis. After internalization of the virus into the
endosomes of the host cell, proteolysis of GP1 by two cysteine
proteases, CTSB/cathepsin B and CTSL/cathepsin L presumably
induces a conformational change of GP2, allowing its binding to
the host entry receptor NPC1 and unmasking its fusion peptide to
initiate membranes fusion (PubMed:22031933, PubMed:26516900).
{ECO:0000269|PubMed:21866103, ECO:0000269|PubMed:22031933}.
-!- FUNCTION: GP2: acts as a class I viral fusion protein. Under the
current model, the protein has at least 3 conformational states:
pre-fusion native state, pre-hairpin intermediate state, and post-
fusion hairpin state. During viral and target cell membrane
fusion, the coiled coil regions (heptad repeats) assume a trimer-
of-hairpins structure, positioning the fusion peptide in close
proximity to the C-terminal region of the ectodomain. The
formation of this structure appears to drive apposition and
subsequent fusion of viral and target cell membranes. Responsible
for penetration of the virus into the cell cytoplasm by mediating
the fusion of the membrane of the endocytosed virus particle with
the endosomal membrane. Low pH in endosomes induces an
irreversible conformational change in GP2, releasing the fusion
hydrophobic peptide.
-!- SUBUNIT: Envelope glycoprotein: homotrimer; each monomer consists
of a GP1 and a GP2 subunit linked by disulfide bonds. The
resulting peplomers (GP1,2) protrude from the virus surface as
spikes. Interacts with host integrin alpha-V/ITGAV and CLEC10A.
Binds also to host CD209 and CLEC4M/DC-SIGN(R), as well as host
FOLR1. Interacts with host entry receptor NPC1. Interacts with
BST2; this interaction inhibits the antiviral effect of BST2 and
this allows viral release from infected cells. Interacts with host
FCN1; this interaction enhances viral entry (PubMed:26984723).
Interacts with host TLR4; this interaction induces T-lymphocyte
death (PubMed:28542576). Shed GP: GP1 and GP2delta are part of
GP1,2delta soluble complexes released by ectodomain shedding.
{ECO:0000269|PubMed:11461707, ECO:0000269|PubMed:12050398,
ECO:0000269|PubMed:12504546, ECO:0000269|PubMed:14990712,
ECO:0000269|PubMed:15596847, ECO:0000269|PubMed:21866103,
ECO:0000269|PubMed:26984723, ECO:0000269|PubMed:28542576}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-16200230, EBI-16200230;
-!- SUBCELLULAR LOCATION: GP2: Virion membrane
{ECO:0000305|PubMed:11877482}; Single-pass type I membrane protein
{ECO:0000255}. Host cell membrane {ECO:0000305|PubMed:11877482};
Single-pass type I membrane protein {ECO:0000255}. Note=In the
cell, localizes to the plasma membrane lipid rafts, which probably
represent the assembly and budding site.
{ECO:0000305|PubMed:11877482}.
-!- SUBCELLULAR LOCATION: GP1: Virion membrane
{ECO:0000305|PubMed:11877482}; Peripheral membrane protein. Host
cell membrane {ECO:0000305|PubMed:11877482}; Peripheral membrane
protein {ECO:0000269|PubMed:9576958}. Note=GP1 is not anchored to
the viral envelope, but forms a disulfid-linked complex with the
extravirion surface GP2 (PubMed:9576958). In the cell, both GP1
and GP2 localize to the plasma membrane lipid rafts, which
probably represent the assembly and budding site
(PubMed:11877482). GP1 can also be shed after proteolytic
processing. {ECO:0000269|PubMed:11877482,
ECO:0000269|PubMed:9576958}.
-!- SUBCELLULAR LOCATION: Shed GP: Secreted
{ECO:0000269|PubMed:15103332, ECO:0000269|PubMed:25412102,
ECO:0000269|PubMed:30085081}. Note=GP2-delta bound to GP1 (GP1,2-
delta) is produced by proteolytic cleavage of GP1,2 by host ADAM17
and shed by the virus. {ECO:0000269|PubMed:15103332}.
-!- DOMAIN: The mucin-like region seems to be involved in the
cytotoxic function. This region is also involved in binding to
human CLEC10A.
-!- DOMAIN: The coiled coil regions play a role in oligomerization and
fusion activity.
-!- PTM: The signal peptide region modulates GP's high mannose
glycosylation, thereby determining the efficiency of the
interactions with DC-SIGN(R). {ECO:0000269|PubMed:12438572}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:12438572}.
-!- PTM: Shed GP: Glycosylated; glycosylation is essential for the
activation of dendritic cells and macrophages.
{ECO:0000269|PubMed:25412102}.
-!- PTM: O-glycosylated in the mucin-like region.
{ECO:0000269|PubMed:12438572}.
-!- PTM: Palmitoylation of GP2 is not required for its function.
{ECO:0000269|PubMed:11152533}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
The precursor is processed into GP1 and GP2 by host cell furin in
the trans Golgi, and maybe by other host proteases, to yield the
mature GP1 and GP2 proteins (PubMed:9576958, PubMed:9614872)
(PubMed:9882347). The cleavage site corresponds to the furin
optimal cleavage sequence [KR]-X-[KR]-R (PubMed:9576958). This
cleavage does not seem to be required for function
(PubMed:9576958). After the internalization of the virus into cell
endosomes, GP1 C-terminus is removed by the endosomal proteases
cathepsin B, cathepsin L, or both, leaving a 19-kDa N-terminal
fragment which is further digested by cathepsin B
(PubMed:16571833). This cleaved 19-kDa GP1 can then bind to the
host entry receptor NPC1 (PubMed:21866103). Proteolytic processing
of GP1,2 by host ADAM17 can remove the transmembrane anchor of GP2
and leads to shedding of complexes consisting in GP1 and truncated
GP2 (GP1,2delta) (PubMed:15103332). {ECO:0000269|PubMed:11152533,
ECO:0000269|PubMed:15103332, ECO:0000269|PubMed:16571833,
ECO:0000269|PubMed:21866103, ECO:0000269|PubMed:9576958,
ECO:0000269|PubMed:9614872, ECO:0000269|PubMed:9882347}.
-!- RNA EDITING: Modified_positions=295 {ECO:0000269|PubMed:8553543,
ECO:0000269|PubMed:8622982}; Note=Partially edited. RNA editing at
this position consists of an insertion of one or two adenine
nucleotides. The sequence displayed here is the full-length
transmembrane glycoprotein GP, derived from the +1A edited RNA.
The unedited RNA gives rise to the small secreted glycoprotein sGP
(AC P60170), the +2A edited RNA gives rise to the super small
secreted glycoprotein ssGP (AC Q9YMG2).;
-!- MISCELLANEOUS: Filoviruses entry requires functional lipid rafts
at the host cell surface.
-!- MISCELLANEOUS: Essential for infectivity, as it is the sole viral
protein expressed at the virion surface.
-!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA96744.1; Type=Frameshift; Positions=296; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; L11365; AAB81004.1; -; Genomic_RNA.
EMBL; U31033; AAA96744.1; ALT_FRAME; Genomic_RNA.
EMBL; U23187; AAC54887.1; -; Genomic_RNA.
EMBL; AF272001; AAG40168.1; -; Genomic_RNA.
EMBL; AY142960; AAN37507.1; -; Genomic_RNA.
EMBL; AF086833; AAD14585.1; -; Genomic_RNA.
EMBL; AF499101; AAM76034.1; -; Genomic_RNA.
PIR; S23155; S23155.
RefSeq; NP_066246.1; NC_002549.1.
PDB; 2EBO; X-ray; 1.90 A; A/B/C=557-630.
PDB; 2RLJ; NMR; -; A=524-539.
PDB; 3CSY; X-ray; 3.40 A; I/K/M/O=32-311, J/L/N/P=464-501.
PDB; 5FHC; X-ray; 6.70 A; J=502-599, K=1-308, K=490-501.
PDB; 5HJ3; X-ray; 3.30 A; C/G/K/O=32-194.
PDB; 5JQ3; X-ray; 2.23 A; A=32-501, B=502-632.
PDB; 5JQ7; X-ray; 2.69 A; A=32-501, B=502-632.
PDB; 5JQB; X-ray; 2.68 A; A=32-501, B=502-632.
PDB; 5KEL; EM; 4.30 A; A/E/F=33-501, B/G/I=502-637.
PDB; 5KEM; EM; 5.50 A; A/F=53-284.
PDB; 5KEN; EM; 4.30 A; A/E/K=33-308, B/F/M=503-615.
PDB; 6EAY; X-ray; 3.72 A; A=502-637, B=32-336.
PDB; 6F5U; X-ray; 2.07 A; A=32-312, B=502-632.
PDB; 6F6I; X-ray; 2.40 A; A=32-336, B=502-632.
PDB; 6F6N; X-ray; 2.15 A; A=32-336.
PDB; 6F6S; X-ray; 2.29 A; A=32-336.
PDB; 6G95; X-ray; 2.31 A; A=32-311, B=502-632.
PDB; 6G9B; X-ray; 2.26 A; A=32-311, B=502-632.
PDB; 6G9I; X-ray; 2.19 A; A=32-311, B=502-632.
PDBsum; 2EBO; -.
PDBsum; 2RLJ; -.
PDBsum; 3CSY; -.
PDBsum; 5FHC; -.
PDBsum; 5HJ3; -.
PDBsum; 5JQ3; -.
PDBsum; 5JQ7; -.
PDBsum; 5JQB; -.
PDBsum; 5KEL; -.
PDBsum; 5KEM; -.
PDBsum; 5KEN; -.
PDBsum; 6EAY; -.
PDBsum; 6F5U; -.
PDBsum; 6F6I; -.
PDBsum; 6F6N; -.
PDBsum; 6F6S; -.
PDBsum; 6G95; -.
PDBsum; 6G9B; -.
PDBsum; 6G9I; -.
ProteinModelPortal; Q05320; -.
SMR; Q05320; -.
DIP; DIP-62002N; -.
ELM; Q05320; -.
IntAct; Q05320; 1.
TCDB; 1.G.12.2.2; the avian leukosis virus gp95 fusion protein (alv-gp95) family.
PRIDE; Q05320; -.
GeneID; 911829; -.
KEGG; vg:911829; -.
OrthoDB; VOG09000092; -.
EvolutionaryTrace; Q05320; -.
Proteomes; UP000007209; Genome.
Proteomes; UP000109874; Genome.
Proteomes; UP000149419; Genome.
Proteomes; UP000150973; Genome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0030430; C:host cell cytoplasm; IDA:CACAO.
GO; GO:0044165; C:host cell endoplasmic reticulum; IMP:CACAO.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; IDA:CACAO.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039587; P:suppression by virus of host tetherin activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0046761; P:viral budding from plasma membrane; IDA:CACAO.
GO; GO:0046718; P:viral entry into host cell; IMP:CACAO.
InterPro; IPR014625; GPC_FiloV.
InterPro; IPR002561; GPC_filovir-type_extra_dom.
Pfam; PF01611; Filo_glycop; 1.
PIRSF; PIRSF036874; GPC_FiloV; 1.
1: Evidence at protein level;
3D-structure; Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Coiled coil; Complete proteome;
Disulfide bond; Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host membrane; Host-virus interaction;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host tetherin by virus; Lipoprotein; Membrane;
Palmitate; Reference proteome; RNA editing; Secreted; Signal;
Transmembrane; Transmembrane helix; Viral attachment to host cell;
Viral attachment to host entry receptor; Viral envelope protein;
Viral immunoevasion; Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
CHAIN 1 637 Shed GP.
/FTId=PRO_0000445686.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 676 Envelope glycoprotein.
/FTId=PRO_0000037485.
CHAIN 33 501 GP1.
/FTId=PRO_0000037486.
CHAIN 502 676 GP2.
/FTId=PRO_0000037487.
TOPO_DOM 33 650 Extracellular. {ECO:0000255}.
TRANSMEM 651 671 Helical. {ECO:0000255}.
TOPO_DOM 672 676 Cytoplasmic. {ECO:0000255}.
REGION 54 201 Receptor-binding. {ECO:0000255}.
REGION 305 485 Mucin-like region.
REGION 524 539 Fusion peptide. {ECO:0000305}.
COILED 554 595 {ECO:0000255}.
COILED 615 634 {ECO:0000255}.
MOTIF 660 664 Important role for host BST2/tetherin
antagonism.
{ECO:0000269|PubMed:27707924}.
SITE 57 57 Involved in receptor recognition and/or
post-binding events. {ECO:0000255}.
SITE 63 63 Involved in receptor recognition and/or
post-binding events. {ECO:0000255}.
SITE 64 64 Involved in receptor recognition and/or
post-binding events. {ECO:0000255}.
SITE 88 88 Involved in receptor recognition and/or
post-binding events. {ECO:0000255}.
SITE 95 95 Involved in receptor recognition and/or
post-binding events. {ECO:0000255}.
SITE 170 170 Involved in receptor recognition and/or
post-binding events. {ECO:0000255}.
SITE 501 502 Cleavage; by host furin.
{ECO:0000269|PubMed:9576958}.
SITE 637 638 Cleavage; by host ADAM17.
{ECO:0000269|PubMed:15103332}.
LIPID 670 670 S-palmitoyl cysteine; by host.
{ECO:0000269|PubMed:11152533}.
LIPID 672 672 S-palmitoyl cysteine; by host.
{ECO:0000269|PubMed:11152533}.
CARBOHYD 40 40 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 228 228 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 238 238 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 257 257 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 268 268 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 317 317 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 346 346 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 386 386 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 436 436 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 454 454 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 462 462 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 563 563 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 618 618 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 53 609 Interchain (between GP1 and GP2 chains).
{ECO:0000269|PubMed:12438572}.
DISULFID 108 135 {ECO:0000255}.
DISULFID 121 147 {ECO:0000255}.
DISULFID 511 556 {ECO:0000255}.
DISULFID 601 608 {ECO:0000269|PubMed:12438572}.
VARIANT 65 65 S -> P (in strain: Isolate mouse-
adapted).
VARIANT 246 246 S -> P (in strain: Isolate mouse-
adapted).
VARIANT 544 544 I -> T.
MUTAGEN 40 40 N->D: Induces GP1 secretion. Complete
loss of virus capability to enter into
host cell. {ECO:0000269|PubMed:12438572}.
MUTAGEN 53 53 C->G: Induces GP1 secretion. Complete
loss of virus capability to enter into
host cell. {ECO:0000269|PubMed:12438572}.
MUTAGEN 55 55 D->A: 80% loss of virus capability to
enter into host cell.
MUTAGEN 55 55 D->E,K: No effect on viral entry.
MUTAGEN 57 57 L->A: Complete loss of virus capability
to enter into host cell.
MUTAGEN 57 57 L->F,I,K: 90% loss of virus capability to
enter into host cell.
MUTAGEN 63 63 L->A: 90% loss of virus capability to
enter into host cell.
MUTAGEN 63 63 L->F: Almost complete loss of virus
capability to enter into host cell.
MUTAGEN 63 63 L->K: Complete loss of virus capability
to enter into host cell.
MUTAGEN 64 64 R->A,E: Complete loss of virus capability
to enter into host cell.
MUTAGEN 64 64 R->K: No loss of virus capability to
enter into host cell.
MUTAGEN 88 88 F->A,E: Complete loss of virus capability
to enter into host cell.
MUTAGEN 88 88 F->A: About 50% loss of ability to
counteract host BST2.
{ECO:0000269|PubMed:27707924}.
MUTAGEN 88 88 F->I: No loss of virus capability to
enter into host cell.
MUTAGEN 95 95 K->A,E: 80% loss of virus capability to
enter into host cell.
MUTAGEN 95 95 K->R: 20% loss of virus capability to
enter into host cell.
MUTAGEN 108 108 C->G: Almost complete loss of expression
of GP1 and GP2. Almost complete loss of
virus capability to enter into host cell.
{ECO:0000269|PubMed:12438572}.
MUTAGEN 111 111 L->A: About 60% loss of ability to
counteract host BST2.
{ECO:0000269|PubMed:27707924}.
MUTAGEN 121 121 C->G: Reduced levels of expression of GP1
and GP2. 50% loss of virus capability to
enter into host cell.
{ECO:0000269|PubMed:12438572}.
MUTAGEN 122 122 L->A: About 60% loss of ability to
counteract host BST2.
{ECO:0000269|PubMed:27707924}.
MUTAGEN 135 135 C->S: Almost complete loss of expression
of GP1 and GP2. Complete loss of virus
capability to enter into host cell.
{ECO:0000269|PubMed:12438572}.
MUTAGEN 147 147 C->S: Reduced levels of expression of GP1
and GP2. Almost complete loss of virus
capability to enter into host cell.
{ECO:0000269|PubMed:12438572}.
MUTAGEN 170 170 I->A: 90% loss of virus capability to
enter into host cell.
MUTAGEN 170 170 I->E: Complete loss of virus capability
to enter into host cell.
MUTAGEN 170 170 I->F: 50% loss of virus capability to
enter into host cell.
MUTAGEN 204 204 N->D: No effect on GP1 and GP2
expression. No loss of virus capability
to enter into host cell.
{ECO:0000269|PubMed:12438572}.
MUTAGEN 238 238 N->Y: No effect on GP1 and GP2
expression. 12% loss of virus capability
to enter into host cell.
{ECO:0000269|PubMed:12438572}.
MUTAGEN 257 257 N->D: No effect on GP1 and GP2
expression. 12% loss of virus capability
to enter into host cell.
{ECO:0000269|PubMed:12438572}.
MUTAGEN 296 296 N->D: No effect on GP1 and GP2
expression. 18% loss of virus capability
to enter into host cell.
{ECO:0000269|PubMed:12438572}.
MUTAGEN 497 501 RRTRR->AGTAA: Almost complete loss of
cleavage between GP1 and GP2. No loss of
infectivity.
{ECO:0000269|PubMed:11152533}.
MUTAGEN 498 501 RTRR->ATAA: No effect on cleavage between
GP1 and GP2.
{ECO:0000269|PubMed:9882347}.
MUTAGEN 511 511 C->G: Induces GP1 secretion. Complete
loss of virus capability to enter into
host cell. {ECO:0000269|PubMed:12438572}.
MUTAGEN 528 528 G->R: Reduced infectivity.
{ECO:0000269|PubMed:10482652}.
MUTAGEN 529 529 L->A,R: Reduced infectivity.
{ECO:0000269|PubMed:10482652}.
MUTAGEN 532 532 I->A: Reduced infectivity.
{ECO:0000269|PubMed:10482652}.
MUTAGEN 532 532 I->R: Almost complete loss of
infectivity. No effect on transport of GP
to the cell surface and incorporation
onto virions.
{ECO:0000269|PubMed:10482652}.
MUTAGEN 535 535 F->A: Reduced infectivity.
{ECO:0000269|PubMed:10482652}.
MUTAGEN 535 535 F->R: Almost complete loss of
infectivity. No effect on transport of GP
to the cell surface and incorporation
onto virions.
{ECO:0000269|PubMed:10482652}.
MUTAGEN 536 536 G->A: Almost complete loss of
infectivity. No effect on transport of GP
to the cell surface and incorporation
onto virions.
{ECO:0000269|PubMed:10482652}.
MUTAGEN 537 537 P->R: Almost complete loss of
infectivity. No effect on transport of GP
to the cell surface and incorporation
onto virions.
{ECO:0000269|PubMed:10482652}.
MUTAGEN 556 556 C->S: Induces GP1 secretion. Complete
loss of virus capability to enter into
host cell. {ECO:0000269|PubMed:12438572}.
MUTAGEN 563 563 N->D: Reduced levels of expression of GP,
GP1 and GP2. 20% loss of virus capability
to enter into host cell.
{ECO:0000269|PubMed:12438572}.
MUTAGEN 601 601 C->S: Induces GP1 secretion. Complete
loss of virus capability to enter into
host cell. {ECO:0000269|PubMed:12438572}.
MUTAGEN 608 608 C->G: Induces GP1 secretion. Complete
loss of virus capability to enter into
host cell. {ECO:0000269|PubMed:12438572}.
MUTAGEN 609 609 C->G: Induces GP1 secretion. Complete
loss of virus capability to enter into
host cell. {ECO:0000269|PubMed:12438572}.
MUTAGEN 618 618 N->D: Slightly reduced levels of
expression of GP1 and GP2. No loss of
virus capability to enter into host cell.
{ECO:0000269|PubMed:12438572}.
MUTAGEN 632 632 D->V: No effect on release of soluble
GP1,2delta.
{ECO:0000269|PubMed:15103332}.
MUTAGEN 633 633 K->R,V: No effect on release of soluble
GP1,2delta.
{ECO:0000269|PubMed:15103332}.
MUTAGEN 634 634 T->I: 50% loss of release of soluble
GP1,2delta.
{ECO:0000269|PubMed:15103332}.
MUTAGEN 635 635 L->V: 60% loss of release of soluble
GP1,2delta.
{ECO:0000269|PubMed:15103332}.
MUTAGEN 635 635 L->V: Increased GP shedding.
{ECO:0000269|PubMed:26092855}.
MUTAGEN 636 636 P->A: 60% loss of release of soluble
GP1,2delta.
MUTAGEN 637 637 D->E: No effect on release of soluble
GP1,2delta.
{ECO:0000269|PubMed:15103332}.
MUTAGEN 637 637 D->L,V: Increased release of soluble
GP1,2delta.
{ECO:0000269|PubMed:15103332}.
MUTAGEN 637 637 D->V: Decreased GP shedding.
{ECO:0000269|PubMed:26092855}.
MUTAGEN 638 638 Q->V: No effect on release of soluble
GP1,2delta.
{ECO:0000269|PubMed:15103332}.
MUTAGEN 639 639 G->V: 40% loss of release of soluble
GP1,2delta.
{ECO:0000269|PubMed:15103332}.
MUTAGEN 640 640 D->V: No effect on release of soluble
GP1,2delta.
{ECO:0000269|PubMed:15103332}.
MUTAGEN 641 641 N->A: No effect on release of soluble
GP1,2delta.
{ECO:0000269|PubMed:15103332}.
MUTAGEN 642 642 D->V: No effect on release of soluble
GP1,2delta.
{ECO:0000269|PubMed:15103332}.
MUTAGEN 643 643 N->A: No effect on release of soluble
GP1,2delta.
{ECO:0000269|PubMed:15103332}.
MUTAGEN 660 660 G->L: About 60% loss of viral release;
when associated with L-664.
{ECO:0000269|PubMed:29669839}.
MUTAGEN 664 664 A->L: About 60% loss of viral release;
when associated with L-660.
{ECO:0000269|PubMed:29669839}.
MUTAGEN 670 670 C->A: Reduced palmitoylation. No effect
on GP processing and association with
retrovirus particle. No loss of virus
capability to enter into host cell. Loss
of localization to the rafts; when
associated with A-670.
{ECO:0000269|PubMed:11152533,
ECO:0000269|PubMed:11877482,
ECO:0000269|PubMed:12438572}.
MUTAGEN 670 670 C->F: Slightly reduced levels of
expression of GP1 and GP2. Greatly
reduced GP processing and association
with retrovirus particle. 43% loss of
virus capability to enter into host cell.
Loss of localization to the rafts; when
associated with A-672.
{ECO:0000269|PubMed:11152533,
ECO:0000269|PubMed:11877482,
ECO:0000269|PubMed:12438572}.
MUTAGEN 672 672 C->A: Reduced palmitoylation. No effect
on GP processing and association with
retrovirus particle. No loss of virus
capability to enter into host cell.
{ECO:0000269|PubMed:11152533,
ECO:0000269|PubMed:12438572}.
MUTAGEN 672 672 C->F: Slightly reduced levels of
expression of GP1 and GP2. Almost no
effect on GP processing and association
with retrovirus particle. 24% loss of
virus capability to enter into host cell.
{ECO:0000269|PubMed:11152533,
ECO:0000269|PubMed:12438572}.
STRAND 36 39 {ECO:0000244|PDB:6F5U}.
STRAND 42 45 {ECO:0000244|PDB:6F5U}.
STRAND 48 50 {ECO:0000244|PDB:6F5U}.
HELIX 60 62 {ECO:0000244|PDB:6F5U}.
STRAND 63 69 {ECO:0000244|PDB:6F5U}.
HELIX 70 73 {ECO:0000244|PDB:6F5U}.
HELIX 79 83 {ECO:0000244|PDB:6F5U}.
STRAND 86 91 {ECO:0000244|PDB:6F5U}.
STRAND 96 98 {ECO:0000244|PDB:6F5U}.
STRAND 100 103 {ECO:0000244|PDB:6F5U}.
STRAND 105 114 {ECO:0000244|PDB:6F5U}.
STRAND 116 118 {ECO:0000244|PDB:3CSY}.
STRAND 120 122 {ECO:0000244|PDB:6F5U}.
STRAND 135 144 {ECO:0000244|PDB:6F5U}.
STRAND 149 154 {ECO:0000244|PDB:6F5U}.
STRAND 159 161 {ECO:0000244|PDB:6F5U}.
STRAND 163 169 {ECO:0000244|PDB:6F5U}.
STRAND 176 185 {ECO:0000244|PDB:6F5U}.
STRAND 216 224 {ECO:0000244|PDB:6F5U}.
STRAND 227 229 {ECO:0000244|PDB:6F5U}.
STRAND 231 243 {ECO:0000244|PDB:6F5U}.
HELIX 250 262 {ECO:0000244|PDB:6F5U}.
STRAND 269 271 {ECO:0000244|PDB:6F5U}.
STRAND 273 275 {ECO:0000244|PDB:6F5U}.
TURN 290 292 {ECO:0000244|PDB:6G9I}.
STRAND 307 310 {ECO:0000244|PDB:6F5U}.
STRAND 515 519 {ECO:0000244|PDB:6F5U}.
TURN 528 531 {ECO:0000244|PDB:6F5U}.
TURN 533 535 {ECO:0000244|PDB:6F5U}.
HELIX 539 541 {ECO:0000244|PDB:6F5U}.
STRAND 544 548 {ECO:0000244|PDB:6F5U}.
HELIX 551 553 {ECO:0000244|PDB:6F5U}.
HELIX 560 594 {ECO:0000244|PDB:2EBO}.
HELIX 595 597 {ECO:0000244|PDB:2EBO}.
HELIX 600 604 {ECO:0000244|PDB:2EBO}.
HELIX 605 609 {ECO:0000244|PDB:2EBO}.
HELIX 616 628 {ECO:0000244|PDB:2EBO}.
SEQUENCE 676 AA; 74464 MW; BE8AB3B339F63261 CRC64;
MGVTGILQLP RDRFKRTSFF LWVIILFQRT FSIPLGVIHN STLQVSDVDK LVCRDKLSST
NQLRSVGLNL EGNGVATDVP SATKRWGFRS GVPPKVVNYE AGEWAENCYN LEIKKPDGSE
CLPAAPDGIR GFPRCRYVHK VSGTGPCAGD FAFHKEGAFF LYDRLASTVI YRGTTFAEGV
VAFLILPQAK KDFFSSHPLR EPVNATEDPS SGYYSTTIRY QATGFGTNET EYLFEVDNLT
YVQLESRFTP QFLLQLNETI YTSGKRSNTT GKLIWKVNPE IDTTIGEWAF WETKKNLTRK
IRSEELSFTV VSNGAKNISG QSPARTSSDP GTNTTTEDHK IMASENSSAM VQVHSQGREA
AVSHLTTLAT ISTSPQSLTT KPGPDNSTHN TPVYKLDISE ATQVEQHHRR TDNDSTASDT
PSATTAAGPP KAENTNTSKS TDFLDPATTT SPQNHSETAG NNNTHHQDTG EESASSGKLG
LITNTIAGVA GLITGGRRTR REAIVNAQPK CNPNLHYWTT QDEGAAIGLA WIPYFGPAAE
GIYIEGLMHN QDGLICGLRQ LANETTQALQ LFLRATTELR TFSILNRKAI DFLLQRWGGT
CHILGPDCCI EPHDWTKNIT DKIDQIIHDF VDKTLPDQGD NDNWWTGWRQ WIPAGIGVTG
VIIAVIALFC ICKFVF


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