VGP_EBOZM
ID VGP_EBOZM Reviewed; 676 AA.
AC Q05320; Q66818; Q77LU5; Q8B9S1; Q8JS62;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Envelope glycoprotein;
DE AltName: Full=GP1,2;
DE Short=GP;
DE Contains:
DE RecName: Full=Shed GP;
DE AltName: Full=GP1,2-delta;
DE Contains:
DE RecName: Full=GP1;
DE Contains:
DE RecName: Full=GP2;
DE Flags: Precursor;
GN Name=GP;
OS Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=128952;
OH NCBI_TaxID=77231; Epomops franqueti (Franquet's epauleted fruit bat).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8237108; DOI=10.1016/0168-1702(93)90063-s;
RA Sanchez A., Kiley M.P., Holloway B.P., Auperin D.D.;
RT "Sequence analysis of the Ebola virus genome: organization, genetic
RT elements, and comparison with the genome of Marburg virus.";
RL Virus Res. 29:215-240(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA / MRNA], AND RNA EDITING.
RX PubMed=8553543; DOI=10.1006/viro.1995.0052;
RA Volchkov V.E., Becker S., Volchkova V.A., Ternovoj V.A., Kotov A.N.,
RA Netesov S.V., Klenk H.-D.;
RT "GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by T7
RT and vaccinia virus polymerases.";
RL Virology 214:421-430(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RNA EDITING.
RX PubMed=8622982; DOI=10.1073/pnas.93.8.3602;
RA Sanchez A., Trappier S.G., Mahy B.W.J., Peters C.J., Nichol S.T.;
RT "The virion glycoproteins of Ebola viruses are encoded in two reading
RT frames and are expressed through transcriptional editing.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:3602-3607(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate guinea pig-adapted;
RX PubMed=11062045; DOI=10.1006/viro.2000.0572;
RA Volchkov V.E., Chepurnov A.A., Volchkova V.A., Ternovoj V.A., Klenk H.D.;
RT "Molecular characterization of guinea pig-adapted variants of Ebola
RT virus.";
RL Virology 277:147-155(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Volchkov V.E.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate mouse-adapted;
RA Wilson J.A., Kondig J.P., Kuehne A.I., Hart M.K.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 359-676.
RX PubMed=1299611; DOI=10.1016/0014-5793(92)80662-z;
RA Volchkov V.E., Blinov V.M., Netesov S.V.;
RT "The envelope glycoprotein of Ebola virus contains an immunosuppressive-
RT like domain similar to oncogenic retroviruses.";
RL FEBS Lett. 305:181-184(1992).
RN [8]
RP PROTEOLYTIC PROCESSING (ENVELOPE GLYCOPROTEIN), AND TOPOLOGY.
RX PubMed=9576958; DOI=10.1073/pnas.95.10.5762;
RA Volchkov V.E., Feldmann H., Volchkova V.A., Klenk H.-D.;
RT "Processing of the Ebola virus glycoprotein by the proprotein convertase
RT furin.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:5762-5767(1998).
RN [9]
RP PROTEOLYTIC PROCESSING (ENVELOPE GLYCOPROTEIN).
RX PubMed=9614872; DOI=10.1006/viro.1998.9143;
RA Volchkov V.E., Volchkova V.A., Slenczka W., Klenk H.-D., Feldmann H.;
RT "Release of viral glycoproteins during Ebola virus infection.";
RL Virology 245:110-119(1998).
RN [10]
RP DOMAIN.
RX PubMed=9499027; DOI=10.1128/jvi.72.3.1775-1781.1998;
RA Ruiz-Arguello M.B., Goni F.M., Pereira F.B., Nieva J.L.;
RT "Phosphatidylinositol-dependent membrane fusion induced by a putative
RT fusogenic sequence of Ebola virus.";
RL J. Virol. 72:1775-1781(1998).
RN [11]
RP DOMAIN, AND MUTAGENESIS OF GLY-528; LEU-529; ILE-532; PHE-535; GLY-536 AND
RP PRO-537.
RX PubMed=10482652; DOI=10.1128/jvi.73.10.8907-8912.1999;
RA Ito H., Watanabe S., Sanchez A., Whitt M.A., Kawaoka Y.;
RT "Mutational analysis of the putative fusion domain of Ebola virus
RT glycoprotein.";
RL J. Virol. 73:8907-8912(1999).
RN [12]
RP PROTEOLYTIC PROCESSING (ENVELOPE GLYCOPROTEIN), AND MUTAGENESIS OF
RP 498-ARG--ARG-501.
RX PubMed=9882347; DOI=10.1128/jvi.73.2.1419-1426.1999;
RA Wool-Lewis R.J., Bates P.;
RT "Endoproteolytic processing of the ebola virus envelope glycoprotein:
RT cleavage is not required for function.";
RL J. Virol. 73:1419-1426(1999).
RN [13]
RP FUNCTION, AND DOMAIN MUCIN/LIKE REGION.
RX PubMed=10932225; DOI=10.1038/78654;
RA Yang Z.-Y., Duckers H.J., Sullivan N.J., Sanchez A., Nabel E.G.,
RA Nabel G.J.;
RT "Identification of the Ebola virus glycoprotein as the main viral
RT determinant of vascular cell cytotoxicity and injury.";
RL Nat. Med. 6:886-889(2000).
RN [14]
RP FUNCTION (ENVELOPE GLYCOPROTEIN).
RX PubMed=11112476; DOI=10.1006/viro.2000.0601;
RA Takada A., Watanabe S., Ito H., Okazaki K., Kida H., Kawaoka Y.;
RT "Downregulation of beta1 integrins by Ebola virus glycoprotein: implication
RT for virus entry.";
RL Virology 278:20-26(2000).
RN [15]
RP PROTEOLYTIC PROCESSING (ENVELOPE GLYCOPROTEIN), PALMITOYLATION AT CYS-670
RP AND CYS-672, AND MUTAGENESIS OF 497-ARG--ARG-501; CYS-670 AND CYS-672.
RX PubMed=11152533; DOI=10.1128/jvi.75.3.1576-1580.2001;
RA Ito H., Watanabe S., Takada A., Kawaoka Y.;
RT "Ebola virus glycoprotein: proteolytic processing, acylation, cell tropism,
RT and detection of neutralizing antibodies.";
RL J. Virol. 75:1576-1580(2001).
RN [16]
RP COILED-COIL.
RX PubMed=11024148; DOI=10.1128/jvi.74.21.10194-10201.2000;
RA Watanabe S., Takada A., Watanabe T., Ito H., Kida H., Kawaoka Y.;
RT "Functional importance of the coiled-coil of the Ebola virus
RT glycoprotein.";
RL J. Virol. 74:10194-10201(2000).
RN [17]
RP INTERACTION WITH HUMAN FOLR1 (ENVELOPE GLYCOPROTEIN).
RX PubMed=11461707; DOI=10.1016/s0092-8674(01)00418-4;
RA Chan S.Y., Empig C.J., Welte F.J., Speck R.F., Schmaljohn A.,
RA Kreisberg J.F., Goldsmith M.A.;
RT "Folate receptor-alpha is a cofactor for cellular entry by Marburg and
RT Ebola viruses.";
RL Cell 106:117-126(2001).
RN [18]
RP DISULFIDE BONDS, GLYCOSYLATION, AND MUTAGENESIS OF ASN-40; CYS-53; CYS-108;
RP CYS-121; CYS-135; CYS-147; ASN-204; ASN-238; ASN-257; ASN-296; CYS-511;
RP CYS-556; ASN-563; CYS-601; CYS-608; CYS-609; ASN-618; CYS-670 AND CYS-672.
RX PubMed=12438572; DOI=10.1128/jvi.76.24.12463-12472.2002;
RA Jeffers S.A., Sanders D.A., Sanchez A.;
RT "Covalent modifications of the ebola virus glycoprotein.";
RL J. Virol. 76:12463-12472(2002).
RN [19]
RP FUNCTION (ENVELOPE GLYCOPROTEIN).
RX PubMed=11836430; DOI=10.1128/jvi.76.5.2518-2528.2002;
RA Simmons G., Wool-Lewis R.J., Baribaud F., Netter R.C., Bates P.;
RT "Ebola virus glycoproteins induce global surface protein down-modulation
RT and loss of cell adherence.";
RL J. Virol. 76:2518-2528(2002).
RN [20]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-670 AND CYS-672.
RX PubMed=11877482; DOI=10.1084/jem.20011500;
RA Bavari S., Bosio C.M., Wiegand E., Ruthel G., Will A.B., Geisbert T.W.,
RA Hevey M., Schmaljohn C., Schmaljohn A., Aman M.J.;
RT "Lipid raft microdomains: a gateway for compartmentalized trafficking of
RT Ebola and Marburg viruses.";
RL J. Exp. Med. 195:593-602(2002).
RN [21]
RP INTERACTION WITH HUMAN CD209 (ENVELOPE GLYCOPROTEIN), INTERACTION WITH HOST
RP CLEC4M (ENVELOPE GLYCOPROTEIN), AND ROLE IN TRANS INFECTION.
RX PubMed=12050398; DOI=10.1128/jvi.76.13.6841-6844.2002;
RA Alvarez C.P., Lasala F., Carrillo J., Muniz O., Corbi A.L., Delgado R.;
RT "C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in
RT cis and in trans.";
RL J. Virol. 76:6841-6844(2002).
RN [22]
RP PUTATIVE ROLE OF FOLR1 IN VIRUS ENTRY INTO THE CELL.
RX PubMed=14645601; DOI=10.1128/jvi.77.24.13433-13438.2003;
RA Simmons G., Rennekamp A.J., Chai N., Vandenberghe L.H., Riley J.L.,
RA Bates P.;
RT "Folate receptor alpha and caveolae are not required for Ebola virus
RT glycoprotein-mediated viral infection.";
RL J. Virol. 77:13433-13438(2003).
RN [23]
RP INTERACTION WITH HUMAN CD209 (ENVELOPE GLYCOPROTEIN), AND INTERACTION WITH
RP HOST CLEC4M (ENVELOPE GLYCOPROTEIN).
RX PubMed=12504546; DOI=10.1006/viro.2002.1730;
RA Simmons G., Reeves J.D., Grogan C.C., Vandenberghe L.H., Baribaud F.,
RA Whitbeck J.C., Burke E., Buchmeier M.J., Soilleux E.J., Riley J.L.,
RA Doms R.W., Bates P., Poehlmann S.;
RT "DC-SIGN and DC-SIGNR bind ebola glycoproteins and enhance infection of
RT macrophages and endothelial cells.";
RL Virology 305:115-123(2003).
RN [24]
RP CLEAVAGE BY HOST ADAM17, MUTAGENESIS OF ASP-632; LYS-633; THR-634; LEU-635;
RP ASP-637; GLN-638; GLY-639; ASP-640; ASN-641; ASP-642 AND ASN-643, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15103332; DOI=10.1038/sj.emboj.7600219;
RA Dolnik O., Volchkova V., Garten W., Carbonnelle C., Becker S., Kahnt J.,
RA Stroeher U., Klenk H.-D., Volchkov V.;
RT "Ectodomain shedding of the glycoprotein GP of Ebola virus.";
RL EMBO J. 23:2175-2184(2004).
RN [25]
RP INTERACTION WITH HUMAN CLEC10A (ENVELOPE GLYCOPROTEIN).
RX PubMed=14990712; DOI=10.1128/jvi.78.6.2943-2947.2004;
RA Takada A., Fujioka K., Tsuiji M., Morikawa A., Higashi N., Ebihara H.,
RA Kobasa D., Feldmann H., Irimura T., Kawaoka Y.;
RT "Human macrophage C-type lectin specific for galactose and N-
RT acetylgalactosamine promotes filovirus entry.";
RL J. Virol. 78:2943-2947(2004).
RN [26]
RP FUNCTION (GP1).
RX PubMed=16051836; DOI=10.1128/jvi.79.16.10442-10450.2005;
RA Wahl-Jensen V.M., Afanasieva T.A., Seebach J., Stroeher U., Feldmann H.,
RA Schnittler H.J.;
RT "Effects of Ebola virus glycoproteins on endothelial cell activation and
RT barrier function.";
RL J. Virol. 79:10442-10450(2005).
RN [27]
RP PROTEOLYSIS (GP1).
RX PubMed=15831716; DOI=10.1126/science.1110656;
RA Chandran K., Sullivan N.J., Felbor U., Whelan S.P., Cunningham J.M.;
RT "Endosomal proteolysis of the Ebola virus glycoprotein is necessary for
RT infection.";
RL Science 308:1643-1645(2005).
RN [28]
RP FUNCTION (GP1,2DELTA), AND SUBUNIT (GP1,2DELTA).
RX PubMed=15681442; DOI=10.1128/jvi.79.4.2413-2419.2005;
RA Wahl-Jensen V., Kurz S.K., Hazelton P.R., Schnittler H.J., Stroeher U.,
RA Burton D.R., Feldmann H.;
RT "Role of Ebola virus secreted glycoproteins and virus-like particles in
RT activation of human macrophages.";
RL J. Virol. 79:2413-2419(2005).
RN [29]
RP DOWN-MODULATION OF HOST INTEGRIN DIMER ALPHA-V/BETA-3, AND INTERACTION WITH
RP HUMAN INTEGRIN ITGAV (ENVELOPE GLYCOPROTEIN).
RX PubMed=15596847; DOI=10.1128/jvi.79.1.547-553.2005;
RA Sullivan N.J., Peterson M., Yang Z.-Y., Kong W.-P., Duckers H., Nabel E.,
RA Nabel G.J.;
RT "Ebola virus glycoprotein toxicity is mediated by a dynamin-dependent
RT protein-trafficking pathway.";
RL J. Virol. 79:547-553(2005).
RN [30]
RP PROTEOLYSIS (GP1).
RX PubMed=16571833; DOI=10.1128/jvi.80.8.4174-4178.2006;
RA Schornberg K., Matsuyama S., Kabsch K., Delos S., Bouton A., White J.;
RT "Role of endosomal cathepsins in entry mediated by the Ebola virus
RT glycoprotein.";
RL J. Virol. 80:4174-4178(2006).
RN [31]
RP FUNCTION.
RX PubMed=16603527; DOI=10.1099/vir.0.81361-0;
RA Alazard-Dany N., Volchkova V., Reynard O., Carbonnelle C., Dolnik O.,
RA Ottmann M., Khromykh A., Volchkov V.E.;
RT "Ebola virus glycoprotein GP is not cytotoxic when expressed constitutively
RT at a moderate level.";
RL J. Gen. Virol. 87:1247-1257(2006).
RN [32]
RP FUNCTION OF SIGNAL PEPTIDE.
RX PubMed=16775318; DOI=10.1128/jvi.02545-05;
RA Marzi A., Akhavan A., Simmons G., Gramberg T., Hofmann H., Bates P.,
RA Lingappa V.R., Poehlmann S.;
RT "The signal peptide of the ebolavirus glycoprotein influences interaction
RT with the cellular lectins DC-SIGN and DC-SIGNR.";
RL J. Virol. 80:6305-6317(2006).
RN [33]
RP RECEPTOR-BINDING REGION.
RX PubMed=16595665; DOI=10.1074/jbc.m601796200;
RA Kuhn J.H., Radoshitzky S.R., Guth A.C., Warfield K.L., Li W., Vincent M.J.,
RA Towner J.S., Nichol S.T., Bavari S., Choe H., Aman M.J., Farzan M.;
RT "Conserved receptor-binding domains of Lake Victoria marburgvirus and Zaire
RT ebolavirus bind a common receptor.";
RL J. Biol. Chem. 281:15951-15958(2006).
RN [34]
RP FUNCTION.
RX PubMed=20862315; DOI=10.1371/journal.ppat.1001110;
RA Saeed M.F., Kolokoltsov A.A., Albrecht T., Davey R.A.;
RT "Cellular entry of ebola virus involves uptake by a macropinocytosis-like
RT mechanism and subsequent trafficking through early and late endosomes.";
RL PLoS Pathog. 6:0-0(2010).
RN [35]
RP FUNCTION.
RX PubMed=20202662; DOI=10.1016/j.virol.2010.02.015;
RA Bhattacharyya S., Warfield K.L., Ruthel G., Bavari S., Aman M.J.,
RA Hope T.J.;
RT "Ebola virus uses clathrin-mediated endocytosis as an entry pathway.";
RL Virology 401:18-28(2010).
RN [36]
RP INTERACTION WITH HOST NPC1 (ENVELOPE GLYCOPROTEIN), AND FUNCTION (GP1).
RX PubMed=21866103; DOI=10.1038/nature10348;
RA Carette J.E., Raaben M., Wong A.C., Herbert A.S., Obernosterer G.,
RA Mulherkar N., Kuehne A.I., Kranzusch P.J., Griffin A.M., Ruthel G.,
RA Dal Cin P., Dye J.M., Whelan S.P., Chandran K., Brummelkamp T.R.;
RT "Ebola virus entry requires the cholesterol transporter Niemann-Pick C1.";
RL Nature 477:340-343(2011).
RN [37]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE (GP1).
RX PubMed=22031933; DOI=10.1128/jvi.05708-11;
RA Brecher M., Schornberg K.L., Delos S.E., Fusco M.L., Saphire E.O.,
RA White J.M.;
RT "Cathepsin cleavage potentiates the Ebola virus glycoprotein to undergo a
RT subsequent fusion-relevant conformational change.";
RL J. Virol. 86:364-372(2012).
RN [38]
RP FUNCTION (SHED GP), SUBCELLULAR LOCATION (SHED GP), AND GLYCOSYLATION (SHED
RP GP).
RX PubMed=25412102; DOI=10.1371/journal.ppat.1004509;
RA Escudero-Perez B., Volchkova V.A., Dolnik O., Lawrence P., Volchkov V.E.;
RT "Shed GP of Ebola virus triggers immune activation and increased vascular
RT permeability.";
RL PLoS Pathog. 10:E1004509-E1004509(2014).
RN [39]
RP FUNCTION (ENVELOPE GLYCOPROTEIN).
RX PubMed=26516900; DOI=10.3390/v7102888;
RA Vande Burgt N.H., Kaletsky R.L., Bates P.;
RT "Requirements within the Ebola viral glycoprotein for tetherin
RT antagonism.";
RL Viruses 7:5587-5602(2015).
RN [40]
RP FUNCTION (SHED GP), AND MUTAGENESIS OF LEU-635 AND ASP-637.
RX PubMed=26092855; DOI=10.1093/infdis/jiv268;
RA Dolnik O., Volchkova V.A., Escudero-Perez B., Lawrence P., Klenk H.D.,
RA Volchkov V.E.;
RT "Shedding of Ebola Virus Surface Glycoprotein Is a Mechanism of Self-
RT regulation of Cellular Cytotoxicity and Has a Direct Effect on Virus
RT Infectivity.";
RL J. Infect. Dis. 212:S322-S328(2015).
RN [41]
RP FUNCTION (ENVELOPE GLYCOPROTEIN), INTERACTION WITH HOST BST2 (ENVELOPE
RP GLYCOPROTEIN), AND MUTAGENESIS OF PHE-88; LEU-111 AND LEU-122.
RX PubMed=27707924; DOI=10.1128/jvi.01563-16;
RA Brinkmann C., Nehlmeier I., Walendy-Gnirss K., Nehls J.,
RA Gonzalez Hernandez M., Hoffmann M., Qiu X., Takada A., Schindler M.,
RA Poehlmann S.;
RT "The Tetherin Antagonism of the Ebola Virus Glycoprotein Requires an Intact
RT Receptor-Binding Domain and Can Be Blocked by GP1-Specific Antibodies.";
RL J. Virol. 90:11075-11086(2016).
RN [42]
RP INTERACTION WITH HOST FCN1 (ENVELOPE GLYCOPROTEIN).
RX PubMed=26984723; DOI=10.1128/jvi.00232-16;
RA Favier A.L., Gout E., Reynard O., Ferraris O., Kleman J.P., Volchkov V.,
RA Peyrefitte C., Thielens N.M.;
RT "Enhancement of Ebola Virus Infection via Ficolin-1 Interaction with the
RT Mucin Domain of GP Glycoprotein.";
RL J. Virol. 90:5256-5269(2016).
RN [43]
RP FUNCTION (ENVELOPE GLYCOPROTEIN), AND INTERACTION WITH HOST TLR4 (ENVELOPE
RP GLYCOPROTEIN).
RX PubMed=28542576; DOI=10.1371/journal.ppat.1006397;
RA Iampietro M., Younan P., Nishida A., Dutta M., Lubaki N.M., Santos R.I.,
RA Koup R.A., Katze M.G., Bukreyev A.;
RT "Ebola virus glycoprotein directly triggers T lymphocyte death despite of
RT the lack of infection.";
RL PLoS Pathog. 13:E1006397-E1006397(2017).
RN [44]
RP FUNCTION (ENVELOPE GLYCOPROTEIN).
RX PubMed=28878074; DOI=10.1128/jvi.01308-17;
RA Rizk M.G., Basler C.F., Guatelli J.;
RT "Cooperation of the Ebola Virus Proteins VP40 and GP1,2 with BST2 To
RT Activate NF-kappaB Independently of Virus-Like Particle Trapping.";
RL J. Virol. 91:0-0(2017).
RN [45]
RP FUNCTION (ENVELOPE GLYCOPROTEIN), MOTIF, AND MUTAGENESIS OF GLY-660 AND
RP ALA-664.
RX PubMed=29669839; DOI=10.1128/jvi.00403-18;
RA Gonzalez-Hernandez M., Hoffmann M., Brinkmann C., Nehls J., Winkler M.,
RA Schindler M., Poehlmann S.;
RT "A GXXXA Motif in the Transmembrane Domain of the Ebola Virus Glycoprotein
RT Is Required for Tetherin Antagonism.";
RL J. Virol. 92:0-0(2018).
RN [46]
RP FUNCTION (ENVELOPE GLYCOPROTEIN).
RX PubMed=30013549; DOI=10.3389/fimmu.2018.01428;
RA Edri A., Shemesh A., Iraqi M., Matalon O., Brusilovsky M., Hadad U.,
RA Radinsky O., Gershoni-Yahalom O., Dye J.M., Mandelboim O., Barda-Saad M.,
RA Lobel L., Porgador A.;
RT "The Ebola-Glycoprotein Modulates the Function of Natural Killer Cells.";
RL Front. Immunol. 9:1428-1428(2018).
RN [47]
RP FUNCTION (SHED GP), AND SUBCELLULAR LOCATION (SHED GP).
RX PubMed=30085081; DOI=10.1093/infdis/jiy406;
RA Iampietro M., Santos R.I., Lubaki N.M., Bukreyev A.;
RT "Ebola Virus Shed Glycoprotein Triggers Differentiation, Infection, and
RT Death of Monocytes Through Toll-Like Receptor 4 Activation.";
RL J. Infect. Dis. 218:S327-S334(2018).
RN [48]
RP INTERACTION WITH HOST NPC1, AND FUNCTION.
RX PubMed=32040508; DOI=10.1371/journal.pbio.3000626;
RA Das D.K., Bulow U., Diehl W.E., Durham N.D., Senjobe F., Chandran K.,
RA Luban J., Munro J.B.;
RT "Conformational changes in the Ebola virus membrane fusion machine induced
RT by pH, Ca2+, and receptor binding.";
RL PLoS Biol. 18:e3000626-e3000626(2020).
RN [49]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 557-630.
RX PubMed=10077567; DOI=10.1073/pnas.96.6.2662;
RA Malashkevich V.N., Schneider B.J., McNally M.L., Milhollen M.A., Pang J.X.,
RA Kim P.S.;
RT "Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-A
RT resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2662-2667(1999).
CC -!- FUNCTION: [Envelope glycoprotein]: Trimeric GP1,2 complexes form the
CC virion surface spikes and mediate the viral entry processes, with GP1
CC acting as the receptor-binding subunit and GP2 as the membrane fusion
CC subunit. At later times of infection, down-regulates the expression of
CC various host cell surface molecules that are essential for immune
CC surveillance and cell adhesion (PubMed:11836430). Down-modulates
CC several integrins including ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6,
CC ITGAV and ITGB1 (PubMed:11112476). This decrease in cell adhesion
CC molecules may lead to cell detachment, contributing to the disruption
CC of blood vessel integrity and hemorrhages developed during infection
CC (cytotoxicity) (Probable). Interacts with host TLR4 and thereby
CC stimulates the differentiation and activation of monocytes leading to
CC bystander death of T-lymphocytes (PubMed:28542576). Down-regulates as
CC well the function of host natural killer cells (PubMed:30013549).
CC Counteracts the antiviral effect of host BST2/tetherin that restricts
CC release of progeny virions from infected cells (PubMed:26516900,
CC PubMed:27707924, PubMed:29669839). However, cooperates with VP40 and
CC host BST2 to activate canonical NF-kappa-B pathway in a manner
CC dependent on neddylation (PubMed:28878074).
CC {ECO:0000269|PubMed:11112476, ECO:0000269|PubMed:11836430,
CC ECO:0000269|PubMed:26516900, ECO:0000269|PubMed:27707924,
CC ECO:0000269|PubMed:28542576, ECO:0000269|PubMed:28878074,
CC ECO:0000269|PubMed:29669839, ECO:0000269|PubMed:30013549,
CC ECO:0000305|PubMed:11112476}.
CC -!- FUNCTION: [Shed GP]: Functions as a decoy for anti-GP1,2 antibodies
CC thereby contributing to viral immune evasion. Interacts and activates
CC host macrophages and dendritic cells inducing up-regulation of cytokine
CC transcription. This effect is mediated throught activation of host
CC TLR4. {ECO:0000269|PubMed:25412102, ECO:0000269|PubMed:26092855,
CC ECO:0000269|PubMed:30085081}.
CC -!- FUNCTION: [GP1]: Responsible for binding to the receptor(s) on target
CC cells. Interacts with CD209/DC-SIGN and CLEC4M/DC-SIGNR which act as
CC cofactors for virus entry into dendritic cells (DCs) and endothelial
CC cells (PubMed:16051836). Binding to the macrophage specific lectin
CC CLEC10A also seems to enhance virus infectivity (By similarity).
CC Interaction with FOLR1/folate receptor alpha may be a cofactor for
CC virus entry in some cell types, although results are contradictory.
CC Members of the Tyro3 receptor tyrosine kinase family also seem to be
CC cell entry factors in filovirus infection (By similarity). Once
CC attached, the virions are internalized through clathrin-dependent
CC endocytosis and/or macropinocytosis. After internalization of the virus
CC into the endosomes of the host cell, proteolysis of GP1 by two cysteine
CC proteases, CTSB/cathepsin B and CTSL/cathepsin L removes the glycan cap
CC and allows GP1 binding to the host entry receptor NPC1
CC (PubMed:21866103, PubMed:32040508). NPC1-binding, Ca(2+) and acidic pH
CC induce a conformational change of GP2, which unmasks its fusion peptide
CC and permit membranes fusion (PubMed:21866103, PubMed:22031933,
CC PubMed:32040508). {ECO:0000250|UniProtKB:O11457,
CC ECO:0000250|UniProtKB:Q66814, ECO:0000269|PubMed:16051836,
CC ECO:0000269|PubMed:21866103, ECO:0000269|PubMed:22031933,
CC ECO:0000269|PubMed:32040508}.
CC -!- FUNCTION: [GP2]: Acts as a class I viral fusion protein. Under the
CC current model, the protein has at least 3 conformational states: pre-
CC fusion native state, pre-hairpin intermediate state, and post-fusion
CC hairpin state. During viral and target cell membrane fusion, the coiled
CC coil regions (heptad repeats) assume a trimer-of-hairpins structure,
CC positioning the fusion peptide in close proximity to the C-terminal
CC region of the ectodomain. The formation of this structure appears to
CC drive apposition and subsequent fusion of viral and target cell
CC membranes. Responsible for penetration of the virus into the cell
CC cytoplasm by mediating the fusion of the membrane of the endocytosed
CC virus particle with the endosomal membrane. Low pH in endosomes induces
CC an irreversible conformational change in GP2, releasing the fusion
CC hydrophobic peptide.
CC -!- SUBUNIT: [Envelope glycoprotein]: Homotrimer; each monomer consists of
CC a GP1 and a GP2 subunit linked by disulfide bonds. The resulting
CC peplomers (GP1,2) protrude from the virus surface as spikes. Interacts
CC with host integrin alpha-V/ITGAV (PubMed:15596847). Interacts with host
CC CLEC10A (PubMed:14990712). Binds also to host CD209 and CLEC4M/DC-
CC SIGN(R) (PubMed:12050398, PubMed:12504546). Interacts with host FOLR1
CC (PubMed:11461707). Interacts with BST2; this interaction inhibits the
CC antiviral effect of BST2 and this allows viral release from infected
CC cells (PubMed:27707924). Interacts with host FCN1; this interaction
CC enhances viral entry (PubMed:26984723). Interacts with host TLR4; this
CC interaction induces T-lymphocyte death (PubMed:28542576).
CC {ECO:0000269|PubMed:11461707, ECO:0000269|PubMed:12050398,
CC ECO:0000269|PubMed:12504546, ECO:0000269|PubMed:14990712,
CC ECO:0000269|PubMed:15596847, ECO:0000269|PubMed:26984723,
CC ECO:0000269|PubMed:27707924, ECO:0000269|PubMed:28542576}.
CC -!- SUBUNIT: [GP1]: Interacts with host entry receptor NPC1.
CC {ECO:0000269|PubMed:21866103, ECO:0000269|PubMed:32040508}.
CC -!- SUBUNIT: [Shed GP]: GP1 and GP2delta are part of GP1,2delta soluble
CC complexes released by ectodomain shedding.
CC {ECO:0000269|PubMed:15681442}.
CC -!- INTERACTION:
CC Q05320; Q05320: GP; NbExp=3; IntAct=EBI-16200230, EBI-16200230;
CC -!- SUBCELLULAR LOCATION: [GP2]: Virion membrane
CC {ECO:0000305|PubMed:11877482}; Single-pass type I membrane protein
CC {ECO:0000255}. Host cell membrane {ECO:0000305|PubMed:11877482};
CC Single-pass type I membrane protein {ECO:0000255}. Note=In the cell,
CC localizes to the plasma membrane lipid rafts, which probably represent
CC the assembly and budding site. {ECO:0000305|PubMed:11877482}.
CC -!- SUBCELLULAR LOCATION: [GP1]: Virion membrane
CC {ECO:0000305|PubMed:11877482}; Peripheral membrane protein. Host cell
CC membrane {ECO:0000305|PubMed:11877482}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9576958}. Note=GP1 is not anchored to the viral
CC envelope, but forms a disulfid-linked complex with the extravirion
CC surface GP2 (PubMed:9576958). In the cell, both GP1 and GP2 localize to
CC the plasma membrane lipid rafts, which probably represent the assembly
CC and budding site (PubMed:11877482). GP1 can also be shed after
CC proteolytic processing. {ECO:0000269|PubMed:11877482,
CC ECO:0000269|PubMed:9576958}.
CC -!- SUBCELLULAR LOCATION: [Shed GP]: Secreted {ECO:0000269|PubMed:15103332,
CC ECO:0000269|PubMed:25412102, ECO:0000269|PubMed:30085081}. Note=GP2-
CC delta bound to GP1 (GP1,2-delta) is produced by proteolytic cleavage of
CC GP1,2 by host ADAM17 and shed by the virus.
CC {ECO:0000269|PubMed:15103332}.
CC -!- DOMAIN: [GP1]: The mucin-like region seems to be involved in the
CC cytotoxic function. This region is also involved in binding to human
CC CLEC10A.
CC -!- DOMAIN: The coiled coil regions play a role in oligomerization and
CC fusion activity.
CC -!- PTM: The signal peptide region modulates GP's high mannose
CC glycosylation, thereby determining the efficiency of the interactions
CC with DC-SIGN(R). {ECO:0000269|PubMed:12438572}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12438572}.
CC -!- PTM: [Shed GP]: Glycosylated; glycosylation is essential for the
CC activation of dendritic cells and macrophages.
CC {ECO:0000269|PubMed:25412102}.
CC -!- PTM: [GP1]: O-glycosylated in the mucin-like region.
CC {ECO:0000269|PubMed:12438572}.
CC -!- PTM: [GP2]: Palmitoylation is not required for its function.
CC {ECO:0000269|PubMed:11152533}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. The
CC precursor is processed into GP1 and GP2 by host cell furin in the trans
CC Golgi, and maybe by other host proteases, to yield the mature GP1 and
CC GP2 proteins (PubMed:9576958, PubMed:9614872) (PubMed:9882347). The
CC cleavage site corresponds to the furin optimal cleavage sequence [KR]-
CC X-[KR]-R (PubMed:9576958). This cleavage does not seem to be required
CC for function (PubMed:9576958). After the internalization of the virus
CC into cell endosomes, GP1 C-terminus is removed by the endosomal
CC proteases cathepsin B, cathepsin L, or both, leaving a 19-kDa N-
CC terminal fragment which is further digested by cathepsin B
CC (PubMed:16571833). This cleaved 19-kDa GP1 can then bind to the host
CC entry receptor NPC1 (PubMed:21866103). Proteolytic processing of GP1,2
CC by host ADAM17 can remove the transmembrane anchor of GP2 and leads to
CC shedding of complexes consisting in GP1 and truncated GP2 (GP1,2delta)
CC (PubMed:15103332). {ECO:0000269|PubMed:11152533,
CC ECO:0000269|PubMed:15103332, ECO:0000269|PubMed:16571833,
CC ECO:0000269|PubMed:21866103, ECO:0000269|PubMed:9576958,
CC ECO:0000269|PubMed:9614872, ECO:0000269|PubMed:9882347}.
CC -!- RNA EDITING: Modified_positions=295 {ECO:0000269|PubMed:8553543,
CC ECO:0000269|PubMed:8622982}; Note=Partially edited. RNA editing at this
CC position consists of an insertion of one or two adenine nucleotides.
CC The sequence displayed here is the full-length transmembrane
CC glycoprotein GP, derived from the +1A edited RNA. The unedited RNA
CC gives rise to the small secreted glycoprotein sGP (AC P60170), the +2A
CC edited RNA gives rise to the super small secreted glycoprotein ssGP (AC
CC Q9YMG2).;
CC -!- MISCELLANEOUS: Filoviruses entry requires functional lipid rafts at the
CC host cell surface.
CC -!- MISCELLANEOUS: Essential for infectivity, as it is the sole viral
CC protein expressed at the virion surface.
CC -!- SIMILARITY: Belongs to the filoviruses glycoprotein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA96744.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L11365; AAB81004.1; -; Genomic_RNA.
DR EMBL; U31033; AAA96744.1; ALT_FRAME; Genomic_RNA.
DR EMBL; U23187; AAC54887.1; -; Genomic_RNA.
DR EMBL; AF272001; AAG40168.1; -; Genomic_RNA.
DR EMBL; AY142960; AAN37507.1; -; Genomic_RNA.
DR EMBL; AF086833; AAD14585.1; -; Genomic_RNA.
DR EMBL; AF499101; AAM76034.1; -; Genomic_RNA.
DR PIR; S23155; S23155.
DR RefSeq; NP_066246.1; NC_002549.1.
DR PDB; 2EBO; X-ray; 1.90 A; A/B/C=557-630.
DR PDB; 2RLJ; NMR; -; A=524-539.
DR PDB; 3CSY; X-ray; 3.40 A; I/K/M/O=32-311, J/L/N/P=464-501.
DR PDB; 5FHC; X-ray; 6.70 A; J=502-599, K=1-308, K=490-501.
DR PDB; 5HJ3; X-ray; 3.30 A; C/G/K/O=32-194.
DR PDB; 5JQ3; X-ray; 2.23 A; A=32-501, B=502-632.
DR PDB; 5JQ7; X-ray; 2.69 A; A=32-501, B=502-632.
DR PDB; 5JQB; X-ray; 2.68 A; A=32-501, B=502-632.
DR PDB; 5KEL; EM; 4.30 A; A/E/F=33-501, B/G/I=502-637.
DR PDB; 5KEM; EM; 5.50 A; A/F=53-284.
DR PDB; 5KEN; EM; 4.30 A; A/E/K=33-308, B/F/M=503-615.
DR PDB; 6EA7; X-ray; 4.25 A; A/C/E=32-194, B/D/F=502-612.
DR PDB; 6EAY; X-ray; 3.72 A; A=502-637, B=32-336.
DR PDB; 6F5U; X-ray; 2.07 A; A=32-312, B=502-632.
DR PDB; 6F6I; X-ray; 2.40 A; A=32-336, B=502-632.
DR PDB; 6F6N; X-ray; 2.15 A; A=32-336.
DR PDB; 6F6S; X-ray; 2.29 A; A=32-336.
DR PDB; 6G95; X-ray; 2.31 A; A=32-311, B=502-632.
DR PDB; 6G9B; X-ray; 2.26 A; A=32-311, B=502-632.
DR PDB; 6G9I; X-ray; 2.19 A; A=32-311, B=502-632.
DR PDB; 6HRO; X-ray; 2.30 A; A=32-312, B=502-632.
DR PDB; 6HS4; X-ray; 2.05 A; A=32-311, B=502-632.
DR PDB; 6MAM; X-ray; 4.10 A; G/I/K=32-226, H/J/L=502-611.
DR PDB; 6NAE; X-ray; 2.75 A; A=32-336, B=502-632.
DR PDB; 6OZ9; X-ray; 3.46 A; A=32-188, B=503-615.
DR PDB; 6QD7; EM; 3.10 A; A/C/E=32-311, B/D/F=502-632.
DR PDB; 6QD8; EM; 3.30 A; A/C/E=32-311, B/D/F=502-632.
DR PDB; 6S8D; EM; 3.49 A; A/C/E=32-334, B/D/F=502-632.
DR PDB; 6S8I; EM; 2.99 A; A/C/E=32-336, B/D/F=502-632.
DR PDB; 6S8J; EM; 2.91 A; A/C/E=32-336, B/D/F=502-632.
DR PDB; 6VKM; X-ray; 3.50 A; A=1-647.
DR PDB; 7JPH; X-ray; 3.19 A; B=502-637.
DR PDB; 7JPI; X-ray; 2.28 A; B=502-637.
DR PDB; 7KEJ; EM; 3.80 A; A/B/C=32-309, D/E/F=461-633.
DR PDB; 7KEX; EM; 4.25 A; A/B/C=32-309, D/E/F=461-629.
DR PDB; 7KF9; EM; 4.40 A; A/B/C=32-309, D/E/F=461-629.
DR PDB; 7KFB; EM; 3.90 A; A/B/C=32-309, D/E/F=461-629.
DR PDB; 7KFH; EM; 3.80 A; A/B/C=32-309, D/E/F=461-629.
DR PDB; 7LYD; X-ray; 2.35 A; A=32-318, B=502-632.
DR PDB; 7LYY; X-ray; 2.75 A; A=32-317, B=502-632.
DR PDB; 7M2D; X-ray; 2.70 A; A=32-317, B=502-632.
DR PDBsum; 2EBO; -.
DR PDBsum; 2RLJ; -.
DR PDBsum; 3CSY; -.
DR PDBsum; 5FHC; -.
DR PDBsum; 5HJ3; -.
DR PDBsum; 5JQ3; -.
DR PDBsum; 5JQ7; -.
DR PDBsum; 5JQB; -.
DR PDBsum; 5KEL; -.
DR PDBsum; 5KEM; -.
DR PDBsum; 5KEN; -.
DR PDBsum; 6EA7; -.
DR PDBsum; 6EAY; -.
DR PDBsum; 6F5U; -.
DR PDBsum; 6F6I; -.
DR PDBsum; 6F6N; -.
DR PDBsum; 6F6S; -.
DR PDBsum; 6G95; -.
DR PDBsum; 6G9B; -.
DR PDBsum; 6G9I; -.
DR PDBsum; 6HRO; -.
DR PDBsum; 6HS4; -.
DR PDBsum; 6MAM; -.
DR PDBsum; 6NAE; -.
DR PDBsum; 6OZ9; -.
DR PDBsum; 6QD7; -.
DR PDBsum; 6QD8; -.
DR PDBsum; 6S8D; -.
DR PDBsum; 6S8I; -.
DR PDBsum; 6S8J; -.
DR PDBsum; 6VKM; -.
DR PDBsum; 7JPH; -.
DR PDBsum; 7JPI; -.
DR PDBsum; 7KEJ; -.
DR PDBsum; 7KEX; -.
DR PDBsum; 7KF9; -.
DR PDBsum; 7KFB; -.
DR PDBsum; 7KFH; -.
DR PDBsum; 7LYD; -.
DR PDBsum; 7LYY; -.
DR PDBsum; 7M2D; -.
DR BMRB; Q05320; -.
DR SMR; Q05320; -.
DR DIP; DIP-62002N; -.
DR ELM; Q05320; -.
DR IntAct; Q05320; 1.
DR BindingDB; Q05320; -.
DR ChEMBL; CHEMBL4105829; -.
DR DrugBank; DB16385; Ansuvimab.
DR DrugBank; DB15898; Atoltivimab.
DR DrugBank; DB15899; Maftivimab.
DR DrugBank; DB15900; Odesivimab.
DR TCDB; 1.G.12.2.2; the avian leukosis virus gp95 fusion protein (alv-gp95) family.
DR ABCD; Q05320; 59 sequenced antibodies.
DR DNASU; 911829; -.
DR GeneID; 911829; -.
DR KEGG; vg:911829; -.
DR EvolutionaryTrace; Q05320; -.
DR Proteomes; UP000007209; Genome.
DR Proteomes; UP000109874; Genome.
DR Proteomes; UP000149419; Genome.
DR Proteomes; UP000150973; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:CACAO.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IMP:CACAO.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IDA:CACAO.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0039587; P:suppression by virus of host tetherin activity; IEA:UniProtKB-KW.
DR GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0046761; P:viral budding from plasma membrane; IDA:CACAO.
DR GO; GO:0046718; P:viral entry into host cell; IMP:CACAO.
DR InterPro; IPR014625; GPC_FiloV.
DR InterPro; IPR002561; GPC_filovir-type_extra_dom.
DR Pfam; PF01611; Filo_glycop; 1.
DR PIRSF; PIRSF036874; GPC_FiloV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Clathrin-mediated endocytosis of virus by host;
KW Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host membrane; Host-virus interaction;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host interferon signaling pathway by virus;
KW Inhibition of host tetherin by virus; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; RNA editing; Secreted; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell;
KW Viral attachment to host entry receptor; Viral envelope protein;
KW Viral immunoevasion; Viral penetration into host cytoplasm; Virion;
KW Virus endocytosis by host; Virus entry into host cell.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..676
FT /note="Envelope glycoprotein"
FT /id="PRO_0000037485"
FT CHAIN 33..637
FT /note="Shed GP"
FT /id="PRO_0000445686"
FT CHAIN 33..501
FT /note="GP1"
FT /id="PRO_0000037486"
FT CHAIN 502..676
FT /note="GP2"
FT /id="PRO_0000037487"
FT TOPO_DOM 33..650
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 651..671
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 672..676
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 54..201
FT /note="Receptor-binding"
FT /evidence="ECO:0000255"
FT REGION 305..485
FT /note="Mucin-like region"
FT REGION 315..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..539
FT /note="Fusion peptide"
FT /evidence="ECO:0000305"
FT COILED 554..595
FT /evidence="ECO:0000255"
FT COILED 615..634
FT /evidence="ECO:0000255"
FT MOTIF 660..664
FT /note="Important role for host BST2/tetherin antagonism"
FT /evidence="ECO:0000269|PubMed:27707924"
FT COMPBIAS 416..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 57
FT /note="Involved in receptor recognition and/or post-binding
FT events"
FT /evidence="ECO:0000255"
FT SITE 63
FT /note="Involved in receptor recognition and/or post-binding
FT events"
FT /evidence="ECO:0000255"
FT SITE 64
FT /note="Involved in receptor recognition and/or post-binding
FT events"
FT /evidence="ECO:0000255"
FT SITE 88
FT /note="Involved in receptor recognition and/or post-binding
FT events"
FT /evidence="ECO:0000255"
FT SITE 95
FT /note="Involved in receptor recognition and/or post-binding
FT events"
FT /evidence="ECO:0000255"
FT SITE 170
FT /note="Involved in receptor recognition and/or post-binding
FT events"
FT /evidence="ECO:0000255"
FT SITE 501..502
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000269|PubMed:9576958"
FT SITE 637..638
FT /note="Cleavage; by host ADAM17"
FT /evidence="ECO:0000269|PubMed:15103332"
FT LIPID 670
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:11152533"
FT LIPID 672
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:11152533"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 53..609
FT /note="Interchain (between GP1 and GP2 chains)"
FT /evidence="ECO:0000269|PubMed:12438572"
FT DISULFID 108..135
FT /evidence="ECO:0000255"
FT DISULFID 121..147
FT /evidence="ECO:0000255"
FT DISULFID 511..556
FT /evidence="ECO:0000255"
FT DISULFID 601..608
FT /evidence="ECO:0000269|PubMed:12438572"
FT VARIANT 65
FT /note="S -> P (in strain: Isolate mouse-adapted)"
FT VARIANT 246
FT /note="S -> P (in strain: Isolate mouse-adapted)"
FT VARIANT 544
FT /note="I -> T"
FT MUTAGEN 40
FT /note="N->D: Induces GP1 secretion. Complete loss of virus
FT capability to enter into host cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 53
FT /note="C->G: Induces GP1 secretion. Complete loss of virus
FT capability to enter into host cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 55
FT /note="D->A: 80% loss of virus capability to enter into
FT host cell."
FT MUTAGEN 55
FT /note="D->E,K: No effect on viral entry."
FT MUTAGEN 57
FT /note="L->A: Complete loss of virus capability to enter
FT into host cell."
FT MUTAGEN 57
FT /note="L->F,I,K: 90% loss of virus capability to enter into
FT host cell."
FT MUTAGEN 63
FT /note="L->A: 90% loss of virus capability to enter into
FT host cell."
FT MUTAGEN 63
FT /note="L->F: Almost complete loss of virus capability to
FT enter into host cell."
FT MUTAGEN 63
FT /note="L->K: Complete loss of virus capability to enter
FT into host cell."
FT MUTAGEN 64
FT /note="R->A,E: Complete loss of virus capability to enter
FT into host cell."
FT MUTAGEN 64
FT /note="R->K: No loss of virus capability to enter into host
FT cell."
FT MUTAGEN 88
FT /note="F->A,E: Complete loss of virus capability to enter
FT into host cell."
FT MUTAGEN 88
FT /note="F->A: About 50% loss of ability to counteract host
FT BST2."
FT /evidence="ECO:0000269|PubMed:27707924"
FT MUTAGEN 88
FT /note="F->I: No loss of virus capability to enter into host
FT cell."
FT MUTAGEN 95
FT /note="K->A,E: 80% loss of virus capability to enter into
FT host cell."
FT MUTAGEN 95
FT /note="K->R: 20% loss of virus capability to enter into
FT host cell."
FT MUTAGEN 108
FT /note="C->G: Almost complete loss of expression of GP1 and
FT GP2. Almost complete loss of virus capability to enter into
FT host cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 111
FT /note="L->A: About 60% loss of ability to counteract host
FT BST2."
FT /evidence="ECO:0000269|PubMed:27707924"
FT MUTAGEN 121
FT /note="C->G: Reduced levels of expression of GP1 and GP2.
FT 50% loss of virus capability to enter into host cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 122
FT /note="L->A: About 60% loss of ability to counteract host
FT BST2."
FT /evidence="ECO:0000269|PubMed:27707924"
FT MUTAGEN 135
FT /note="C->S: Almost complete loss of expression of GP1 and
FT GP2. Complete loss of virus capability to enter into host
FT cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 147
FT /note="C->S: Reduced levels of expression of GP1 and GP2.
FT Almost complete loss of virus capability to enter into host
FT cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 170
FT /note="I->A: 90% loss of virus capability to enter into
FT host cell."
FT MUTAGEN 170
FT /note="I->E: Complete loss of virus capability to enter
FT into host cell."
FT MUTAGEN 170
FT /note="I->F: 50% loss of virus capability to enter into
FT host cell."
FT MUTAGEN 204
FT /note="N->D: No effect on GP1 and GP2 expression. No loss
FT of virus capability to enter into host cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 238
FT /note="N->Y: No effect on GP1 and GP2 expression. 12% loss
FT of virus capability to enter into host cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 257
FT /note="N->D: No effect on GP1 and GP2 expression. 12% loss
FT of virus capability to enter into host cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 296
FT /note="N->D: No effect on GP1 and GP2 expression. 18% loss
FT of virus capability to enter into host cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 497..501
FT /note="RRTRR->AGTAA: Almost complete loss of cleavage
FT between GP1 and GP2. No loss of infectivity."
FT /evidence="ECO:0000269|PubMed:11152533"
FT MUTAGEN 498..501
FT /note="RTRR->ATAA: No effect on cleavage between GP1 and
FT GP2."
FT /evidence="ECO:0000269|PubMed:9882347"
FT MUTAGEN 511
FT /note="C->G: Induces GP1 secretion. Complete loss of virus
FT capability to enter into host cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 528
FT /note="G->R: Reduced infectivity."
FT /evidence="ECO:0000269|PubMed:10482652"
FT MUTAGEN 529
FT /note="L->A,R: Reduced infectivity."
FT /evidence="ECO:0000269|PubMed:10482652"
FT MUTAGEN 532
FT /note="I->A: Reduced infectivity."
FT /evidence="ECO:0000269|PubMed:10482652"
FT MUTAGEN 532
FT /note="I->R: Almost complete loss of infectivity. No effect
FT on transport of GP to the cell surface and incorporation
FT onto virions."
FT /evidence="ECO:0000269|PubMed:10482652"
FT MUTAGEN 535
FT /note="F->A: Reduced infectivity."
FT /evidence="ECO:0000269|PubMed:10482652"
FT MUTAGEN 535
FT /note="F->R: Almost complete loss of infectivity. No effect
FT on transport of GP to the cell surface and incorporation
FT onto virions."
FT /evidence="ECO:0000269|PubMed:10482652"
FT MUTAGEN 536
FT /note="G->A: Almost complete loss of infectivity. No effect
FT on transport of GP to the cell surface and incorporation
FT onto virions."
FT /evidence="ECO:0000269|PubMed:10482652"
FT MUTAGEN 537
FT /note="P->R: Almost complete loss of infectivity. No effect
FT on transport of GP to the cell surface and incorporation
FT onto virions."
FT /evidence="ECO:0000269|PubMed:10482652"
FT MUTAGEN 556
FT /note="C->S: Induces GP1 secretion. Complete loss of virus
FT capability to enter into host cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 563
FT /note="N->D: Reduced levels of expression of GP, GP1 and
FT GP2. 20% loss of virus capability to enter into host cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 601
FT /note="C->S: Induces GP1 secretion. Complete loss of virus
FT capability to enter into host cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 608
FT /note="C->G: Induces GP1 secretion. Complete loss of virus
FT capability to enter into host cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 609
FT /note="C->G: Induces GP1 secretion. Complete loss of virus
FT capability to enter into host cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 618
FT /note="N->D: Slightly reduced levels of expression of GP1
FT and GP2. No loss of virus capability to enter into host
FT cell."
FT /evidence="ECO:0000269|PubMed:12438572"
FT MUTAGEN 632
FT /note="D->V: No effect on release of soluble GP1,2delta."
FT /evidence="ECO:0000269|PubMed:15103332"
FT MUTAGEN 633
FT /note="K->R,V: No effect on release of soluble GP1,2delta."
FT /evidence="ECO:0000269|PubMed:15103332"
FT MUTAGEN 634
FT /note="T->I: 50% loss of release of soluble GP1,2delta."
FT /evidence="ECO:0000269|PubMed:15103332"
FT MUTAGEN 635
FT /note="L->V: 60% loss of release of soluble GP1,2delta."
FT /evidence="ECO:0000269|PubMed:15103332"
FT MUTAGEN 635
FT /note="L->V: Increased GP shedding."
FT /evidence="ECO:0000269|PubMed:26092855"
FT MUTAGEN 636
FT /note="P->A: 60% loss of release of soluble GP1,2delta."
FT MUTAGEN 637
FT /note="D->E: No effect on release of soluble GP1,2delta."
FT /evidence="ECO:0000269|PubMed:15103332"
FT MUTAGEN 637
FT /note="D->L,V: Increased release of soluble GP1,2delta."
FT /evidence="ECO:0000269|PubMed:15103332"
FT MUTAGEN 637
FT /note="D->V: Decreased GP shedding."
FT /evidence="ECO:0000269|PubMed:26092855"
FT MUTAGEN 638
FT /note="Q->V: No effect on release of soluble GP1,2delta."
FT /evidence="ECO:0000269|PubMed:15103332"
FT MUTAGEN 639
FT /note="G->V: 40% loss of release of soluble GP1,2delta."
FT /evidence="ECO:0000269|PubMed:15103332"
FT MUTAGEN 640
FT /note="D->V: No effect on release of soluble GP1,2delta."
FT /evidence="ECO:0000269|PubMed:15103332"
FT MUTAGEN 641
FT /note="N->A: No effect on release of soluble GP1,2delta."
FT /evidence="ECO:0000269|PubMed:15103332"
FT MUTAGEN 642
FT /note="D->V: No effect on release of soluble GP1,2delta."
FT /evidence="ECO:0000269|PubMed:15103332"
FT MUTAGEN 643
FT /note="N->A: No effect on release of soluble GP1,2delta."
FT /evidence="ECO:0000269|PubMed:15103332"
FT MUTAGEN 660
FT /note="G->L: About 60% loss of viral release; when
FT associated with L-664."
FT /evidence="ECO:0000269|PubMed:29669839"
FT MUTAGEN 664
FT /note="A->L: About 60% loss of viral release; when
FT associated with L-660."
FT /evidence="ECO:0000269|PubMed:29669839"
FT MUTAGEN 670
FT /note="C->A: Reduced palmitoylation. No effect on GP
FT processing and association with retrovirus particle. No
FT loss of virus capability to enter into host cell. Loss of
FT localization to the rafts; when associated with A-670."
FT /evidence="ECO:0000269|PubMed:11152533,
FT ECO:0000269|PubMed:11877482, ECO:0000269|PubMed:12438572"
FT MUTAGEN 670
FT /note="C->F: Slightly reduced levels of expression of GP1
FT and GP2. Greatly reduced GP processing and association with
FT retrovirus particle. 43% loss of virus capability to enter
FT into host cell. Loss of localization to the rafts; when
FT associated with A-672."
FT /evidence="ECO:0000269|PubMed:11152533,
FT ECO:0000269|PubMed:11877482, ECO:0000269|PubMed:12438572"
FT MUTAGEN 672
FT /note="C->A: Reduced palmitoylation. No effect on GP
FT processing and association with retrovirus particle. No
FT loss of virus capability to enter into host cell."
FT /evidence="ECO:0000269|PubMed:11152533,
FT ECO:0000269|PubMed:12438572"
FT MUTAGEN 672
FT /note="C->F: Slightly reduced levels of expression of GP1
FT and GP2. Almost no effect on GP processing and association
FT with retrovirus particle. 24% loss of virus capability to
FT enter into host cell."
FT /evidence="ECO:0000269|PubMed:11152533,
FT ECO:0000269|PubMed:12438572"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:6HS4"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6QD7"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:6HS4"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:6HS4"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:3CSY"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 176..185
FT /evidence="ECO:0007829|PDB:6HS4"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:7JPI"
FT TURN 191..194
FT /evidence="ECO:0007829|PDB:7JPI"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:6HS4"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:6HS4"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:7LYD"
FT STRAND 515..520
FT /evidence="ECO:0007829|PDB:6HS4"
FT TURN 528..531
FT /evidence="ECO:0007829|PDB:6HS4"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:6HS4"
FT HELIX 539..541
FT /evidence="ECO:0007829|PDB:6HS4"
FT STRAND 543..548
FT /evidence="ECO:0007829|PDB:6HS4"
FT HELIX 551..553
FT /evidence="ECO:0007829|PDB:6HS4"
FT HELIX 560..594
FT /evidence="ECO:0007829|PDB:2EBO"
FT HELIX 595..597
FT /evidence="ECO:0007829|PDB:2EBO"
FT HELIX 600..604
FT /evidence="ECO:0007829|PDB:2EBO"
FT HELIX 605..609
FT /evidence="ECO:0007829|PDB:2EBO"
FT HELIX 616..628
FT /evidence="ECO:0007829|PDB:2EBO"
SQ 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
