Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]

 ENV_HV1H2               Reviewed;         856 AA.
P04578; O09779;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
15-JUL-1999, sequence version 2.
25-OCT-2017, entry version 161.
RecName: Full=Envelope glycoprotein gp160 {ECO:0000255|HAMAP-Rule:MF_04083};
AltName: Full=Env polyprotein {ECO:0000255|HAMAP-Rule:MF_04083};
Contains:
RecName: Full=Surface protein gp120 {ECO:0000255|HAMAP-Rule:MF_04083};
Short=SU {ECO:0000255|HAMAP-Rule:MF_04083};
AltName: Full=Glycoprotein 120 {ECO:0000255|HAMAP-Rule:MF_04083};
Short=gp120 {ECO:0000255|HAMAP-Rule:MF_04083};
Contains:
RecName: Full=Transmembrane protein gp41 {ECO:0000255|HAMAP-Rule:MF_04083};
Short=TM {ECO:0000255|HAMAP-Rule:MF_04083};
AltName: Full=Glycoprotein 41 {ECO:0000255|HAMAP-Rule:MF_04083};
Short=gp41 {ECO:0000255|HAMAP-Rule:MF_04083};
Flags: Precursor;
Name=env {ECO:0000255|HAMAP-Rule:MF_04083};
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
(HIV-1).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Primate lentivirus group.
NCBI_TaxID=11706;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=3040055; DOI=10.1089/aid.1987.3.57;
Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S.,
Gallo R.C., Wong-Staal F.;
"Complete nucleotide sequences of functional clones of the AIDS
virus.";
AIDS Res. Hum. Retroviruses 3:57-69(1987).
[2]
SEQUENCE REVISION.
Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S.,
Gallo R.C., Wong-Staal F.;
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION (ENVELOPE GLYCOPROTEIN GP160).
PubMed=2450679; DOI=10.1016/0092-8674(88)90487-4;
McCune J.M., Rabin L.B., Feinberg M.B., Lieberman M., Kosek J.C.,
Reyes G.R., Weissman I.L.;
"Endoproteolytic cleavage of gp160 is required for the activation of
human immunodeficiency virus.";
Cell 53:55-67(1988).
[4]
FUNCTION (TRANSMEMBRANE PROTEIN GP41).
PubMed=2243396;
Helseth E., Olshevsky U., Gabuzda D., Ardman B., Haseltine W.,
Sodroski J.;
"Changes in the transmembrane region of the human immunodeficiency
virus type 1 gp41 envelope glycoprotein affect membrane fusion.";
J. Virol. 64:6314-6318(1990).
[5]
FUNCTION (ENVELOPE GLYCOPROTEIN GP160).
PubMed=1360148; DOI=10.1038/360358a0;
Hallenberger S., Bosch V., Angliker H., Shaw E., Klenk H.D.,
Garten W.;
"Inhibition of furin-mediated cleavage activation of HIV-1
glycoprotein gp160.";
Nature 360:358-361(1992).
[6]
IMMUNOSUPPRESSIVE REGION.
PubMed=7986401;
Denner J., Norley S., Kurth R.;
"The immunosuppressive peptide of HIV-1: functional domains and immune
response in AIDS patients.";
AIDS 8:1063-1072(1994).
[7]
PALMITOYLATION, AND MUTAGENESIS OF CYS-764 AND CYS-837.
PubMed=7568235; DOI=10.1073/pnas.92.21.9871;
Yang C., Spies C.P., Compans R.W.;
"The human and simian immunodeficiency virus envelope glycoprotein
transmembrane subunits are palmitoylated.";
Proc. Natl. Acad. Sci. U.S.A. 92:9871-9875(1995).
[8]
INTERACTION OF SURFACE PROTEIN GP120 WITH GALACTOSYL CERAMIDE AND
SULFO-GALACTOSYL CERAMIDE.
PubMed=7494242;
Harouse J.M., Collman R.G., Gonzalez-Scarano F.;
"Human immunodeficiency virus type 1 infection of SK-N-MC cells:
domains of gp120 involved in entry into a CD4-negative, galactosyl
ceramide/3' sulfo-galactosyl ceramide-positive cell line.";
J. Virol. 69:7383-7390(1995).
[9]
DOMAIN YXXL MOTIF.
PubMed=10233963;
Deschambeault J., Lalonde J.P., Cervantes-Acosta G., Lodge R.,
Cohen E.A., Lemay G.;
"Polarized human immunodeficiency virus budding in lymphocytes
involves a tyrosine-based signal and favors cell-to-cell viral
transmission.";
J. Virol. 73:5010-5017(1999).
[10]
FUNCTION (SURFACE PROTEIN GP120).
PubMed=11257134; DOI=10.1084/jem.193.6.671;
Bashirova A.A., Geijtenbeek T.B.H., van Duijnhoven G.C.F.,
van Vliet S.J., Eilering J.B.G., Martin M.P., Wu L., Martin T.D.,
Viebig N., Knolle P.A., Kewalramani V.N., van Kooyk Y., Carrington M.;
"A dendritic cell-specific intercellular adhesion molecule 3-grabbing
nonintegrin (DC-SIGN)-related protein is highly expressed on human
liver sinusoidal endothelial cells and promotes HIV-1 infection.";
J. Exp. Med. 193:671-678(2001).
[11]
REVIEW.
PubMed=12974773; DOI=10.1034/j.1600-0463.2003.11107803.x;
Geijtenbeek T.B., van Kooyk Y.;
"Pathogens target DC-SIGN to influence their fate DC-SIGN functions as
a pathogen receptor with broad specificity.";
APMIS 111:698-714(2003).
[12]
DISULFIDE BOND.
PubMed=12218052; DOI=10.1074/jbc.M205467200;
Barbouche R., Miquelis R., Jones I.M., Fenouillet E.;
"Protein-disulfide isomerase-mediated reduction of two disulfide bonds
of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is
required for fusion.";
J. Biol. Chem. 278:3131-3136(2003).
[13]
INTERACTION OF SURFACE PROTEIN GP120 WITH HOST CD209/DC-SIGN AND
CLEC4M/DC-SIGNR.
PubMed=12502850; DOI=10.1128/JVI.77.2.1337-1346.2003;
Lin G., Simmons G., Poehlmann S., Baribaud F., Ni H., Leslie G.J.,
Haggarty B.S., Bates P., Weissman D., Hoxie J.A., Doms R.W.;
"Differential N-linked glycosylation of human immunodeficiency virus
and Ebola virus envelope glycoproteins modulates interactions with DC-
SIGN and DC-SIGNR.";
J. Virol. 77:1337-1346(2003).
[14]
STOICHIOMETRY (ENVELOPE GLYCOPROTEIN GP160).
PubMed=16160141; DOI=10.1128/JVI.79.19.12132-12147.2005;
Yang X., Kurteva S., Ren X., Lee S., Sodroski J.;
"Stoichiometry of envelope glycoprotein trimers in the entry of human
immunodeficiency virus type 1.";
J. Virol. 79:12132-12147(2005).
[15]
REVIEW.
PubMed=12873764; DOI=10.1016/S0005-2736(03)00161-5;
Gallo S.A., Finnegan C.M., Viard M., Raviv Y., Dimitrov A.,
Rawat S.S., Puri A., Durell S., Blumenthal R.;
"The HIV Env-mediated fusion reaction.";
Biochim. Biophys. Acta 1614:36-50(2003).
[16]
REVIEW.
PubMed=15719026; DOI=10.1038/sj.cdd.4401584;
Perfettini J.-L., Castedo M., Roumier T., Andreau K., Nardacci R.,
Piacentini M., Kroemer G.;
"Mechanisms of apoptosis induction by the HIV-1 envelope.";
Cell Death Differ. 12:916-923(2005).
[17]
REVIEW.
PubMed=15725757; DOI=10.1089/aid.2005.21.171;
Hartley O., Klasse P.J., Sattentau Q.J., Moore J.P.;
"V3: HIV's switch-hitter.";
AIDS Res. Hum. Retroviruses 21:171-189(2005).
[18]
REVIEW.
PubMed=16114975; DOI=10.2165/00003495-200565130-00002;
Reeves J.D., Piefer A.J.;
"Emerging drug targets for antiretroviral therapy.";
Drugs 65:1747-1766(2005).
[19]
REVIEW.
PubMed=16437164; DOI=10.1038/sj.emboj.7600947;
Lusso P.;
"HIV and the chemokine system: 10 years later.";
EMBO J. 25:447-456(2006).
[20]
DI-LEUCINE INTERNALIZATION MOTIF.
PubMed=17108326; DOI=10.1091/mbc.E06-06-0535;
Byland R., Vance P.J., Hoxie J.A., Marsh M.;
"A conserved dileucine motif mediates clathrin and AP-2-dependent
endocytosis of the HIV-1 envelope protein.";
Mol. Biol. Cell 18:414-425(2007).
[21]
MEMBRANE-PROXIMAL EXTERNAL REGION.
PubMed=18322034; DOI=10.1128/MMBR.00020-07;
Montero M., van Houten N.E., Wang X., Scott J.K.;
"The membrane-proximal external region of the human immunodeficiency
virus type 1 envelope: dominant site of antibody neutralization and
target for vaccine design.";
Microbiol. Mol. Biol. Rev. 72:54-84(2008).
[22]
INTERACTION OF SURFACE PROTEIN GP120 WITH HEPARAN SULFATE.
STRAIN=HXBC2;
PubMed=18378683; DOI=10.1074/jbc.M800066200;
Crublet E., Andrieu J.P., Vives R.R., Lortat-Jacob H.;
"The HIV-1 envelope glycoprotein gp120 features four heparan sulfate
binding domains, including the co-receptor binding site.";
J. Biol. Chem. 283:15193-15200(2008).
[23]
FUNCTION.
PubMed=19410541; DOI=10.1016/j.cell.2009.02.046;
Miyauchi K., Kim Y., Latinovic O., Morozov V., Melikyan G.B.;
"HIV enters cells via endocytosis and dynamin-dependent fusion with
endosomes.";
Cell 137:433-444(2009).
[24]
IMMUNOSUPPRESSIVE REGION.
PubMed=23383108; DOI=10.1371/journal.pone.0055199;
Denner J., Eschricht M., Lauck M., Semaan M., Schlaermann P., Ryu H.,
Akyuez L.;
"Modulation of cytokine release and gene expression by the
immunosuppressive domain of gp41 of HIV-1.";
PLoS ONE 8:E55199-E55199(2013).
[25]
GLYCOSYLATION AT ASN-88; ASN-156; ASN-160; ASN-197; ASN-234; ASN-262;
ASN-276; ASN-295; ASN-332; ASN-339; ASN-386; ASN-392; ASN-448; ASN-611
AND ASN-637.
STRAIN=BG505;
PubMed=26972002; DOI=10.1016/j.celrep.2016.02.058;
Behrens A.J., Vasiljevic S., Pritchard L.K., Harvey D.J., Andev R.S.,
Krumm S.A., Struwe W.B., Cupo A., Kumar A., Zitzmann N.,
Seabright G.E., Kramer H.B., Spencer D.I., Royle L., Lee J.H.,
Klasse P.J., Burton D.R., Wilson I.A., Ward A.B., Sanders R.W.,
Moore J.P., Doores K.J., Crispin M.;
"Composition and antigenic effects of individual glycan sites of a
trimeric HIV-1 envelope glycoprotein.";
Cell Rep. 14:2695-2706(2016).
[26]
GLYCOSYLATION.
PubMed=28667249; DOI=10.1038/s41598-017-04532-9;
Yang M., Huang J., Simon R., Wang L.X., MacKerell A.D. Jr.;
"Conformational heterogeneity of the HIV envelope glycan shield.";
Sci. Rep. 7:4435-4435(2017).
[27]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 628-661 AND 546-581.
PubMed=9108481; DOI=10.1016/S0092-8674(00)80205-6;
Chan D.C., Fass D., Berger J.M., Kim P.S.;
"Core structure of gp41 from the HIV envelope glycoprotein.";
Cell 89:263-273(1997).
[28]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 83-127; 195-297; 330-396 AND
410-492, AND GLYCOSYLATION AT ASN-197; ASN-262; ASN-276; ASN-289;
ASN-295; ASN-332; ASN-339; ASN-386; ASN-392 AND ASN-448.
PubMed=9641677; DOI=10.1038/31405;
Kwong P.D., Wyatt R., Robinson J., Sweet R.W., Sodroski J.,
Hendrickson W.A.;
"Structure of an HIV gp120 envelope glycoprotein in complex with the
CD4 receptor and a neutralizing human antibody.";
Nature 393:648-659(1998).
[29]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 546-579 AND 628-655.
PubMed=10677212; DOI=10.1021/bi9921687;
Shu W., Liu J., Ji H., Radigen L., Jiang S., Lu M.;
"Helical interactions in the HIV-1 gp41 core reveal structural basis
for the inhibitory activity of gp41 peptides.";
Biochemistry 39:1634-1642(2000).
[30]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 546-579 AND 628-655.
PubMed=10636883; DOI=10.1074/jbc.275.3.1839;
Shu W., Ji H., Lu M.;
"Interactions between HIV-1 gp41 core and detergents and their
implications for membrane fusion.";
J. Biol. Chem. 275:1839-1845(2000).
[31]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 83-127; 195-297 AND 330-492,
AND GLYCOSYLATION AT ASN-197; ASN-234; ASN-262; ASN-276; ASN-289;
ASN-295; ASN-339; ASN-386; ASN-392; ASN-448 AND ASN-463.
PubMed=11188697; DOI=10.1016/S0969-2126(00)00547-5;
Kwong P.D., Wyatt R., Majeed S., Robinson J., Sweet R.W., Sodroski J.,
Hendrickson W.A.;
"Structures of HIV-1 gp120 envelope glycoproteins from laboratory-
adapted and primary isolates.";
Structure 8:1329-1339(2000).
[32]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 546-579 AND 628-655.
PubMed=12044159; DOI=10.1021/bi025648y;
Wang S., York J., Shu W., Stoller M.O., Nunberg J.H., Lu M.;
"Interhelical interactions in the gp41 core: implications for
activation of HIV-1 membrane fusion.";
Biochemistry 41:7283-7292(2002).
[33]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 565-581.
PubMed=12417739; DOI=10.1073/pnas.232566599;
Sia S.K., Carr P.A., Cochran A.G., Malashkevich V.N., Kim P.S.;
"Short constrained peptides that inhibit HIV-1 entry.";
Proc. Natl. Acad. Sci. U.S.A. 99:14664-14669(2002).
[34]
STRUCTURE BY NMR OF 659-671.
PubMed=12860131; DOI=10.1016/S0022-2836(03)00611-9;
Barbato G., Bianchi E., Ingallinella P., Hurni W.H., Miller M.D.,
Ciliberto G., Cortese R., Bazzo R., Shiver J.W., Pessi A.;
"Structural analysis of the epitope of the anti-HIV antibody 2F5 sheds
light into its mechanism of neutralization and HIV fusion.";
J. Mol. Biol. 330:1101-1115(2003).
[35]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 195-492, AND GLYCOSYLATION
AT ASN-197; ASN-234; ASN-262; ASN-276; ASN-289; ASN-295; ASN-392;
ASN-448 AND ASN-463.
PubMed=14981267; DOI=10.1073/pnas.0308527100;
Huang C.C., Venturi M., Majeed S., Moore M.J., Phogat S., Zhang M.Y.,
Dimitrov D.S., Hendrickson W.A., Robinson J., Sodroski J., Wyatt R.,
Choe H., Farzan M., Kwong P.D.;
"Structural basis of tyrosine sulfation and VH-gene usage in
antibodies that recognize the HIV type 1 coreceptor-binding site on
gp120.";
Proc. Natl. Acad. Sci. U.S.A. 101:2706-2711(2004).
[36]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 83-492, AND GLYCOSYLATION AT
ASN-356.
PubMed=17301785; DOI=10.1038/nature05580;
Zhou T., Xu L., Dey B., Hessell A.J., Van Ryk D., Xiang S.H., Yang X.,
Zhang M.Y., Zwick M.B., Arthos J., Burton D.R., Dimitrov D.S.,
Sodroski J., Wyatt R., Nabel G.J., Kwong P.D.;
"Structural definition of a conserved neutralization epitope on HIV-1
gp120.";
Nature 445:732-737(2007).
[37]
STRUCTURE BY NMR OF 662-683.
PubMed=18191596; DOI=10.1016/j.immuni.2007.11.018;
Sun Z.Y., Oh K.J., Kim M., Yu J., Brusic V., Song L., Qiao Z.,
Wang J.H., Wagner G., Reinherz E.L.;
"HIV-1 broadly neutralizing antibody extracts its epitope from a
kinked gp41 ectodomain region on the viral membrane.";
Immunity 28:52-63(2008).
[38]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 660-670.
PubMed=18824005; DOI=10.1016/j.jmb.2008.09.024;
Julien J.P., Bryson S., Nieva J.L., Pai E.F.;
"Structural details of HIV-1 recognition by the broadly neutralizing
monoclonal antibody 2F5: epitope conformation, antigen-recognition
loop mobility, and anion-binding site.";
J. Mol. Biol. 384:377-392(2008).
[39]
STRUCTURE BY ELECTRON MICROSCOPY (20.00 ANGSTROMS) OF 90-124; 198-297;
330-396 AND 410-492.
PubMed=18668044; DOI=10.1038/nature07159;
Liu J., Bartesaghi A., Borgnia M.J., Sapiro G., Subramaniam S.;
"Molecular architecture of native HIV-1 gp120 trimers.";
Nature 455:109-113(2008).
[40]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 83-492, AND GLYCOSYLATION AT
ASN-88 AND ASN-356.
PubMed=19965434; DOI=10.1126/science.1175868;
Chen L., Kwon Y.D., Zhou T., Wu X., O'Dell S., Cavacini L.,
Hessell A.J., Pancera M., Tang M., Xu L., Yang Z.Y., Zhang M.Y.,
Arthos J., Burton D.R., Dimitrov D.S., Nabel G.J., Posner M.R.,
Sodroski J., Wyatt R., Mascola J.R., Kwong P.D.;
"Structural basis of immune evasion at the site of CD4 attachment on
HIV-1 gp120.";
Science 326:1123-1127(2009).
[41]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 543-582; 590-639; 625-662
AND 654-688.
PubMed=21124990; DOI=10.1371/journal.ppat.1001195;
Sabin C., Corti D., Buzon V., Seaman M.S., Lutje Hulsik D., Hinz A.,
Vanzetta F., Agatic G., Silacci C., Mainetti L., Scarlatti G.,
Sallusto F., Weiss R., Lanzavecchia A., Weissenhorn W.;
"Crystal structure and size-dependent neutralization properties of
HK20, a human monoclonal antibody binding to the highly conserved
heptad repeat 1 of gp41.";
PLoS Pathog. 6:E1001195-E1001195(2010).
[42]
X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 254-297; 330-401; 412-419
AND 445-477, AND GLYCOSYLATION AT ASN-332.
PubMed=21998254; DOI=10.1126/science.1213256;
Pejchal R., Doores K.J., Walker L.M., Khayat R., Huang P.S.,
Wang S.K., Stanfield R.L., Julien J.P., Ramos A., Crispin M.,
Depetris R., Katpally U., Marozsan A., Cupo A., Maloveste S., Liu Y.,
McBride R., Ito Y., Sanders R.W., Ogohara C., Paulson J.C., Feizi T.,
Scanlan C.N., Wong C.H., Moore J.P., Olson W.C., Ward A.B.,
Poignard P., Schief W.R., Burton D.R., Wilson I.A.;
"A potent and broad neutralizing antibody recognizes and penetrates
the HIV glycan shield.";
Science 334:1097-1103(2011).
[43]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 546-581.
PubMed=22228771; DOI=10.1074/jbc.M111.317883;
Yao X., Chong H., Zhang C., Waltersperger S., Wang M., Cui S., He Y.;
"Broad antiviral activity and crystal structure of HIV-1 fusion
inhibitor sifuvirtide.";
J. Biol. Chem. 287:6788-6796(2012).
[44]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 254-399, AND GLYCOSYLATION
AT ASN-262.
PubMed=23539181; DOI=10.1126/science.1234150;
Jardine J., Julien J.P., Menis S., Ota T., Kalyuzhniy O., McGuire A.,
Sok D., Huang P.S., MacPherson S., Jones M., Nieusma T., Mathison J.,
Baker D., Ward A.B., Burton D.R., Stamatatos L., Nemazee D.,
Wilson I.A., Schief W.R.;
"Rational HIV immunogen design to target specific germline B cell
receptors.";
Science 340:711-716(2013).
[45]
STRUCTURE BY NMR OF 657-683.
PubMed=24075869; DOI=10.1016/j.jmb.2013.09.030;
Sun Z.Y., Cheng Y., Kim M., Song L., Choi J., Kudahl U.J., Brusic V.,
Chowdhury B., Yu L., Seaman M.S., Bellot G., Shih W.M., Wagner G.,
Reinherz E.L.;
"Disruption of helix-capping residues 671 and 674 reveals a role in
HIV-1 entry for a specialized hinge segment of the membrane proximal
external region of gp41.";
J. Mol. Biol. 426:1095-1108(2014).
-!- FUNCTION: Envelope glycoprotein gp160: Oligomerizes in the host
endoplasmic reticulum into predominantly trimers. In a second
time, gp160 transits in the host Golgi, where glycosylation is
completed. The precursor is then proteolytically cleaved in the
trans-Golgi and thereby activated by cellular furin or furin-like
proteases to produce gp120 and gp41. {ECO:0000255|HAMAP-
Rule:MF_04083, ECO:0000269|PubMed:1360148,
ECO:0000269|PubMed:2450679}.
-!- FUNCTION: Surface protein gp120: Attaches the virus to the host
lymphoid cell by binding to the primary receptor CD4. This
interaction induces a structural rearrangement creating a high
affinity binding site for a chemokine coreceptor like CXCR4 and/or
CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR,
which are respectively found on dendritic cells (DCs), and on
endothelial cells of liver sinusoids and lymph node sinuses. These
interactions allow capture of viral particles at mucosal surfaces
by these cells and subsequent transmission to permissive cells.
HIV subverts the migration properties of dendritic cells to gain
access to CD4+ T-cells in lymph nodes. Virus transmission to
permissive T-cells occurs either in trans (without DCs infection,
through viral capture and transmission), or in cis (following DCs
productive infection, through the usual CD4-gp120 interaction),
thereby inducing a robust infection. In trans infection, bound
virions remain infectious over days and it is proposed that they
are not degraded, but protected in non-lysosomal acidic organelles
within the DCs close to the cell membrane thus contributing to the
viral infectious potential during DCs' migration from the
periphery to the lymphoid tissues. On arrival at lymphoid tissues,
intact virions recycle back to DCs' cell surface allowing virus
transmission to CD4+ T-cells. {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:11257134, ECO:0000269|PubMed:19410541}.
-!- FUNCTION: Transmembrane protein gp41: 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 fusion
of viral and target intracellular membranes, 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. Complete fusion occurs in host cell
endosomes and is dynamin-dependent, however some lipid transfer
might occur at the plasma membrane. The virus undergoes clathrin-
dependent internalization long before endosomal fusion, thus
minimizing the surface exposure of conserved viral epitopes during
fusion and reducing the efficacy of inhibitors targeting these
epitopes. Membranes fusion leads to delivery of the nucleocapsid
into the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:19410541, ECO:0000269|PubMed:2243396}.
-!- SUBUNIT: The mature envelope protein (Env) consists of a
homotrimer of non-covalently associated gp120-gp41 heterodimers.
The resulting complex protrudes from the virus surface as a spike.
There seems to be as few as 10 spikes on the average virion.
Surface protein gp120 interacts with host CD4, CCR5 and CXCR4.
Gp120 also interacts with the C-type lectins CD209/DC-SIGN and
CLEC4M/DC-SIGNR (collectively referred to as DC-SIGN(R)). Gp120
and gp41 interact with GalCer. Gp120 interacts with host
ITGA4/ITGB7 complex; on CD4+ T-cells, this interaction results in
rapid activation of integrin ITGAL/LFA-1, which facilitates
efficient cell-to-cell spreading of HIV-1. Gp120 interacts with
cell-associated heparan sulfate; this interaction increases virus
infectivity on permissive cells and may be involved in infection
of CD4- cells. {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:12502850, ECO:0000269|PubMed:18378683,
ECO:0000269|PubMed:7494242}.
-!- INTERACTION:
P27824:CANX (xeno); NbExp=3; IntAct=EBI-6163496, EBI-355947;
P01730:CD4 (xeno); NbExp=2; IntAct=EBI-6163496, EBI-353826;
P08962:CD63 (xeno); NbExp=4; IntAct=EBI-6179711, EBI-762053;
Q9ULD8:KCNH3 (xeno); NbExp=3; IntAct=EBI-6163496, EBI-8079227;
P04608:tat; NbExp=4; IntAct=EBI-6163496, EBI-6164389;
-!- SUBCELLULAR LOCATION: Surface protein gp120: Virion membrane
{ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein
{ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane
{ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein
{ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane
{ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=The surface
protein is not anchored to the viral envelope, but associates with
the extravirion surface through its binding to TM. It is probably
concentrated at the site of budding and incorporated into the
virions possibly by contacts between the cytoplasmic tail of Env
and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.
-!- SUBCELLULAR LOCATION: Transmembrane protein gp41: Virion membrane
{ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane
{ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane
{ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane
protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=It is probably
concentrated at the site of budding and incorporated into the
virions possibly by contacts between the cytoplasmic tail of Env
and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.
-!- DOMAIN: Some of the most genetically diverse regions of the viral
genome are present in Env. They are called variable regions 1
through 5 (V1 through V5). Coreceptor usage of gp120 is determined
mainly by the primary structure of the third variable region (V3)
in the outer domain of gp120. The sequence of V3 determines which
coreceptor, CCR5 and/or CXCR4 (corresponding to R5/macrophage,
X4/T cell and R5X4/T cell and macrophage tropism), is used to
trigger the fusion potential of the Env complex, and hence which
cells the virus can infect. Binding to CCR5 involves a region
adjacent in addition to V3. {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:10233963}.
-!- DOMAIN: The membrane proximal external region (MPER) present in
gp41 is a tryptophan-rich region recognized by the antibodies 2F5,
Z13, and 4E10. MPER seems to play a role in fusion.
{ECO:0000255|HAMAP-Rule:MF_04083, ECO:0000269|PubMed:10233963}.
-!- DOMAIN: The 17 amino acids long immunosuppressive region is
present in many retroviral envelope proteins. Synthetic peptides
derived from this relatively conserved sequence inhibit immune
function in vitro and in vivo. {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:23383108}.
-!- DOMAIN: The YXXL motif is involved in determining the exact site
of viral release at the surface of infected mononuclear cells and
promotes endocytosis. YXXL and di-leucine endocytosis motifs
interact directly or indirectly with the clathrin adapter
complexes, opperate independently, and their activities are not
additive. {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:10233963}.
-!- DOMAIN: The CD4-binding region is targeted by the antibody b12.
{ECO:0000255|HAMAP-Rule:MF_04083, ECO:0000269|PubMed:10233963}.
-!- PTM: Palmitoylation of the transmembrane protein and of Env
polyprotein (prior to its proteolytic cleavage) is essential for
their association with host cell membrane lipid rafts.
Palmitoylation is therefore required for envelope trafficking to
classical lipid rafts, but not for viral replication.
{ECO:0000255|HAMAP-Rule:MF_04083, ECO:0000269|PubMed:7568235}.
-!- PTM: Highly glycosylated by host. The high number of glycan on the
protein is reffered to as 'glycan shield' because it contributes
to hide protein sequence from adaptive immune system.
{ECO:0000255|HAMAP-Rule:MF_04083, ECO:0000269|PubMed:26972002,
ECO:0000269|PubMed:28667249}.
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
Envelope glycoproteins are synthesized as a inactive precursor
that is heavily N-glycosylated and processed likely by host cell
furin in the Golgi to yield the mature SU and TM proteins. The
cleavage site between SU and TM requires the minimal sequence
[KR]-X-[KR]-R. About 2 of the 9 disulfide bonds of gp41 are
reduced by P4HB/PDI, following binding to CD4 receptor.
{ECO:0000255|HAMAP-Rule:MF_04083, ECO:0000269|PubMed:12218052,
ECO:0000269|PubMed:2450679}.
-!- MISCELLANEOUS: Inhibitors targeting HIV-1 viral envelope proteins
are used as antiretroviral drugs. Attachment of virions to the
cell surface via non-specific interactions and CD4 binding can be
blocked by inhibitors that include cyanovirin-N,
cyclotriazadisulfonamide analogs, PRO 2000, TNX 355 and PRO 542.
In addition, BMS 806 can block CD4-induced conformational changes.
Env interactions with the coreceptor molecules can be targeted by
CCR5 antagonists including SCH-D, maraviroc (UK 427857) and
aplaviroc (GW 873140), and the CXCR4 antagonist AMD 070. Fusion of
viral and cellular membranes can be inhibited by peptides such as
enfuvirtide and tifuvirtide (T 1249). Resistance to inhibitors
associated with mutations in Env are observed. Most of the time,
single mutations confer only a modest reduction in drug
susceptibility. Combination of several mutations is usually
required to develop a high-level drug resistance.
{ECO:0000255|HAMAP-Rule:MF_04083}.
-!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M
(for Major), O (for Outlier), and N (for New, or Non-M, Non-O).
The vast majority of strains found worldwide belong to the group
M. Group O seems to be endemic to and largely confined to Cameroon
and neighboring countries in West Central Africa, where these
viruses represent a small minority of HIV-1 strains. The group N
is represented by a limited number of isolates from Cameroonian
persons. The group M is further subdivided in 9 clades or subtypes
(A to D, F to H, J and K). {ECO:0000255|HAMAP-Rule:MF_04083}.
-!- SIMILARITY: Belongs to the HIV-1 env protein family.
{ECO:0000255|HAMAP-Rule:MF_04083}.
-!- WEB RESOURCE: Name=BioAfrica HIV proteomics resource; Note=Env
entry;
URL="http://www.bioafrica.net/proteomics/ENVprot.html";
-!- WEB RESOURCE: Name=BioAfrica HIV proteomics resource; Note=gp120
entry;
URL="http://www.bioafrica.net/proteomics/ENV-GP120prot.html";
-!- WEB RESOURCE: Name=BioAfrica HIV proteomics resource; Note=gp41
entry;
URL="http://www.bioafrica.net/proteomics/ENV-GP41prot.html";
-!- WEB RESOURCE: Name=hivdb; Note=HIV drug resistance database;
URL="http://hivdb.stanford.edu";
-!- WEB RESOURCE: Name=BioAfrica: HIV bioinformatics in Africa;
URL="http://www.bioafrica.net/index.html";
-!- WEB RESOURCE: Name=HIV drug resistance mutations;
URL="https://www.iasusa.org/content/hiv-drug-resistance-mutations";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; K03455; AAB50262.1; -; Genomic_RNA.
EMBL; AF038399; AAB99976.1; -; Genomic_DNA.
EMBL; AF033819; AAC82596.1; -; Genomic_RNA.
RefSeq; NP_057856.1; NC_001802.1.
PDB; 1AIK; X-ray; 2.00 A; C=628-661, N=546-581.
PDB; 1DF4; X-ray; 1.45 A; A=546-579, A=628-655.
PDB; 1DF5; X-ray; 2.70 A; A=546-579, A=628-655.
PDB; 1DLB; X-ray; 2.00 A; A=546-579, A=628-655.
PDB; 1G9M; X-ray; 2.20 A; G=83-127, G=195-297, G=330-492.
PDB; 1GC1; X-ray; 2.50 A; G=83-127, G=195-297, G=330-396, G=410-492.
PDB; 1GZL; X-ray; 1.80 A; A/B=565-581, C/D=628-639.
PDB; 1K33; X-ray; 1.75 A; A=546-579, A=628-655.
PDB; 1K34; X-ray; 1.88 A; A=546-579, A=628-655.
PDB; 1MZI; NMR; -; A=659-671.
PDB; 1OPN; Model; -; G=156-492.
PDB; 1OPT; Model; -; G=156-492.
PDB; 1OPW; Model; -; G=156-492.
PDB; 1RZJ; X-ray; 2.20 A; G=195-492.
PDB; 2CMR; X-ray; 2.00 A; A=543-662.
PDB; 2ME1; NMR; -; A=657-683.
PDB; 2MG1; NMR; -; A=683-704.
PDB; 2MG2; NMR; -; A=675-693.
PDB; 2MG3; NMR; -; A=675-693.
PDB; 2NY7; X-ray; 2.30 A; G=83-492.
PDB; 2PV6; NMR; -; A=662-683.
PDB; 2XRA; X-ray; 2.30 A; A=543-662.
PDB; 3D0V; X-ray; 2.05 A; C=660-670.
PDB; 3DNL; EM; 20.00 A; A/D/G=90-124, B/E/H=198-297, B/E/H=330-396, C/F/I=410-492.
PDB; 3DNN; EM; 20.00 A; A/D/G=90-124, B/E/H=198-297, B/E/H=330-396, C/F/I=410-492.
PDB; 3DNO; EM; 20.00 A; A/D/G=90-124, B/E/H=198-297, B/E/H=330-396, C/F/I=410-492.
PDB; 3DRO; X-ray; 3.90 A; P=659-671.
PDB; 3IDX; X-ray; 2.50 A; G=83-492.
PDB; 3IDY; X-ray; 3.20 A; A/G=83-492.
PDB; 3J70; EM; -; D/P/U=31-500.
PDB; 3MNZ; X-ray; 1.80 A; P=653-671.
PDB; 3TYG; X-ray; 3.25 A; A=254-297, A=330-401.
PDB; 3VIE; X-ray; 1.80 A; A/C/E=546-581.
PDB; 4JPJ; X-ray; 2.50 A; A/B/C/D=254-399.
PDB; 4JPK; X-ray; 2.40 A; A=254-399.
PDB; 4YDV; X-ray; 2.70 A; P/Q=596-606.
PDB; 4ZTO; X-ray; 2.30 A; P/Q=430-444.
PDB; 5BN0; X-ray; 2.80 A; A/C/D=627-661, B/E/N=546-581.
PDB; 5C0R; X-ray; 3.19 A; A=546-577, A=628-654.
PDB; 5C0S; X-ray; 4.30 A; A=546-577, A=630-654.
PDB; 5CIL; X-ray; 1.81 A; P=671-683.
PDB; 5CIN; X-ray; 1.70 A; P=671-683.
PDB; 5CMU; X-ray; 2.11 A; A/B/C=546-635.
PDB; 5CMZ; X-ray; 2.57 A; A/C=546-590.
PDB; 5CN0; X-ray; 1.90 A; A=546-581.
PDB; 5DD0; X-ray; 2.49 A; P=660-670.
PDB; 5GHW; X-ray; 2.40 A; P=664-690.
PDB; 5H0N; X-ray; 2.80 A; A/C/E/G/I/K=536-581.
PDB; 5HFL; X-ray; 2.29 A; A/B/C/D/E/F=546-581.
PDB; 5HM1; X-ray; 2.96 A; D/E/F=582-596.
PDB; 5IVX; X-ray; 2.10 A; P=311-320.
PDB; 5KA5; X-ray; 1.80 A; A=543-582, A=625-661.
PDB; 5KA6; X-ray; 1.85 A; A/B/C=543-582, A/B/C=625-661.
PDB; 5X08; X-ray; 1.49 A; P=671-683.
PDBsum; 1AIK; -.
PDBsum; 1DF4; -.
PDBsum; 1DF5; -.
PDBsum; 1DLB; -.
PDBsum; 1G9M; -.
PDBsum; 1GC1; -.
PDBsum; 1GZL; -.
PDBsum; 1K33; -.
PDBsum; 1K34; -.
PDBsum; 1MZI; -.
PDBsum; 1OPN; -.
PDBsum; 1OPT; -.
PDBsum; 1OPW; -.
PDBsum; 1RZJ; -.
PDBsum; 2CMR; -.
PDBsum; 2ME1; -.
PDBsum; 2MG1; -.
PDBsum; 2MG2; -.
PDBsum; 2MG3; -.
PDBsum; 2NY7; -.
PDBsum; 2PV6; -.
PDBsum; 2XRA; -.
PDBsum; 3D0V; -.
PDBsum; 3DNL; -.
PDBsum; 3DNN; -.
PDBsum; 3DNO; -.
PDBsum; 3DRO; -.
PDBsum; 3IDX; -.
PDBsum; 3IDY; -.
PDBsum; 3J70; -.
PDBsum; 3MNZ; -.
PDBsum; 3TYG; -.
PDBsum; 3VIE; -.
PDBsum; 4JPJ; -.
PDBsum; 4JPK; -.
PDBsum; 4YDV; -.
PDBsum; 4ZTO; -.
PDBsum; 5BN0; -.
PDBsum; 5C0R; -.
PDBsum; 5C0S; -.
PDBsum; 5CIL; -.
PDBsum; 5CIN; -.
PDBsum; 5CMU; -.
PDBsum; 5CMZ; -.
PDBsum; 5CN0; -.
PDBsum; 5DD0; -.
PDBsum; 5GHW; -.
PDBsum; 5H0N; -.
PDBsum; 5HFL; -.
PDBsum; 5HM1; -.
PDBsum; 5IVX; -.
PDBsum; 5KA5; -.
PDBsum; 5KA6; -.
PDBsum; 5X08; -.
DisProt; DP00976; -.
ProteinModelPortal; P04578; -.
SMR; P04578; -.
BioGrid; 1205544; 155.
DIP; DIP-58525N; -.
IntAct; P04578; 155.
MINT; MINT-7968605; -.
BindingDB; P04578; -.
ChEMBL; CHEMBL3520; -.
TCDB; 1.G.16.1.3; the human immunodeficiency virus type 1 (hiv-1) fusion peptide (hiv-fp) family.
iPTMnet; P04578; -.
SwissPalm; P04578; -.
GeneID; 155971; -.
KEGG; vg:155971; -.
KO; K19287; -.
OrthoDB; VOG09000036; -.
Reactome; R-HSA-1462054; Alpha-defensins.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-171286; Synthesis and processing of ENV and VPU.
Reactome; R-HSA-173107; Binding and entry of HIV virion.
Reactome; R-HSA-175474; Assembly Of The HIV Virion.
Reactome; R-HSA-5621480; Dectin-2 family.
EvolutionaryTrace; P04578; -.
PRO; PR:P04578; -.
Proteomes; UP000002241; Genome.
Proteomes; UP000105453; Genome.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; TAS:Reactome.
GO; GO:0019012; C:virion; IDA:UniProtKB.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0090527; P:actin filament reorganization; IDA:UniProtKB.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IDA:UniProtKB.
GO; GO:0030260; P:entry into host cell; TAS:Reactome.
GO; GO:0030683; P:evasion or tolerance by virus of host immune response; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IDA:UniProtKB.
GO; GO:1903905; P:positive regulation of establishment of T cell polarity; IDA:UniProtKB.
GO; GO:1903908; P:positive regulation of plasma membrane raft polarization; IDA:UniProtKB.
GO; GO:1903911; P:positive regulation of receptor clustering; IDA:UniProtKB.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0019058; P:viral life cycle; TAS:Reactome.
GO; GO:0019082; P:viral protein processing; IDA:UniProtKB.
GO; GO:0019068; P:virion assembly; TAS:Reactome.
GO; GO:0019062; P:virion attachment to host cell; IDA:UniProtKB.
CDD; cd09909; HIV-1-like_HR1-HR2; 1.
Gene3D; 2.170.40.20; -; 2.
HAMAP; MF_04083; HIV_ENV; 1.
InterPro; IPR036377; Gp120_core_sf.
InterPro; IPR000328; GP41-like.
InterPro; IPR000777; HIV1_Gp120.
Pfam; PF00516; GP120; 1.
Pfam; PF00517; GP41; 1.
SUPFAM; SSF56502; SSF56502; 3.
1: Evidence at protein level;
3D-structure; AIDS; Apoptosis;
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 endosome; Host membrane;
Host-virus interaction; Lipoprotein; Membrane; Palmitate;
Reference proteome; Signal; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral envelope protein;
Viral immunoevasion; Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
SIGNAL 1 32 {ECO:0000255|HAMAP-Rule:MF_04083}.
CHAIN 33 856 Envelope glycoprotein gp160.
{ECO:0000255|HAMAP-Rule:MF_04083}.
/FTId=PRO_0000239240.
CHAIN 33 511 Surface protein gp120.
{ECO:0000255|HAMAP-Rule:MF_04083}.
/FTId=PRO_0000038427.
CHAIN 512 856 Transmembrane protein gp41.
{ECO:0000255|HAMAP-Rule:MF_04083}.
/FTId=PRO_0000038428.
TOPO_DOM 33 684 Extracellular. {ECO:0000255|HAMAP-
Rule:MF_04083}.
TRANSMEM 685 705 Helical. {ECO:0000255|HAMAP-
Rule:MF_04083}.
TOPO_DOM 706 856 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_04083}.
REGION 131 156 V1. {ECO:0000255|HAMAP-Rule:MF_04083}.
REGION 157 196 V2. {ECO:0000255|HAMAP-Rule:MF_04083}.
REGION 296 330 V3. {ECO:0000255|HAMAP-Rule:MF_04083}.
REGION 364 374 CD4-binding loop. {ECO:0000255|HAMAP-
Rule:MF_04083}.
REGION 385 418 V4. {ECO:0000255|HAMAP-Rule:MF_04083}.
REGION 461 471 V5.
REGION 463 471 V5. {ECO:0000255|HAMAP-Rule:MF_04083}.
REGION 512 532 Fusion peptide. {ECO:0000255|HAMAP-
Rule:MF_04083}.
REGION 574 592 Immunosuppression. {ECO:0000255|HAMAP-
Rule:MF_04083,
ECO:0000269|PubMed:23383108}.
REGION 662 683 MPER; binding to GalCer.
{ECO:0000255|HAMAP-Rule:MF_04083}.
COILED 633 667 {ECO:0000255|HAMAP-Rule:MF_04083}.
MOTIF 712 715 YXXL motif; contains endocytosis signal.
{ECO:0000255|HAMAP-Rule:MF_04083}.
MOTIF 855 856 Di-leucine internalization motif.
{ECO:0000255|HAMAP-Rule:MF_04083}.
SITE 511 512 Cleavage; by host furin.
{ECO:0000255|HAMAP-Rule:MF_04083}.
LIPID 764 764 S-palmitoyl cysteine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:7568235}.
LIPID 837 837 S-palmitoyl cysteine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:7568235}.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:19965434,
ECO:0000269|PubMed:26972002}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 156 156 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:26972002}.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:26972002}.
CARBOHYD 186 186 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:11188697,
ECO:0000269|PubMed:14981267,
ECO:0000269|PubMed:26972002,
ECO:0000269|PubMed:9641677}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 234 234 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:11188697,
ECO:0000269|PubMed:14981267,
ECO:0000269|PubMed:26972002}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 262 262 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:11188697,
ECO:0000269|PubMed:14981267,
ECO:0000269|PubMed:23539181,
ECO:0000269|PubMed:26972002,
ECO:0000269|PubMed:9641677}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:11188697,
ECO:0000269|PubMed:14981267,
ECO:0000269|PubMed:26972002,
ECO:0000269|PubMed:9641677}.
CARBOHYD 289 289 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:11188697,
ECO:0000269|PubMed:14981267,
ECO:0000269|PubMed:9641677}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:11188697,
ECO:0000269|PubMed:14981267,
ECO:0000269|PubMed:26972002,
ECO:0000269|PubMed:9641677}.
CARBOHYD 301 301 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 332 332 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:21998254,
ECO:0000269|PubMed:26972002,
ECO:0000269|PubMed:9641677}.
CARBOHYD 339 339 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:11188697,
ECO:0000269|PubMed:26972002,
ECO:0000269|PubMed:9641677}.
CARBOHYD 356 356 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000244|PDB:2NY7,
ECO:0000244|PDB:3IDX,
ECO:0000244|PDB:3IDY, ECO:0000255|HAMAP-
Rule:MF_04083,
ECO:0000269|PubMed:17301785,
ECO:0000269|PubMed:19965434}.
CARBOHYD 386 386 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:11188697,
ECO:0000269|PubMed:26972002,
ECO:0000269|PubMed:9641677}.
CARBOHYD 392 392 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:11188697,
ECO:0000269|PubMed:14981267,
ECO:0000269|PubMed:26972002,
ECO:0000269|PubMed:9641677}.
CARBOHYD 397 397 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 448 448 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:11188697,
ECO:0000269|PubMed:14981267,
ECO:0000269|PubMed:26972002,
ECO:0000269|PubMed:9641677}.
CARBOHYD 463 463 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:11188697,
ECO:0000269|PubMed:14981267}.
CARBOHYD 611 611 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:26972002}.
CARBOHYD 616 616 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 624 624 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 637 637 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:26972002}.
CARBOHYD 674 674 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
DISULFID 54 74 {ECO:0000255|HAMAP-Rule:MF_04083}.
DISULFID 119 205 {ECO:0000255|HAMAP-Rule:MF_04083}.
DISULFID 126 196 {ECO:0000255|HAMAP-Rule:MF_04083}.
DISULFID 131 157 {ECO:0000255|HAMAP-Rule:MF_04083}.
DISULFID 218 247 {ECO:0000255|HAMAP-Rule:MF_04083}.
DISULFID 228 239 {ECO:0000255|HAMAP-Rule:MF_04083}.
DISULFID 296 331 {ECO:0000255|HAMAP-Rule:MF_04083}.
DISULFID 378 445 {ECO:0000255|HAMAP-Rule:MF_04083}.
DISULFID 385 418 {ECO:0000255|HAMAP-Rule:MF_04083}.
DISULFID 598 604 {ECO:0000255|HAMAP-Rule:MF_04083}.
MUTAGEN 764 764 C->S: Complete loss of palmitoylation,
decreased association with host cell
membrane lipid rafts, decreased
incorporation onto virions and severe
reduction of infectivity; when associated
with S-837. {ECO:0000269|PubMed:7568235}.
MUTAGEN 837 837 C->S: Complete loss of palmitoylation,
decreased association with host cell
membrane lipid rafts, decreased
incorporation onto virions and severe
reduction of infectivity; when associated
with S-764. {ECO:0000269|PubMed:7568235}.
STRAND 40 42 {ECO:0000244|PDB:3J70}.
STRAND 45 47 {ECO:0000244|PDB:3J70}.
STRAND 53 55 {ECO:0000244|PDB:3J70}.
HELIX 65 72 {ECO:0000244|PDB:3J70}.
STRAND 84 93 {ECO:0000244|PDB:1G9M}.
TURN 95 98 {ECO:0000244|PDB:2NY7}.
HELIX 99 113 {ECO:0000244|PDB:1G9M}.
STRAND 119 123 {ECO:0000244|PDB:1G9M}.
STRAND 128 130 {ECO:0000244|PDB:3IDY}.
STRAND 139 144 {ECO:0000244|PDB:3J70}.
TURN 145 148 {ECO:0000244|PDB:3J70}.
STRAND 149 155 {ECO:0000244|PDB:3J70}.
STRAND 157 159 {ECO:0000244|PDB:3J70}.
STRAND 163 173 {ECO:0000244|PDB:3J70}.
STRAND 179 184 {ECO:0000244|PDB:3J70}.
STRAND 199 201 {ECO:0000244|PDB:1G9M}.
STRAND 210 212 {ECO:0000244|PDB:2NY7}.
STRAND 215 218 {ECO:0000244|PDB:3J70}.
STRAND 223 228 {ECO:0000244|PDB:1G9M}.
STRAND 235 247 {ECO:0000244|PDB:1G9M}.
STRAND 251 254 {ECO:0000244|PDB:2NY7}.
STRAND 256 258 {ECO:0000244|PDB:1G9M}.
STRAND 260 262 {ECO:0000244|PDB:1G9M}.
STRAND 267 269 {ECO:0000244|PDB:1G9M}.
STRAND 271 273 {ECO:0000244|PDB:1G9M}.
STRAND 277 279 {ECO:0000244|PDB:1GC1}.
STRAND 280 282 {ECO:0000244|PDB:3TYG}.
STRAND 284 297 {ECO:0000244|PDB:1G9M}.
TURN 298 300 {ECO:0000244|PDB:1RZJ}.
STRAND 330 334 {ECO:0000244|PDB:1G9M}.
HELIX 335 352 {ECO:0000244|PDB:1G9M}.
STRAND 359 361 {ECO:0000244|PDB:1G9M}.
HELIX 369 372 {ECO:0000244|PDB:1G9M}.
STRAND 374 378 {ECO:0000244|PDB:1G9M}.
STRAND 381 385 {ECO:0000244|PDB:1G9M}.
HELIX 388 390 {ECO:0000244|PDB:1G9M}.
STRAND 393 395 {ECO:0000244|PDB:1G9M}.
HELIX 398 410 {ECO:0000244|PDB:3J70}.
STRAND 413 417 {ECO:0000244|PDB:1G9M}.
STRAND 420 425 {ECO:0000244|PDB:1G9M}.
STRAND 427 430 {ECO:0000244|PDB:1G9M}.
STRAND 432 434 {ECO:0000244|PDB:1G9M}.
TURN 440 442 {ECO:0000244|PDB:3IDX}.
STRAND 444 456 {ECO:0000244|PDB:1G9M}.
STRAND 466 470 {ECO:0000244|PDB:1G9M}.
HELIX 475 483 {ECO:0000244|PDB:1G9M}.
STRAND 486 490 {ECO:0000244|PDB:1G9M}.
STRAND 495 497 {ECO:0000244|PDB:3J70}.
HELIX 549 577 {ECO:0000244|PDB:1DF4}.
HELIX 590 604 {ECO:0000244|PDB:2XRA}.
HELIX 629 650 {ECO:0000244|PDB:1DF4}.
HELIX 663 667 {ECO:0000244|PDB:2XRA}.
HELIX 672 674 {ECO:0000244|PDB:5CIN}.
HELIX 675 682 {ECO:0000244|PDB:5CIN}.
HELIX 683 688 {ECO:0000244|PDB:2XRA}.
HELIX 690 693 {ECO:0000244|PDB:2MG3}.
SEQUENCE 856 AA; 97213 MW; 6FAB16AF85107FE0 CRC64;
MRVKEKYQHL WRWGWRWGTM LLGMLMICSA TEKLWVTVYY GVPVWKEATT TLFCASDAKA
YDTEVHNVWA THACVPTDPN PQEVVLVNVT ENFNMWKNDM VEQMHEDIIS LWDQSLKPCV
KLTPLCVSLK CTDLKNDTNT NSSSGRMIME KGEIKNCSFN ISTSIRGKVQ KEYAFFYKLD
IIPIDNDTTS YKLTSCNTSV ITQACPKVSF EPIPIHYCAP AGFAILKCNN KTFNGTGPCT
NVSTVQCTHG IRPVVSTQLL LNGSLAEEEV VIRSVNFTDN AKTIIVQLNT SVEINCTRPN
NNTRKRIRIQ RGPGRAFVTI GKIGNMRQAH CNISRAKWNN TLKQIASKLR EQFGNNKTII
FKQSSGGDPE IVTHSFNCGG EFFYCNSTQL FNSTWFNSTW STEGSNNTEG SDTITLPCRI
KQIINMWQKV GKAMYAPPIS GQIRCSSNIT GLLLTRDGGN SNNESEIFRP GGGDMRDNWR
SELYKYKVVK IEPLGVAPTK AKRRVVQREK RAVGIGALFL GFLGAAGSTM GAASMTLTVQ
ARQLLSGIVQ QQNNLLRAIE AQQHLLQLTV WGIKQLQARI LAVERYLKDQ QLLGIWGCSG
KLICTTAVPW NASWSNKSLE QIWNHTTWME WDREINNYTS LIHSLIEESQ NQQEKNEQEL
LELDKWASLW NWFNITNWLW YIKLFIMIVG GLVGLRIVFA VLSIVNRVRQ GYSPLSFQTH
LPTPRGPDRP EGIEEEGGER DRDRSIRLVN GSLALIWDDL RSLCLFSYHR LRDLLLIVTR
IVELLGRRGW EALKYWWNLL QYWSQELKNS AVSLLNATAI AVAEGTDRVI EVVQGACRAI
RHIPRRIRQG LERILL


Related products :

Catalog number Product name Quantity
orb81719 HIV-1 gag p17-p24, gp41-gp120 protein HIV-1 gag p17-p24, gp41-gp120 is non-glycosylated polypeptide chain, containing sequence of HIV-1 immunodominant regions p17-p24, gp41-gp120. For research use onl 100
orb81701 HIV-1 gp41 His tag protein HIV-1 gp41 His tag Recombinant- is non-glycosylated 69 kDa polypeptide chain, containing the envelope glycoprotein 41 (subtype-B) gene of the HIV1 having 6X His tag chaperon 100
orb81702 HIV-1 gp41, MBP tag protein HIV-1 gp41 MBP tag Recombinant- is non-glycosylated 62 kDa polypeptide chain, containing the envelope glycoprotein 41 (subtype-B) gene of the HIV1 having maltose binding pr 100
orb81708 HIV-1 gp41,gp120 protein HIV-1 gp41-gp120 is non-glycosylated polypeptide chain fused to 6xHis Tag. For research use only. 100
orb81731 HIV Type-O gp41, MBP tag protein HIV Type-O gp41 MBP tag Recombinant- is non-glycosylated 60 kDa polypeptide chain, containing the envelope glycoprotein 41 (subtype-B) gene of the HIV having maltose b 100
E13651976 Human Envelope glycoprotein GP120 (Gp120) ELISA Kit 1
orb81687 HIV-1 Envelope (233) protein HIV-1 envelope is an E.coli-derived recombinant protein that composes all of the reported immunogenic determinants found in gp41 and small portion of gp120. The gene encod 100
HGP412-R Recombinant (E. coli) HIV-1 gp41 protein ( Contains all the immunogenic determinants found in gp41 and a small portion of gp120) (soluble) 100 ug
HGP412-R Recombinant (E. coli) HIV_1 gp41 protein (Contains all the immunogenic determinants found in gp41 and a small portion of gp120) (soluble) 100 ug
orb81688 HIV-1 Envelope His tag protein HIV-1 envelope His Tag Recombinant-is an E.coli-derived 74.18 kDa protein that contains immunodominant regions of gp120 C-terminus and gp41 N-terminus of the HIV1 and ha 100
HGP412-R Recombinant (E. coli) HIV-1 gp41 protein ( Contains all the immunogenic determinants found in gp41 and a small portion of gp120) (soluble) Species Reactivity: 100 ug Product tipe: Recomb. Protein
DEV301-1-2 HIV_1 gp120, env. peptide, spanning C_term. of gp120 & most of gp41, DEV_1 1 mg.
ACLHIV101B HIV_I Envelope (spanning C_terminus of gp120 and gp41), recombinant 500 µg.
Z5010240 Recombinant HIV_I Envelope (spanning C_terminus of gp120 and gp41) 500 µg
Z5010240 Recombinant HIV_I Envelope (spanning C_terminus of gp120 and gp41) 500 µg
ACLHIV101 HIV_I Envelope (spanning C_terminus of gp120 and gp41), recombinant 100 µg.
orb81728 HIV-1 Envelope conjugated to HIV-2 gp39 protein HIV-1,2 recombinant- E.coli derived recombinant 27 kDa protein contains the C- terminus of gp120 and most of gp41. The protein is conjugated to 23 amino 100
orb81719 HIV-1 gag p17-p24, gp41-gp120 protein Proteins 100
orb81708 HIV-1 gp41,gp120 protein Proteins 100
EIAAB06400 Cd8b,Cd8b1,Ly-3,Lymphocyte antigen 3,Lyt3,Lyt-3,Mouse,Mus musculus,T-cell membrane glycoprotein Ly-3,T-cell surface glycoprotein CD8 beta chain,T-cell surface glycoprotein Lyt-3
BRP1111 HIV-M2 (gp41+gp120+gp36+O) Recombinant Protein 100μg
BRP1112 HIV-M2 (gp41+gp120+gp36+O) Recombinant Protein 1mg
orb81714 HIV-1 gp120 CM protein HIV-1 gp120 CM Recombinant- is the external envelope protein, full-length 100-120 kDa, derived from the env. gene of HIV-1 and glycosylated with N-linked sugars and produced usi 2
orb81712 HIV-1 gp120 LAV protein HIV-1 gp120 LAV Recombinant- is the external envelope protein, full-length 100-120 kDa, derived from the env. gene of HIV-1 and glycosylated with N-linked sugars and produced u 2
orb81713 HIV-1 gp120 MN protein HIV-1 gp120 MN Recombinant- is the external envelope protein, full-length 100-120 kDa, derived from the env. gene of HIV-1 and glycosylated with N-linked sugars and produced usi 2


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur