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

 ENV_HV1BR               Reviewed;         861 AA.
P03377; Q85582;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
30-AUG-2017, entry version 148.
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
BRU/LAI) (HIV-1).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Primate lentivirus group.
NCBI_TaxID=11686;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=2981635; DOI=10.1016/0092-8674(85)90303-4;
Wain-Hobson S., Sonigo P., Danos O., Cole S., Alizon M.;
"Nucleotide sequence of the AIDS virus, LAV.";
Cell 40:9-17(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=Clone pNL4-3;
Buckler C.E.;
Submitted (JUL-1989) to the EMBL/GenBank/DDBJ databases.
[3]
SEQUENCE REVISION TO 537 AND 538.
Strebel K.J., Martin M.A.;
Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
[4]
INTERACTION OF SURFACE PROTEIN GP120 WITH HUMAN CD209/DC-SIGN.
PubMed=1518869; DOI=10.1073/pnas.89.17.8356;
Curtis B.M., Scharnowske S., Watson A.J.;
"Sequence and expression of a membrane-associated C-type lectin that
exhibits CD4-independent binding of human immunodeficiency virus
envelope glycoprotein gp 120.";
Proc. Natl. Acad. Sci. U.S.A. 89:8356-8360(1992).
[5]
INTERACTION OF SURFACE PROTEIN GP120 WITH HOST CD209/DC-SIGN.
STRAIN=Clone pNL4-3;
PubMed=11312337; DOI=10.1128/JVI.75.10.4664-4672.2001;
Pohlmann S., Baribaud F., Lee B., Leslie G.J., Sanchez M.D.,
Hiebenthal-Millow K., Munch J., Kirchhoff F., Doms R.W.;
"DC-SIGN interactions with human immunodeficiency virus type 1 and 2
and simian immunodeficiency virus.";
J. Virol. 75:4664-4672(2001).
[6]
INTERACTION OF SURFACE PROTEIN GP120 WITH HUMAN CD209/DC-SIGN.
STRAIN=Clone pNL4-3;
PubMed=11825572; DOI=10.1016/S1074-7613(02)00259-5;
Kwon D.S., Gregorio G., Bitton N., Hendrickson W.A., Littman D.R.;
"DC-SIGN-mediated internalization of HIV is required for trans-
enhancement of T cell infection.";
Immunity 16:135-144(2002).
[7]
REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY P4HB/PDI.
PubMed=12218051; DOI=10.1074/jbc.M204547200;
Gallina A., Hanley T.M., Mandel R., Trahey M., Broder C.C.,
Viglianti G.A., Ryser H.J.;
"Inhibitors of protein-disulfide isomerase prevent cleavage of
disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1
entry.";
J. Biol. Chem. 277:50579-50588(2002).
[8]
PROTEOLYTIC PROCESSING OF POLYPROTEIN BY HOST FURIN.
STRAIN=Clone pNL4-3;
PubMed=15371436; DOI=10.1074/jbc.M403394200;
Kibler K.V., Miyazato A., Yedavalli V.S.R.K., Dayton A.I.,
Jacobs B.L., Dapolito G., Kim S.-J., Jeang K.-T.;
"Polyarginine inhibits gp160 processing by furin and suppresses
productive human immunodeficiency virus type 1 infection.";
J. Biol. Chem. 279:49055-49063(2004).
[9]
ROLE OF PALMITOYLATION, AND MUTAGENESIS OF CYS-769.
STRAIN=Clone pNL4-3;
PubMed=15113929; DOI=10.1128/JVI.78.10.5500-5506.2004;
Bhattacharya J., Peters P.J., Clapham P.R.;
"Human immunodeficiency virus type 1 envelope glycoproteins that lack
cytoplasmic domain cysteines: impact on association with membrane
lipid rafts and incorporation onto budding virus particles.";
J. Virol. 78:5500-5506(2004).
[10]
REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY HUMAN TXN.
STRAIN=Clone pNL4-3;
PubMed=16507315; DOI=10.1016/j.virol.2006.01.041;
Ou W., Silver J.;
"Role of protein disulfide isomerase and other thiol-reactive proteins
in HIV-1 envelope protein-mediated fusion.";
Virology 350:406-417(2006).
[11]
DISULFIDE BONDS.
PubMed=18653472; DOI=10.1091/mbc.E07-12-1282;
van Anken E., Sanders R.W., Liscaljet I.M., Land A., Bontjer I.,
Tillemans S., Nabatov A.A., Paxton W.A., Berkhout B., Braakman I.;
"Only five of 10 strictly conserved disulfide bonds are essential for
folding and eight for function of the HIV-1 envelope glycoprotein.";
Mol. Biol. Cell 19:4298-4309(2008).
[12]
INTERACTION OF GP120 WITH HUMAN ITGA4/ITGB7 HETERODIMER, AND
MUTAGENESIS OF 184-LEU-ASP-185.
STRAIN=Clone pNL4-3;
PubMed=18264102; DOI=10.1038/ni1566;
Arthos J., Cicala C., Martinelli E., Macleod K., Van Ryk D., Wei D.,
Xiao Z., Veenstra T.D., Conrad T.P., Lempicki R.A., McLaughlin S.,
Pascuccio M., Gopaul R., McNally J., Cruz C.C., Censoplano N.,
Chung E., Reitano K.N., Kottilil S., Goode D.J., Fauci A.S.;
"HIV-1 envelope protein binds to and signals through integrin
alpha4beta7, the gut mucosal homing receptor for peripheral T cells.";
Nat. Immunol. 9:301-309(2008).
[13]
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).
[14]
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).
[15]
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).
[16]
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).
[17]
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).
[18]
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).
[19]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 537-670.
PubMed=11026535; DOI=10.1016/S0968-0896(00)00155-3;
Zhou G., Ferrer M., Chopra R., Kapoor T.M., Strassmaier T.,
Weissenhorn W., Skehel J.J., Oprian D., Schreiber S.L., Harrison S.C.,
Wiley D.C.;
"The structure of an HIV-1 specific cell entry inhibitor in complex
with the HIV-1 gp41 trimeric core.";
Bioorg. Med. Chem. 8:2219-2227(2000).
[20]
STRUCTURE BY FTIR OF 517-539.
PubMed=11853678; DOI=10.1016/S0005-2736(01)00443-6;
Gordon L.M., Mobley P.W., Pilpa R., Sherman M.A., Waring A.J.;
"Conformational mapping of the N-terminal peptide of HIV-1 gp41 in
membrane environments using (13)C-enhanced Fourier transform infrared
spectroscopy.";
Biochim. Biophys. Acta 1559:96-120(2002).
[21]
STRUCTURE BY FTIR OF 517-539.
PubMed=15044732; DOI=10.1110/ps.03407704;
Gordon L.M., Mobley P.W., Lee W., Eskandari S., Kaznessis Y.N.,
Sherman M.A., Waring A.J.;
"Conformational mapping of the N-terminal peptide of HIV-1 gp41 in
lipid detergent and aqueous environments using 13C-enhanced Fourier
transform infrared spectroscopy.";
Protein Sci. 13:1012-1030(2004).
-!- 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}.
-!- 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}.
-!- 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}.
-!- 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:11312337, ECO:0000269|PubMed:11825572,
ECO:0000269|PubMed:1518869, ECO:0000269|PubMed:18264102}.
-!- 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}.
-!- 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}.
-!- 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}.
-!- 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}.
-!- DOMAIN: The CD4-binding region is targeted by the antibody b12.
{ECO:0000255|HAMAP-Rule:MF_04083}.
-!- 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:15113929}.
-!- 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:15371436,
ECO:0000269|PubMed:16507315}.
-!- 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=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";
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EMBL; K02013; AAB59751.1; -; Genomic_RNA.
EMBL; A04321; CAA00352.1; -; Unassigned_RNA.
EMBL; M19921; AAA44992.2; -; Genomic_RNA.
PIR; A03975; VCLJLV.
PDB; 1ENV; X-ray; 2.60 A; A=546-593, A=633-670.
PDB; 1ERF; IR; -; A=517-539.
PDB; 1FAV; X-ray; 3.00 A; A=546-595, C=639-670.
PDB; 1P5A; IR; -; A=517-539.
PDB; 1U6U; NMR; -; A=310-326.
PDB; 1U6V; NMR; -; A=310-326.
PDB; 2ZZO; X-ray; 2.20 A; C=633-666, N=551-586.
PDB; 3G9R; X-ray; 2.00 A; A/B/C/D/E/F=667-689.
PDB; 3MNW; X-ray; 2.20 A; P=657-676.
PDB; 3VGX; X-ray; 1.74 A; C=558-595, D=626-657.
PDB; 3VTP; X-ray; 1.90 A; C=555-595, D=631-666.
PDBsum; 1ENV; -.
PDBsum; 1ERF; -.
PDBsum; 1FAV; -.
PDBsum; 1P5A; -.
PDBsum; 1U6U; -.
PDBsum; 1U6V; -.
PDBsum; 2ZZO; -.
PDBsum; 3G9R; -.
PDBsum; 3MNW; -.
PDBsum; 3VGX; -.
PDBsum; 3VTP; -.
ProteinModelPortal; P03377; -.
SMR; P03377; -.
IntAct; P03377; 1.
BindingDB; P03377; -.
ChEMBL; CHEMBL5826; -.
OrthoDB; VOG09000036; -.
Reactome; R-HSA-5621480; Dectin-2 family.
EvolutionaryTrace; P03377; -.
Proteomes; UP000007692; Genome.
GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; ISS: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; ISS:UniProtKB.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; ISS:UniProtKB.
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; ISS:UniProtKB.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0019082; P:viral protein processing; ISS:UniProtKB.
GO; GO:0019062; P:virion attachment to host cell; ISS:UniProtKB.
CDD; cd09909; HIV-1-like_HR1-HR2; 1.
HAMAP; MF_04083; HIV_ENV; 1.
InterPro; IPR000328; GP41-like.
InterPro; IPR000777; HIV1_GP160.
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 33 861 Envelope glycoprotein gp160.
{ECO:0000255|HAMAP-Rule:MF_04083}.
/FTId=PRO_0000239474.
CHAIN 33 516 Surface protein gp120.
{ECO:0000255|HAMAP-Rule:MF_04083}.
/FTId=PRO_0000038388.
CHAIN 517 861 Transmembrane protein gp41.
{ECO:0000255|HAMAP-Rule:MF_04083}.
/FTId=PRO_0000038389.
TOPO_DOM 33 689 Extracellular. {ECO:0000255|HAMAP-
Rule:MF_04083}.
TRANSMEM 690 710 Helical. {ECO:0000255|HAMAP-
Rule:MF_04083}.
TOPO_DOM 711 861 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_04083}.
REGION 131 161 V1. {ECO:0000255|HAMAP-Rule:MF_04083}.
REGION 162 201 V2. {ECO:0000255|HAMAP-Rule:MF_04083}.
REGION 301 335 V3. {ECO:0000255|HAMAP-Rule:MF_04083}.
REGION 369 379 CD4-binding loop. {ECO:0000255|HAMAP-
Rule:MF_04083}.
REGION 390 423 V4. {ECO:0000255|HAMAP-Rule:MF_04083}.
REGION 466 476 V5.
REGION 468 476 V5. {ECO:0000255|HAMAP-Rule:MF_04083}.
REGION 517 537 Fusion peptide. {ECO:0000255|HAMAP-
Rule:MF_04083}.
REGION 579 597 Immunosuppression. {ECO:0000255|HAMAP-
Rule:MF_04083}.
REGION 667 688 MPER; binding to GalCer.
{ECO:0000255|HAMAP-Rule:MF_04083}.
COILED 638 672 {ECO:0000255|HAMAP-Rule:MF_04083}.
MOTIF 184 186 Putative binding site to alpha-4/beta-7
integrin.
MOTIF 717 720 YXXL motif; contains endocytosis signal.
{ECO:0000255|HAMAP-Rule:MF_04083}.
MOTIF 860 861 Di-leucine internalization motif.
{ECO:0000255|HAMAP-Rule:MF_04083}.
COMPBIAS 465 468 Poly-Asn.
SITE 516 517 Cleavage; by host furin.
{ECO:0000255|HAMAP-Rule:MF_04083}.
LIPID 769 769 S-palmitoyl cysteine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
LIPID 842 842 S-palmitoyl cysteine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 88 88 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
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 146 146 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 165 165 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 191 191 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 202 202 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 239 239 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 267 267 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 281 281 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 294 294 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 306 306 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 337 337 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 344 344 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 361 361 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 391 391 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 397 397 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 402 402 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 411 411 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 453 453 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 468 468 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 616 616 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 621 621 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 630 630 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 642 642 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
CARBOHYD 679 679 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04083}.
DISULFID 54 74 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:18653472}.
DISULFID 119 210 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:18653472}.
DISULFID 126 201 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:18653472}.
DISULFID 131 162 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:18653472}.
DISULFID 223 252 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:18653472}.
DISULFID 233 244 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:18653472}.
DISULFID 301 336 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:18653472}.
DISULFID 383 450 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:18653472}.
DISULFID 390 423 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:18653472}.
DISULFID 603 609 {ECO:0000255|HAMAP-Rule:MF_04083,
ECO:0000269|PubMed:18653472}.
VARIANT 135 137 GNA -> KND (in strain: Clone pNL4-3).
VARIANT 143 147 Missing (in strain: Clone pNL4-3).
VARIANT 151 153 EMM -> RMI (in strain: Clone pNL4-3).
VARIANT 172 172 G -> D (in strain: Clone pNL4-3).
VARIANT 187 187 I -> V (in strain: Clone pNL4-3).
VARIANT 192 193 Missing (in strain: Clone pNL4-3).
VARIANT 197 199 TLT -> RLI (in strain: Clone pNL4-3).
VARIANT 274 274 E -> D (in strain: Clone pNL4-3).
VARIANT 295 295 Q -> T (in strain: Clone pNL4-3).
VARIANT 538 538 R -> A (in strain: Clone pNL4-3).
VARIANT 552 552 G -> D (in strain: Clone pNL4-3).
VARIANT 689 689 I -> L (in strain: Clone pNL4-3).
VARIANT 728 728 T -> I (in strain: Clone pNL4-3).
VARIANT 818 818 S -> N (in strain: Clone pNL4-3).
VARIANT 838 842 VQGAC -> LQAAY (in strain: Clone pNL4-3).
MUTAGEN 184 185 LD->AA: Partial loss of CD4-independent
binding. {ECO:0000269|PubMed:18264102}.
MUTAGEN 769 769 C->F: Almost no effect on virions
assembly and infectivity.
{ECO:0000269|PubMed:15113929}.
STRAND 311 314 {ECO:0000244|PDB:1U6U}.
STRAND 322 325 {ECO:0000244|PDB:1U6U}.
HELIX 559 594 {ECO:0000244|PDB:3VGX}.
HELIX 633 655 {ECO:0000244|PDB:3VGX}.
HELIX 659 674 {ECO:0000244|PDB:3MNW}.
SEQUENCE 861 AA; 97488 MW; 04DE2B4D4E4FD63A CRC64;
MRVKEKYQHL WRWGWKWGTM LLGILMICSA TEKLWVTVYY GVPVWKEATT TLFCASDAKA
YDTEVHNVWA THACVPTDPN PQEVVLVNVT ENFNMWKNDM VEQMHEDIIS LWDQSLKPCV
KLTPLCVSLK CTDLGNATNT NSSNTNSSSG EMMMEKGEIK NCSFNISTSI RGKVQKEYAF
FYKLDIIPID NDTTSYTLTS CNTSVITQAC PKVSFEPIPI HYCAPAGFAI LKCNNKTFNG
TGPCTNVSTV QCTHGIRPVV STQLLLNGSL AEEEVVIRSA NFTDNAKTII VQLNQSVEIN
CTRPNNNTRK SIRIQRGPGR AFVTIGKIGN MRQAHCNISR AKWNATLKQI ASKLREQFGN
NKTIIFKQSS GGDPEIVTHS FNCGGEFFYC NSTQLFNSTW FNSTWSTEGS NNTEGSDTIT
LPCRIKQFIN MWQEVGKAMY APPISGQIRC SSNITGLLLT RDGGNNNNGS EIFRPGGGDM
RDNWRSELYK YKVVKIEPLG VAPTKAKRRV VQREKRAVGI GALFLGFLGA AGSTMGARSM
TLTVQARQLL SGIVQQQNNL LRAIEAQQHL LQLTVWGIKQ LQARILAVER YLKDQQLLGI
WGCSGKLICT TAVPWNASWS NKSLEQIWNN MTWMEWDREI NNYTSLIHSL IEESQNQQEK
NEQELLELDK WASLWNWFNI TNWLWYIKIF IMIVGGLVGL RIVFAVLSIV NRVRQGYSPL
SFQTHLPTPR GPDRPEGIEE EGGERDRDRS IRLVNGSLAL IWDDLRSLCL FSYHRLRDLL
LIVTRIVELL GRRGWEALKY WWNLLQYWSQ ELKNSAVSLL NATAIAVAEG TDRVIEVVQG
ACRAIRHIPR RIRQGLERIL L


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