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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)]

 W0IAM2_9HIV1            Unreviewed;       857 AA.
19-MAR-2014, integrated into UniProtKB/TrEMBL.
19-MAR-2014, sequence version 1.
16-JAN-2019, entry version 44.
RecName: Full=Envelope glycoprotein gp160 {ECO:0000256|HAMAP-Rule:MF_04083};
AltName: Full=Env polyprotein {ECO:0000256|HAMAP-Rule:MF_04083};
RecName: Full=Surface protein gp120 {ECO:0000256|HAMAP-Rule:MF_04083};
Short=SU {ECO:0000256|HAMAP-Rule:MF_04083};
AltName: Full=Glycoprotein 120 {ECO:0000256|HAMAP-Rule:MF_04083};
Short=gp120 {ECO:0000256|HAMAP-Rule:MF_04083};
RecName: Full=Transmembrane protein gp41 {ECO:0000256|HAMAP-Rule:MF_04083};
Short=TM {ECO:0000256|HAMAP-Rule:MF_04083};
AltName: Full=Glycoprotein 41 {ECO:0000256|HAMAP-Rule:MF_04083};
Short=gp41 {ECO:0000256|HAMAP-Rule:MF_04083};
Name=env {ECO:0000256|HAMAP-Rule:MF_04083,
Human immunodeficiency virus 1.
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
NCBI_TaxID=11676 {ECO:0000313|EMBL:AHF81782.1};
NCBI_TaxID=9606; Homo sapiens (Human).
[1] {ECO:0000313|EMBL:AHF81782.1}
STRAIN=888 {ECO:0000313|EMBL:AHF81782.1};
PubMed=24369910; DOI=10.1186/1742-4690-10-162;
Pena-Cruz V., Etemad B., Chatziandreou N., Nyein P.H., Stock S.,
Reynolds S.J., Laeyendecker O., Gray R.H., Serwadda D., Lee S.J.,
Quinn T.C., Sagar M.;
"HIV-1 envelope replication and ?4?7 utilization among newly infected
subjects and their corresponding heterosexual partners.";
Retrovirology 10:162-162(2013).
-!- 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:0000256|HAMAP-
-!- 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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_04083}.
-!- SUBCELLULAR LOCATION: Host cell membrane
{ECO:0000256|SAAS:SAAS01060237}; Peripheral membrane protein
{ECO:0000256|SAAS:SAAS01060237}. Host cell membrane
{ECO:0000256|SAAS:SAAS01060091}; Single-pass type I membrane
protein {ECO:0000256|SAAS:SAAS01060091}. Host endosome membrane
{ECO:0000256|SAAS:SAAS01060316}; Single-pass type I membrane
protein {ECO:0000256|SAAS:SAAS01060316}. Virion membrane
{ECO:0000256|SAAS:SAAS00796993}; Single-pass type I membrane
protein {ECO:0000256|SAAS:SAAS00796993}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000256|HAMAP-
Rule:MF_04083}; Peripheral membrane protein {ECO:0000256|HAMAP-
Rule:MF_04083}. Host cell membrane {ECO:0000256|HAMAP-
Rule:MF_04083}; Peripheral membrane protein {ECO:0000256|HAMAP-
Rule:MF_04083}. Host endosome membrane {ECO:0000256|HAMAP-
Rule:MF_04083}; Single-pass type I membrane protein
{ECO:0000256|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:0000256|HAMAP-Rule:MF_04083}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000256|HAMAP-
Rule:MF_04083}; Single-pass type I membrane protein
{ECO:0000256|HAMAP-Rule:MF_04083}. Host cell membrane
{ECO:0000256|HAMAP-Rule:MF_04083}; Single-pass type I membrane
protein {ECO:0000256|HAMAP-Rule:MF_04083}. Host endosome membrane
{ECO:0000256|HAMAP-Rule:MF_04083}; Single-pass type I membrane
protein {ECO:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_04083,
-!- DOMAIN: The CD4-binding region is targeted by the antibody b12.
-!- 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:0000256|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.
-!- 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.
-!- 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.
-!- 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.
-!- 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:0000256|HAMAP-Rule:MF_04083}.
-!- 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.
-!- SIMILARITY: Belongs to the HIV-1 env protein family.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04083,
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; KF986052; AHF81782.1; -; Genomic_DNA.
GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
GO; GO:0090527; P:actin filament reorganization; IEA:UniProtKB-UniRule.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-UniRule.
GO; GO:0030683; P:evasion or tolerance by virus of host immune response; IEA:UniProtKB-UniRule.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
GO; GO:1903905; P:positive regulation of establishment of T cell polarity; IEA:UniProtKB-UniRule.
GO; GO:1903908; P:positive regulation of plasma membrane raft polarization; IEA:UniProtKB-UniRule.
GO; GO:1903911; P:positive regulation of receptor clustering; IEA:UniProtKB-UniRule.
GO; GO:0019082; P:viral protein processing; IEA:UniProtKB-UniRule.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
CDD; cd09909; HIV-1-like_HR1-HR2; 1.
Gene3D;; -; 2.
HAMAP; MF_04083; HIV_ENV; 1.
InterPro; IPR036377; Gp120_core_sf.
InterPro; IPR037527; Gp160.
InterPro; IPR000328; GP41-like.
InterPro; IPR000777; HIV1_Gp120.
Pfam; PF00516; GP120; 1.
Pfam; PF00517; GP41; 1.
SUPFAM; SSF56502; SSF56502; 2.
3: Inferred from homology;
Apoptosis {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS01060203};
Clathrin-mediated endocytosis of virus by host {ECO:0000256|HAMAP-
Cleavage on pair of basic residues {ECO:0000256|HAMAP-Rule:MF_04083,
Coiled coil {ECO:0000256|HAMAP-Rule:MF_04083};
Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04083,
Fusion of virus membrane with host endosomal membrane
Fusion of virus membrane with host membrane {ECO:0000256|HAMAP-
Rule:MF_04083}; Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04083};
Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS01060118};
Host endosome {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS01060155};
Host membrane {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS01060118};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797747};
Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04083};
Membrane {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797734,
Palmitate {ECO:0000256|HAMAP-Rule:MF_04083};
Signal {ECO:0000256|HAMAP-Rule:MF_04083};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797734};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797734};
Viral attachment to host cell {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797747};
Viral envelope protein {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797156,
Viral immunoevasion {ECO:0000256|HAMAP-Rule:MF_04083};
Viral penetration into host cytoplasm {ECO:0000256|HAMAP-
Virion {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797156,
ECO:0000256|SAAS:SAAS00797747, ECO:0000313|EMBL:AHF81782.1};
Virus endocytosis by host {ECO:0000256|HAMAP-Rule:MF_04083};
Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04083,
ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797747}.
TRANSMEM 16 41 Helical. {ECO:0000256|RuleBase:RU363095}.
TRANSMEM 513 534 Helical. {ECO:0000256|RuleBase:RU363095}.
TRANSMEM 679 706 Helical. {ECO:0000256|RuleBase:RU363095}.
TOPO_DOM 707 857 Cytoplasmic. {ECO:0000256|HAMAP-
DOMAIN 33 512 GP120. {ECO:0000259|Pfam:PF00516}.
DOMAIN 531 721 GP41. {ECO:0000259|Pfam:PF00517}.
REGION 130 155 V1. {ECO:0000256|HAMAP-Rule:MF_04083}.
REGION 362 372 CD4-binding loop. {ECO:0000256|HAMAP-
REGION 462 472 V5. {ECO:0000256|HAMAP-Rule:MF_04083}.
REGION 513 533 Fusion peptide. {ECO:0000256|HAMAP-
REGION 575 593 Immunosuppression. {ECO:0000256|HAMAP-
REGION 663 684 MPER; binding to GalCer.
COILED 634 668 {ECO:0000256|HAMAP-Rule:MF_04083}.
MOTIF 713 716 YXXL motif; contains endocytosis signal.
SITE 512 513 Cleavage; by host furin.
LIPID 765 765 S-palmitoyl cysteine; by host.
DISULFID 53 73 {ECO:0000256|HAMAP-Rule:MF_04083}.
DISULFID 130 156 {ECO:0000256|HAMAP-Rule:MF_04083}.
DISULFID 219 248 {ECO:0000256|HAMAP-Rule:MF_04083}.
DISULFID 229 240 {ECO:0000256|HAMAP-Rule:MF_04083}.
DISULFID 599 605 {ECO:0000256|HAMAP-Rule:MF_04083}.
SEQUENCE 857 AA; 96967 MW; 5829C9728CD02B15 CRC64;

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