ID   W6A110_9PLVG            Unreviewed;       854 AA.
AC   W6A110;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   05-JUN-2019, entry version 42.
DE   RecName: Full=Envelope glycoprotein gp160 {ECO:0000256|HAMAP-Rule:MF_04083};
DE   AltName: Full=Env polyprotein {ECO:0000256|HAMAP-Rule:MF_04083};
DE   Contains:
DE     RecName: Full=Surface protein gp120 {ECO:0000256|HAMAP-Rule:MF_04083};
DE              Short=SU {ECO:0000256|HAMAP-Rule:MF_04083};
DE     AltName: Full=Glycoprotein 120 {ECO:0000256|HAMAP-Rule:MF_04083};
DE              Short=gp120 {ECO:0000256|HAMAP-Rule:MF_04083};
DE   Contains:
DE     RecName: Full=Transmembrane protein gp41 {ECO:0000256|HAMAP-Rule:MF_04083};
DE              Short=TM {ECO:0000256|HAMAP-Rule:MF_04083};
DE     AltName: Full=Glycoprotein 41 {ECO:0000256|HAMAP-Rule:MF_04083};
DE              Short=gp41 {ECO:0000256|HAMAP-Rule:MF_04083};
GN   Name=env {ECO:0000256|HAMAP-Rule:MF_04083,
GN   ECO:0000313|EMBL:AHI49131.1};
OS   Simian-Human immunodeficiency virus.
OC   Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus;
OC   Primate lentivirus group; unclassified Primate lentivirus group.
OX   NCBI_TaxID=57667 {ECO:0000313|EMBL:AHI49131.1};
RN   [1] {ECO:0000313|EMBL:AHI49131.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ba-L {ECO:0000313|EMBL:AHI49131.1};
RX   PubMed=23966410; DOI=10.1128/JVI.01361-13;
RA   Klein K., Veazey R.S., Warrier R., Hraber P., Doyle-Meyers L.A.,
RA   Buffa V., Liao H.X., Haynes B.F., Shaw G.M., Shattock R.J.;
RT   "Neutralizing IgG at the portal of infection mediates protection
RT   against vaginal simian/human immunodeficiency virus challenge.";
RL   J. Virol. 87:11604-11616(2013).
CC   -!- FUNCTION: Envelope glycoprotein gp160: Oligomerizes in the host
CC       endoplasmic reticulum into predominantly trimers. In a second
CC       time, gp160 transits in the host Golgi, where glycosylation is
CC       completed. The precursor is then proteolytically cleaved in the
CC       trans-Golgi and thereby activated by cellular furin or furin-like
CC       proteases to produce gp120 and gp41. {ECO:0000256|HAMAP-
CC       Rule:MF_04083}.
CC   -!- FUNCTION: Surface protein gp120: Attaches the virus to the host
CC       lymphoid cell by binding to the primary receptor CD4. This
CC       interaction induces a structural rearrangement creating a high
CC       affinity binding site for a chemokine coreceptor like CXCR4 and/or
CC       CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR,
CC       which are respectively found on dendritic cells (DCs), and on
CC       endothelial cells of liver sinusoids and lymph node sinuses. These
CC       interactions allow capture of viral particles at mucosal surfaces
CC       by these cells and subsequent transmission to permissive cells.
CC       HIV subverts the migration properties of dendritic cells to gain
CC       access to CD4+ T-cells in lymph nodes. Virus transmission to
CC       permissive T-cells occurs either in trans (without DCs infection,
CC       through viral capture and transmission), or in cis (following DCs
CC       productive infection, through the usual CD4-gp120 interaction),
CC       thereby inducing a robust infection. In trans infection, bound
CC       virions remain infectious over days and it is proposed that they
CC       are not degraded, but protected in non-lysosomal acidic organelles
CC       within the DCs close to the cell membrane thus contributing to the
CC       viral infectious potential during DCs' migration from the
CC       periphery to the lymphoid tissues. On arrival at lymphoid tissues,
CC       intact virions recycle back to DCs' cell surface allowing virus
CC       transmission to CD4+ T-cells. {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- FUNCTION: Transmembrane protein gp41: Acts as a class I viral
CC       fusion protein. Under the current model, the protein has at least
CC       3 conformational states: pre-fusion native state, pre-hairpin
CC       intermediate state, and post-fusion hairpin state. During fusion
CC       of viral and target intracellular membranes, the coiled coil
CC       regions (heptad repeats) assume a trimer-of-hairpins structure,
CC       positioning the fusion peptide in close proximity to the C-
CC       terminal region of the ectodomain. The formation of this structure
CC       appears to drive apposition and subsequent fusion of viral and
CC       target cell membranes. Complete fusion occurs in host cell
CC       endosomes and is dynamin-dependent, however some lipid transfer
CC       might occur at the plasma membrane. The virus undergoes clathrin-
CC       dependent internalization long before endosomal fusion, thus
CC       minimizing the surface exposure of conserved viral epitopes during
CC       fusion and reducing the efficacy of inhibitors targeting these
CC       epitopes. Membranes fusion leads to delivery of the nucleocapsid
CC       into the cytoplasm. {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- SUBUNIT: The mature envelope protein (Env) consists of a
CC       homotrimer of non-covalently associated gp120-gp41 heterodimers.
CC       The resulting complex protrudes from the virus surface as a spike.
CC       There seems to be as few as 10 spikes on the average virion.
CC       Surface protein gp120 interacts with host CD4, CCR5 and CXCR4.
CC       Gp120 also interacts with the C-type lectins CD209/DC-SIGN and
CC       CLEC4M/DC-SIGNR (collectively referred to as DC-SIGN(R)). Gp120
CC       and gp41 interact with GalCer. Gp120 interacts with host
CC       ITGA4/ITGB7 complex; on CD4+ T-cells, this interaction results in
CC       rapid activation of integrin ITGAL/LFA-1, which facilitates
CC       efficient cell-to-cell spreading of HIV-1. Gp120 interacts with
CC       cell-associated heparan sulfate; this interaction increases virus
CC       infectivity on permissive cells and may be involved in infection
CC       of CD4- cells. {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- SUBCELLULAR LOCATION: Host cell membrane
CC       {ECO:0000256|SAAS:SAAS01060237}; Peripheral membrane protein
CC       {ECO:0000256|SAAS:SAAS01060237}. Host cell membrane
CC       {ECO:0000256|SAAS:SAAS01060091}; Single-pass type I membrane
CC       protein {ECO:0000256|SAAS:SAAS01060091}. Host endosome membrane
CC       {ECO:0000256|SAAS:SAAS01060316}; Single-pass type I membrane
CC       protein {ECO:0000256|SAAS:SAAS01060316}. Virion membrane
CC       {ECO:0000256|SAAS:SAAS00796993}; Single-pass type I membrane
CC       protein {ECO:0000256|SAAS:SAAS00796993}.
CC   -!- SUBCELLULAR LOCATION: Surface protein gp120: Virion membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04083}; Peripheral membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_04083}. Host cell membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04083}; Peripheral membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_04083}. Host endosome membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04083}; Single-pass type I membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_04083}. Note=The surface
CC       protein is not anchored to the viral envelope, but associates with
CC       the extravirion surface through its binding to TM. It is probably
CC       concentrated at the site of budding and incorporated into the
CC       virions possibly by contacts between the cytoplasmic tail of Env
CC       and the N-terminus of Gag. {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- SUBCELLULAR LOCATION: Transmembrane protein gp41: Virion membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04083}; Single-pass type I membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_04083}. Host cell membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04083}; Single-pass type I membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_04083}. Host endosome membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04083}; Single-pass type I membrane
CC       protein {ECO:0000256|HAMAP-Rule:MF_04083}. Note=It is probably
CC       concentrated at the site of budding and incorporated into the
CC       virions possibly by contacts between the cytoplasmic tail of Env
CC       and the N-terminus of Gag. {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- DOMAIN: Some of the most genetically diverse regions of the viral
CC       genome are present in Env. They are called variable regions 1
CC       through 5 (V1 through V5). Coreceptor usage of gp120 is determined
CC       mainly by the primary structure of the third variable region (V3)
CC       in the outer domain of gp120. The sequence of V3 determines which
CC       coreceptor, CCR5 and/or CXCR4 (corresponding to R5/macrophage,
CC       X4/T cell and R5X4/T cell and macrophage tropism), is used to
CC       trigger the fusion potential of the Env complex, and hence which
CC       cells the virus can infect. Binding to CCR5 involves a region
CC       adjacent in addition to V3. {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- DOMAIN: The 17 amino acids long immunosuppressive region is
CC       present in many retroviral envelope proteins. Synthetic peptides
CC       derived from this relatively conserved sequence inhibit immune
CC       function in vitro and in vivo. {ECO:0000256|HAMAP-Rule:MF_04083,
CC       ECO:0000256|RuleBase:RU363095}.
CC   -!- DOMAIN: The CD4-binding region is targeted by the antibody b12.
CC       {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- DOMAIN: The YXXL motif is involved in determining the exact site
CC       of viral release at the surface of infected mononuclear cells and
CC       promotes endocytosis. YXXL and di-leucine endocytosis motifs
CC       interact directly or indirectly with the clathrin adapter
CC       complexes, opperate independently, and their activities are not
CC       additive. {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- DOMAIN: The membrane proximal external region (MPER) present in
CC       gp41 is a tryptophan-rich region recognized by the antibodies 2F5,
CC       Z13, and 4E10. MPER seems to play a role in fusion.
CC       {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- PTM: Highly glycosylated by host. The high number of glycan on the
CC       protein is reffered to as 'glycan shield' because it contributes
CC       to hide protein sequence from adaptive immune system.
CC       {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- PTM: Palmitoylation of the transmembrane protein and of Env
CC       polyprotein (prior to its proteolytic cleavage) is essential for
CC       their association with host cell membrane lipid rafts.
CC       Palmitoylation is therefore required for envelope trafficking to
CC       classical lipid rafts, but not for viral replication.
CC       {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC       Envelope glycoproteins are synthesized as a inactive precursor
CC       that is heavily N-glycosylated and processed likely by host cell
CC       furin in the Golgi to yield the mature SU and TM proteins. The
CC       cleavage site between SU and TM requires the minimal sequence
CC       [KR]-X-[KR]-R. About 2 of the 9 disulfide bonds of gp41 are
CC       reduced by P4HB/PDI, following binding to CD4 receptor.
CC       {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M
CC       (for Major), O (for Outlier), and N (for New, or Non-M, Non-O).
CC       The vast majority of strains found worldwide belong to the group
CC       M. Group O seems to be endemic to and largely confined to Cameroon
CC       and neighboring countries in West Central Africa, where these
CC       viruses represent a small minority of HIV-1 strains. The group N
CC       is represented by a limited number of isolates from Cameroonian
CC       persons. The group M is further subdivided in 9 clades or subtypes
CC       (A to D, F to H, J and K). {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- MISCELLANEOUS: Inhibitors targeting HIV-1 viral envelope proteins
CC       are used as antiretroviral drugs. Attachment of virions to the
CC       cell surface via non-specific interactions and CD4 binding can be
CC       blocked by inhibitors that include cyanovirin-N,
CC       cyclotriazadisulfonamide analogs, PRO 2000, TNX 355 and PRO 542.
CC       In addition, BMS 806 can block CD4-induced conformational changes.
CC       Env interactions with the coreceptor molecules can be targeted by
CC       CCR5 antagonists including SCH-D, maraviroc (UK 427857) and
CC       aplaviroc (GW 873140), and the CXCR4 antagonist AMD 070. Fusion of
CC       viral and cellular membranes can be inhibited by peptides such as
CC       enfuvirtide and tifuvirtide (T 1249). Resistance to inhibitors
CC       associated with mutations in Env are observed. Most of the time,
CC       single mutations confer only a modest reduction in drug
CC       susceptibility. Combination of several mutations is usually
CC       required to develop a high-level drug resistance.
CC       {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- SIMILARITY: Belongs to the HIV-1 env protein family.
CC       {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04083,
CC       ECO:0000256|RuleBase:RU363095}.
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DR   EMBL; KF734097; AHI49117.1; -; Other_DNA.
DR   EMBL; KF734099; AHI49118.1; -; Other_DNA.
DR   EMBL; KF734100; AHI49119.1; -; Other_DNA.
DR   EMBL; KF734103; AHI49120.1; -; Other_DNA.
DR   EMBL; KF734104; AHI49121.1; -; Other_DNA.
DR   EMBL; KF734106; AHI49123.1; -; Other_DNA.
DR   EMBL; KF734109; AHI49125.1; -; Other_DNA.
DR   EMBL; KF734110; AHI49126.1; -; Other_DNA.
DR   EMBL; KF734111; AHI49127.1; -; Other_DNA.
DR   EMBL; KF734116; AHI49130.1; -; Other_DNA.
DR   EMBL; KF734117; AHI49131.1; -; Other_DNA.
DR   EMBL; KF734118; AHI49132.1; -; Other_DNA.
DR   EMBL; KF734120; AHI49134.1; -; Other_DNA.
DR   EMBL; KF734150; AHI49160.1; -; Other_DNA.
DR   EMBL; KF734151; AHI49161.1; -; Other_DNA.
DR   EMBL; KF734152; AHI49162.1; -; Other_DNA.
DR   EMBL; KF734155; AHI49165.1; -; Other_DNA.
DR   EMBL; KF734156; AHI49166.1; -; Other_DNA.
DR   EMBL; KF734157; AHI49167.1; -; Other_DNA.
DR   EMBL; KF734158; AHI49168.1; -; Other_DNA.
DR   EMBL; KF734159; AHI49169.1; -; Other_DNA.
DR   EMBL; KF734163; AHI49172.1; -; Other_DNA.
DR   EMBL; KF734166; AHI49175.1; -; Other_DNA.
DR   EMBL; KF734167; AHI49176.1; -; Other_DNA.
DR   EMBL; KF734169; AHI49178.1; -; Other_DNA.
DR   EMBL; KF734174; AHI49182.1; -; Other_DNA.
DR   EMBL; KF734177; AHI49185.1; -; Other_DNA.
DR   EMBL; KF734178; AHI49186.1; -; Other_DNA.
DR   EMBL; KF734179; AHI49187.1; -; Other_DNA.
DR   EMBL; KF734181; AHI49188.1; -; Other_DNA.
DR   EMBL; KF734183; AHI49189.1; -; Other_DNA.
DR   EMBL; KF734184; AHI49190.1; -; Other_DNA.
DR   EMBL; KF734324; AHI49309.1; -; Other_DNA.
DR   EMBL; KF734325; AHI49310.1; -; Other_DNA.
DR   EMBL; KF734331; AHI49315.1; -; Other_DNA.
DR   EMBL; KF734335; AHI49317.1; -; Other_DNA.
DR   EMBL; KF734337; AHI49319.1; -; Other_DNA.
DR   EMBL; KF734344; AHI49326.1; -; Other_DNA.
DR   EMBL; KF734354; AHI49335.1; -; Other_DNA.
DR   EMBL; KF734356; AHI49337.1; -; Other_DNA.
DR   EMBL; KF734357; AHI49338.1; -; Other_DNA.
DR   EMBL; KF734358; AHI49339.1; -; Other_DNA.
DR   EMBL; KF734361; AHI49342.1; -; Other_DNA.
DR   EMBL; KF734366; AHI49347.1; -; Other_DNA.
DR   EMBL; KF734367; AHI49348.1; -; Other_DNA.
DR   EMBL; KF734368; AHI49349.1; -; Other_DNA.
DR   EMBL; KF734369; AHI49350.1; -; Other_DNA.
DR   EMBL; KF734372; AHI49352.1; -; Other_DNA.
DR   EMBL; KF734374; AHI49354.1; -; Other_DNA.
DR   GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0090527; P:actin filament reorganization; IEA:UniProtKB-UniRule.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-UniRule.
DR   GO; GO:0030683; P:evasion or tolerance by virus of host immune response; IEA:UniProtKB-UniRule.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:1903905; P:positive regulation of establishment of T cell polarity; IEA:UniProtKB-UniRule.
DR   GO; GO:1903908; P:positive regulation of plasma membrane raft polarization; IEA:UniProtKB-UniRule.
DR   GO; GO:1903911; P:positive regulation of receptor clustering; IEA:UniProtKB-UniRule.
DR   GO; GO:0019082; P:viral protein processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
DR   CDD; cd09909; HIV-1-like_HR1-HR2; 1.
DR   Gene3D; 2.170.40.20; -; 2.
DR   HAMAP; MF_04083; HIV_ENV; 1.
DR   InterPro; IPR036377; Gp120_core_sf.
DR   InterPro; IPR037527; Gp160.
DR   InterPro; IPR000328; GP41-like.
DR   InterPro; IPR000777; HIV1_Gp120.
DR   Pfam; PF00516; GP120; 1.
DR   Pfam; PF00517; GP41; 1.
DR   SUPFAM; SSF56502; SSF56502; 2.
PE   3: Inferred from homology;
KW   Apoptosis {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS01060203};
KW   Clathrin-mediated endocytosis of virus by host {ECO:0000256|HAMAP-
KW   Rule:MF_04083};
KW   Cleavage on pair of basic residues {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095};
KW   Coiled coil {ECO:0000256|HAMAP-Rule:MF_04083};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|SAAS:SAAS01050261};
KW   Fusion of virus membrane with host endosomal membrane
KW   {ECO:0000256|HAMAP-Rule:MF_04083};
KW   Fusion of virus membrane with host membrane {ECO:0000256|HAMAP-
KW   Rule:MF_04083, ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS01050351};
KW   Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04083};
KW   Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS01060118};
KW   Host endosome {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS01060155};
KW   Host membrane {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS01060308};
KW   Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797036};
KW   Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04083};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797370};
KW   Palmitate {ECO:0000256|HAMAP-Rule:MF_04083};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_04083};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797262};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797734};
KW   Viral attachment to host cell {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797747};
KW   Viral envelope protein {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797156,
KW   ECO:0000313|EMBL:AHI49131.1};
KW   Viral immunoevasion {ECO:0000256|HAMAP-Rule:MF_04083};
KW   Viral penetration into host cytoplasm {ECO:0000256|HAMAP-
KW   Rule:MF_04083, ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS01050355};
KW   Virion {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00796948};
KW   Virus endocytosis by host {ECO:0000256|HAMAP-Rule:MF_04083};
KW   Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797206}.
FT   TRANSMEM    510    533       Helical. {ECO:0000256|RuleBase:RU363095}.
FT   TRANSMEM    676    697       Helical. {ECO:0000256|RuleBase:RU363095}.
FT   TOPO_DOM    704    854       Cytoplasmic. {ECO:0000256|HAMAP-Rule:
FT                                MF_04083}.
FT   DOMAIN       33    509       GP120. {ECO:0000259|Pfam:PF00516}.
FT   DOMAIN      528    717       GP41. {ECO:0000259|Pfam:PF00517}.
FT   REGION      366    376       CD4-binding loop. {ECO:0000256|HAMAP-
FT                                Rule:MF_04083}.
FT   REGION      459    469       V5. {ECO:0000256|HAMAP-Rule:MF_04083}.
FT   REGION      510    530       Fusion peptide. {ECO:0000256|HAMAP-Rule:
FT                                MF_04083}.
FT   REGION      572    590       Immunosuppression. {ECO:0000256|HAMAP-
FT                                Rule:MF_04083}.
FT   REGION      660    681       MPER; binding to GalCer.
FT                                {ECO:0000256|HAMAP-Rule:MF_04083}.
FT   REGION      717    741       Disordered. {ECO:0000256|MobiDB-lite:
FT                                W6A110}.
FT   COILED      631    665       {ECO:0000256|HAMAP-Rule:MF_04083}.
FT   MOTIF       710    713       YXXL motif; contains endocytosis signal.
FT                                {ECO:0000256|HAMAP-Rule:MF_04083}.
FT   MOTIF       853    854       Di-leucine internalization motif.
FT                                {ECO:0000256|HAMAP-Rule:MF_04083}.
FT   COMPBIAS    727    741       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                W6A110}.
FT   SITE        509    510       Cleavage; by host furin.
FT                                {ECO:0000256|HAMAP-Rule:MF_04083}.
FT   DISULFID     53     73       {ECO:0000256|HAMAP-Rule:MF_04083}.
FT   DISULFID    222    251       {ECO:0000256|HAMAP-Rule:MF_04083}.
FT   DISULFID    232    243       {ECO:0000256|HAMAP-Rule:MF_04083}.
FT   DISULFID    596    602       {ECO:0000256|HAMAP-Rule:MF_04083}.
SQ   SEQUENCE   854 AA;  96972 MW;  F4A7CB534239E931 CRC64;
     MRVTEIRKSY QHWWRWGIML LGILMICNAE EKLWVTVYYG VPVWKEATTT LFCASDAKAY
     DTEEHNVWAT HACVPTDPNP QEVELKNVTE NFNMWKNNMV EQMHEDIISL WDQSLKPCVK
     LTPLCVTLNC TDLRNATNGN DTNTTSSSRG MVGGGEMKNC SFNITTNIRG KVQKEYALFY
     KLDIAPIDNN SNNRYRLISC NTSVITQACP KVSFEPIPIH YCAPAGFAIL KCKDKKFNGK
     GPCTNVSTVQ CTHGIRPVVS TQLLLNGSLA EEEVVIRSAN FADNAKIIIV QLNESVEINC
     TRPNNNTRKS IHIGPGRAFY TTGEIIGDIR QAHCNLSRAK WNDTLNKIVI KLREQFGNKT
     IVFKHSSGGD PEIVTHSFNC GGEFFYCDST QLFNSTWNVT EESNNTVENN TITLPCRIKQ
     IINMWQEVGR AMYAPPIRGQ IRCSSNITGL LLTRDGGPED NKTEVFRPGG GDMRDNWRSE
     LYKYKVVKIE PLGVAPTKAK RRVVQREKRA VGIGAVFLGF LGAAGSTMGA AAMTLTVQAR
     LLLSGIVQQQ NNLLRAIEAQ QHLLQLTVWG VKQLQARVLA VERYLRDQQL LGIWGCSGKL
     ICTTAVPWNA SWSNKSLNKI WDNMTWIEWD REINNYTSII YSLIEESQNQ QEKNEQELLE
     LDKWASLWNW FDITKWLWYI KIFIMIVGGL IGLRIVFSVL SIVNRVRQGY SPLSFQTHLP
     ASRGPDRPGG IEEEGGERDR DRSGPLVNGF LALIWVDLRS LFLFSYHRLR DLLLIVIRIV
     ELLGRRGWEV LKYWWNLLQY WSQELKNSAV SLLNATAVAV AEGTDRVIEV LQRAVRAILH
     IPRRIRQGLE RALL
//