ID   Q6TCP8_9HIV1            Unreviewed;       841 AA.
AC   Q6TCP8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 2.
DT   27-MAR-2024, entry version 142.
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:AAR09542.2};
OS   Human immunodeficiency virus 1.
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:AAR09542.2};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:AAR09542.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ZM109F.PB4 {ECO:0000313|EMBL:AAR09542.2};
RX   PubMed=15044802; DOI=10.1126/science.1093137;
RA   Derdeyn C.A., Decker J.M., Bibollet-Ruche F., Mokili J.L., Muldoon M.,
RA   Denham S.A., Heil M.L., Kasolo F., Musonda R., Hahn B.H., Shaw G.M.,
RA   Korber B.T., Allen S., Hunter E.;
RT   "Envelope-constrained neutralization-sensitive HIV-1 after heterosexual
RT   transmission.";
RL   Science 303:2019-2022(2004).
RN   [2] {ECO:0000313|EMBL:AAR09542.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ZM109F.PB4 {ECO:0000313|EMBL:AAR09542.2};
RA   Ge S., Xie B., Chen S.;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0007829|PDB:3U2S}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 125-244, GLYCOSYLATION AT
RP   ASN-149, AND DISULFIDE BONDS.
RX   PubMed=22113616; DOI=10.1038/nature10696;
RA   McLellan J.S., Pancera M., Carrico C., Gorman J., Julien J.P., Khayat R.,
RA   Louder R., Pejchal R., Sastry M., Dai K., O'Dell S., Patel N.,
RA   Shahzad-ul-Hussan S., Yang Y., Zhang B., Zhou T., Zhu J., Boyington J.C.,
RA   Chuang G.Y., Diwanji D., Georgiev I., Kwon Y.D., Lee D., Louder M.K.,
RA   Moquin S., Schmidt S.D., Yang Z.Y., Bonsignori M., Crump J.A., Kapiga S.H.,
RA   Sam N.E., Haynes B.F., Burton D.R., Koff W.C., Walker L.M., Phogat S.,
RA   Wyatt R., Orwenyo J., Wang L.X., Arthos J., Bewley C.A., Mascola J.R.,
RA   Nabel G.J., Schief W.R., Ward A.B., Wilson I.A., Kwong P.D.;
RT   "Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody
RT   PG9.";
RL   Nature 480:336-343(2011).
RN   [4] {ECO:0007829|PDB:4DQO}
RP   X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 125-244, GLYCOSYLATION AT ASN-149
RP   AND ASN-162, AND DISULFIDE BONDS.
RX   PubMed=23708607; DOI=10.1038/nsmb.2600;
RA   Pancera M., Shahzad-Ul-Hussan S., Doria-Rose N.A., McLellan J.S.,
RA   Bailer R.T., Dai K., Loesgen S., Louder M.K., Staupe R.P., Yang Y.,
RA   Zhang B., Parks R., Eudailey J., Lloyd K.E., Blinn J., Alam S.M.,
RA   Haynes B.F., Amin M.N., Wang L.X., Burton D.R., Koff W.C., Nabel G.J.,
RA   Mascola J.R., Bewley C.A., Kwong P.D.;
RT   "Structural basis for diverse N-glycan recognition by HIV-1-neutralizing
RT   V1-V2-directed antibody PG16.";
RL   Nat. Struct. Mol. Biol. 20:804-813(2013).
RN   [5] {ECO:0007829|PDB:4YWG}
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 125-244, AND DISULFIDE BONDS.
RX   PubMed=26018158; DOI=10.1128/JVI.00754-15;
RA   Pan R., Gorny M.K., Zolla-Pazner S., Kong X.P.;
RT   "The V1V2 Region of HIV-1 gp120 Forms a Five-Stranded Beta Barrel.";
RL   J. Virol. 89:8003-8010(2015).
CC   -!- FUNCTION: Envelope glycoprotein gp160: Oligomerizes in the host
CC       endoplasmic reticulum into predominantly trimers. In a second time,
CC       gp160 transits in the host Golgi, where glycosylation is completed. The
CC       precursor is then proteolytically cleaved in the trans-Golgi and
CC       thereby activated by cellular furin or furin-like proteases to produce
CC       gp120 and gp41. {ECO:0000256|HAMAP-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 interaction
CC       induces a structural rearrangement creating a high affinity binding
CC       site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a
CC       ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively
CC       found on dendritic cells (DCs), and on endothelial cells of liver
CC       sinusoids and lymph node sinuses. These interactions allow capture of
CC       viral particles at mucosal surfaces by these cells and subsequent
CC       transmission to permissive cells. HIV subverts the migration properties
CC       of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus
CC       transmission to permissive T-cells occurs either in trans (without DCs
CC       infection, through viral capture and transmission), or in cis
CC       (following DCs productive infection, through the usual CD4-gp120
CC       interaction), thereby inducing a robust infection. In trans infection,
CC       bound 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 periphery to
CC       the lymphoid tissues. On arrival at lymphoid tissues, intact virions
CC       recycle back to DCs' cell surface allowing virus transmission to CD4+
CC       T-cells. {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- FUNCTION: Transmembrane protein gp41: Acts as a class I viral fusion
CC       protein. Under the current model, the protein has at least 3
CC       conformational states: pre-fusion native state, pre-hairpin
CC       intermediate state, and post-fusion hairpin state. During fusion of
CC       viral and target intracellular membranes, the coiled coil regions
CC       (heptad repeats) assume a trimer-of-hairpins structure, positioning the
CC       fusion peptide in close proximity to the C-terminal region of the
CC       ectodomain. The formation of this structure appears to drive apposition
CC       and subsequent fusion of viral and target cell membranes. Complete
CC       fusion occurs in host cell endosomes and is dynamin-dependent, however
CC       some lipid transfer might occur at the plasma membrane. The virus
CC       undergoes clathrin-dependent internalization long before endosomal
CC       fusion, thus minimizing the surface exposure of conserved viral
CC       epitopes during fusion and reducing the efficacy of inhibitors
CC       targeting these epitopes. Membranes fusion leads to delivery of the
CC       nucleocapsid into the cytoplasm. {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- SUBUNIT: The mature envelope protein (Env) consists of a homotrimer of
CC       non-covalently associated gp120-gp41 heterodimers. The resulting
CC       complex protrudes from the virus surface as a spike. There seems to be
CC       as few as 10 spikes on the average virion. Surface protein gp120
CC       interacts with host CD4, CCR5 and CXCR4. Gp120 also interacts with the
CC       C-type lectins CD209/DC-SIGN and CLEC4M/DC-SIGNR (collectively referred
CC       to as DC-SIGN(R)). Gp120 and gp41 interact with GalCer. Gp120 interacts
CC       with host ITGA4/ITGB7 complex; on CD4+ T-cells, this interaction
CC       results in rapid activation of integrin ITGAL/LFA-1, which facilitates
CC       efficient cell-to-cell spreading of HIV-1. Gp120 interacts with cell-
CC       associated heparan sulfate; this interaction increases virus
CC       infectivity on permissive cells and may be involved in infection of
CC       CD4- cells. {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cell
CC       membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane
CC       protein {ECO:0000256|ARBA:ARBA00004251}. Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004481}. Endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004530}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004530}. Host cell membrane
CC       {ECO:0000256|ARBA:ARBA00004505}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004505}. Host cell membrane
CC       {ECO:0000256|ARBA:ARBA00004402}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004402}. Host endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004433}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004433}. Host endosome membrane
CC       {ECO:0000256|ARBA:ARBA00004578}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004578}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004479}. Virion membrane
CC       {ECO:0000256|ARBA:ARBA00004650}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004650}. Virion membrane
CC       {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein
CC       {ECO:0000256|ARBA:ARBA00004563}.
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 protein
CC       {ECO:0000256|HAMAP-Rule:MF_04083}. Note=The surface protein is not
CC       anchored to the viral envelope, but associates with the extravirion
CC       surface through its binding to TM. It is probably concentrated at the
CC       site of budding and incorporated into the virions possibly by contacts
CC       between the cytoplasmic tail of Env and the N-terminus of Gag.
CC       {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 protein
CC       {ECO:0000256|HAMAP-Rule:MF_04083}. Host cell membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_04083}. Host endosome membrane
CC       {ECO:0000256|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein
CC       {ECO:0000256|HAMAP-Rule:MF_04083}. Note=It is probably concentrated at
CC       the site of budding and incorporated into the virions possibly by
CC       contacts between the cytoplasmic tail of Env and the N-terminus of Gag.
CC       {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 through 5
CC       (V1 through V5). Coreceptor usage of gp120 is determined mainly by the
CC       primary structure of the third variable region (V3) in the outer domain
CC       of gp120. The sequence of V3 determines which coreceptor, CCR5 and/or
CC       CXCR4 (corresponding to R5/macrophage, X4/T cell and R5X4/T cell and
CC       macrophage tropism), is used to trigger the fusion potential of the Env
CC       complex, and hence which cells the virus can infect. Binding to CCR5
CC       involves a region adjacent in addition to V3. {ECO:0000256|HAMAP-
CC       Rule:MF_04083}.
CC   -!- DOMAIN: The 17 amino acids long immunosuppressive region is present in
CC       many retroviral envelope proteins. Synthetic peptides derived from this
CC       relatively conserved sequence inhibit immune function in vitro and in
CC       vivo. {ECO:0000256|HAMAP-Rule:MF_04083, 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 of
CC       viral release at the surface of infected mononuclear cells and promotes
CC       endocytosis. YXXL and di-leucine endocytosis motifs interact directly
CC       or indirectly with the clathrin adapter complexes, opperate
CC       independently, and their activities are not additive.
CC       {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- DOMAIN: The membrane proximal external region (MPER) present in gp41 is
CC       a tryptophan-rich region recognized by the antibodies 2F5, Z13, and
CC       4E10. MPER seems to play a role in fusion. {ECO:0000256|HAMAP-
CC       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 to
CC       hide protein sequence from adaptive immune system. {ECO:0000256|HAMAP-
CC       Rule:MF_04083}.
CC   -!- PTM: Palmitoylation of the transmembrane protein and of Env polyprotein
CC       (prior to its proteolytic cleavage) is essential for their association
CC       with host cell membrane lipid rafts. Palmitoylation is therefore
CC       required for envelope trafficking to classical lipid rafts, but not for
CC       viral replication. {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 that is
CC       heavily N-glycosylated and processed likely by host cell furin in the
CC       Golgi to yield the mature SU and TM proteins. The cleavage site between
CC       SU and TM requires the minimal sequence [KR]-X-[KR]-R. About 2 of the 9
CC       disulfide bonds of gp41 are reduced by P4HB/PDI, following binding to
CC       CD4 receptor. {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M (for
CC       Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast
CC       majority of strains found worldwide belong to the group M. Group O
CC       seems to be endemic to and largely confined to Cameroon and neighboring
CC       countries in West Central Africa, where these viruses represent a small
CC       minority of HIV-1 strains. The group N is represented by a limited
CC       number of isolates from Cameroonian persons. The group M is further
CC       subdivided in 9 clades or subtypes (A to D, F to H, J and K).
CC       {ECO:0000256|HAMAP-Rule:MF_04083}.
CC   -!- MISCELLANEOUS: Inhibitors targeting HIV-1 viral envelope proteins are
CC       used as antiretroviral drugs. Attachment of virions to the cell surface
CC       via non-specific interactions and CD4 binding can be blocked by
CC       inhibitors that include cyanovirin-N, cyclotriazadisulfonamide analogs,
CC       PRO 2000, TNX 355 and PRO 542. In addition, BMS 806 can block CD4-
CC       induced conformational changes. Env interactions with the coreceptor
CC       molecules can be targeted by CCR5 antagonists including SCH-D,
CC       maraviroc (UK 427857) and aplaviroc (GW 873140), and the CXCR4
CC       antagonist AMD 070. Fusion of viral and cellular membranes can be
CC       inhibited by peptides such as enfuvirtide and tifuvirtide (T 1249).
CC       Resistance to inhibitors associated with mutations in Env are observed.
CC       Most of the time, single mutations confer only a modest reduction in
CC       drug susceptibility. Combination of several mutations is usually
CC       required to develop a high-level drug resistance. {ECO:0000256|HAMAP-
CC       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 of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_04083,
CC       ECO:0000256|RuleBase:RU363095}.
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DR   EMBL; AY424138; AAR09542.2; -; Genomic_DNA.
DR   PDB; 3U2S; X-ray; 1.80 A; C/G=125-216.
DR   PDB; 4DQO; X-ray; 2.44 A; C=125-216.
DR   PDB; 4YWG; X-ray; 3.00 A; G/Q=125-216.
DR   PDBsum; 3U2S; -.
DR   PDBsum; 4DQO; -.
DR   PDBsum; 4YWG; -.
DR   SMR; Q6TCP8; -.
DR   GlyCosmos; Q6TCP8; 3 sites, No reported glycans.
DR   ABCD; Q6TCP8; 2 sequenced antibodies.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0075512; P:clathrin-dependent endocytosis of virus by host cell; 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   GO; GO:0019049; P:virus-mediated perturbation of host defense response; IEA:UniProtKB-UniRule.
DR   CDD; cd09909; HIV-1-like_HR1-HR2; 1.
DR   Gene3D; 1.10.287.210; -; 1.
DR   Gene3D; 2.170.40.20; Human immunodeficiency virus 1, Gp160, envelope glycoprotein; 2.
DR   Gene3D; 1.20.5.490; Single helix bin; 1.
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; 2.
DR   Pfam; PF00517; GP41; 1.
DR   SUPFAM; SSF56502; gp120 core; 2.
DR   SUPFAM; SSF58069; Virus ectodomain; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3U2S, ECO:0007829|PDB:4DQO};
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703, ECO:0000256|HAMAP-Rule:MF_04083};
KW   Clathrin-mediated endocytosis of virus by host
KW   {ECO:0000256|ARBA:ARBA00022570, ECO:0000256|HAMAP-Rule:MF_04083};
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685,
KW   ECO:0000256|HAMAP-Rule:MF_04083};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|HAMAP-
KW   Rule:MF_04083};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW   Rule:MF_04083};
KW   Fusion of virus membrane with host endosomal membrane
KW   {ECO:0000256|ARBA:ARBA00022510, 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   Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04083};
KW   Host cell membrane {ECO:0000256|ARBA:ARBA00022511, ECO:0000256|HAMAP-
KW   Rule:MF_04083};
KW   Host endosome {ECO:0000256|ARBA:ARBA00023046, ECO:0000256|HAMAP-
KW   Rule:MF_04083};
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870, ECO:0000256|HAMAP-
KW   Rule:MF_04083};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, ECO:0000256|HAMAP-
KW   Rule:MF_04083};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW   Rule:MF_04083};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_04083};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_04083};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_04083};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095};
KW   Viral attachment to host cell {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095};
KW   Viral envelope protein {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095};
KW   Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280, ECO:0000256|HAMAP-
KW   Rule:MF_04083};
KW   Viral penetration into host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095};
KW   Virion {ECO:0000256|HAMAP-Rule:MF_04083, ECO:0000256|RuleBase:RU363095};
KW   Virus endocytosis by host {ECO:0000256|ARBA:ARBA00022890,
KW   ECO:0000256|HAMAP-Rule:MF_04083};
KW   Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04083,
KW   ECO:0000256|RuleBase:RU363095}.
FT   CHAIN           32..841
FT                   /note="Envelope glycoprotein gp160"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04083"
FT                   /id="PRO_5023358867"
FT   CHAIN           490..841
FT                   /note="Transmembrane protein gp41"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04083"
FT                   /id="PRO_5023358868"
FT   TRANSMEM        13..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363095"
FT   TRANSMEM        490..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363095"
FT   TRANSMEM        656..683
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363095"
FT   TOPO_DOM        684..841
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04083"
FT   DOMAIN          33..132
FT                   /note="Human immunodeficiency virus 1 envelope glycoprotein
FT                   Gp120"
FT                   /evidence="ECO:0000259|Pfam:PF00516"
FT   DOMAIN          142..489
FT                   /note="Human immunodeficiency virus 1 envelope glycoprotein
FT                   Gp120"
FT                   /evidence="ECO:0000259|Pfam:PF00516"
FT   DOMAIN          508..698
FT                   /note="Retroviral envelope protein GP41-like"
FT                   /evidence="ECO:0000259|Pfam:PF00517"
FT   REGION          355..365
FT                   /note="CD4-binding loop"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04083"
FT   REGION          490..510
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04083"
FT   REGION          552..570
FT                   /note="Immunosuppression"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04083"
FT   REGION          640..661
FT                   /note="MPER; binding to GalCer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04083"
FT   COILED          611..645
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04083"
FT   MOTIF           690..693
FT                   /note="YXXL motif; contains endocytosis signal"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04083"
FT   SITE            489..490
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04083"
FT   LIPID           742
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04083"
FT   CARBOHYD        129
FT                   /note="N-acetyl-D-glucosamine 1"
FT                   /evidence="ECO:0007829|PDB:4YWG"
FT   CARBOHYD        129
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007829|PDB:4YWG"
FT   CARBOHYD        149
FT                   /note="N-acetyl-D-glucosamine 2"
FT                   /evidence="ECO:0007829|PDB:4YWG"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007829|PDB:4YWG"
FT   CARBOHYD        162
FT                   /note="N-acetyl-D-glucosamine 3"
FT                   /evidence="ECO:0007829|PDB:3U2S, ECO:0007829|PDB:4YWG"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0007829|PDB:3U2S, ECO:0007829|PDB:4YWG"
FT   DISULFID        53..73
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04083"
FT   DISULFID        125..190
FT                   /evidence="ECO:0007829|PDB:3U2S, ECO:0007829|PDB:4DQO"
FT   DISULFID        130..146
FT                   /evidence="ECO:0007829|PDB:3U2S, ECO:0007829|PDB:4DQO"
FT   DISULFID        212..241
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04083"
FT   DISULFID        222..233
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04083"
FT   DISULFID        576..582
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04083"
SQ   SEQUENCE   841 AA;  95156 MW;  1175F660B06DD6D8 CRC64;
     MRVKGILRNC QQWWIWGILG FWMLMICNVV GNLWVTVYYG VPVWKEAKTT LFCASDAKSY
     EREVHNVWAT HACVPTDPDP QELVMANVTE NFNMWKNDMV DQMHEDIISL WDQSLKPCVK
     LTPLCVTLNC TSPAAHNESE TRVKHCSFNI TTDVKDRKQK VNATFYDLDI VPLSSSDNSS
     NSSLYRLISC NTSTITQACP KVSFDPIPIH YCAPAGYAIL KCNNKTFSGK GPCSNVSTVQ
     CTHGIRPVVS TQLLLNGSLA EEEIVIRSEN LTDNAKTIIV HLNKSVEIEC IRPGNNTRKS
     IRLGPGQTFY ATGDVIGDIR KAYCKINGSE WNETLTKVSE KLKEYFNKTI RFAQHSGGDL
     EVTTHSFNCR GEFFYCNTSE LFNSNATESN ITLPCRIKQI INMWQGVGRA MYAPPIRGEI
     KCTSNITGLL LTRDGGNNNN STEEIFRPEG GNMRDNWRSE LYKYKVVEIK PLGIAPTEAK
     RRVVQREKRA VGIGAVFLGF LGAAGSTMGA ASITLTVQAR QLLSGIVQQQ SNLLRAIEAQ
     QHLLQLTVWG IKQLQARVLA IERYLQDQQL LGIWGCSGKL ICTTAVPWNS SWSNKSKEEI
     WGNMTWMQWD KEVSNYTFTI YQLLEESQYQ QEQNEKELLA LNKWNDLWSW FNITNWLWYI
     KIFIMIVGGL IGLRIIFAVL SIVNRVRQGY SPLSFQTLTP NPGGPDRLGR IEGEGGEQDK
     NRSIRLVNGF LALIWDDLWS LCRFSYHLLR DFILIVARAV ELLGRSSLKG LQRGWEALKY
     LGNLMQYWGL ELKRSAINLL DTTAVAVAEG TDRIIELAQG IYRAICNIPR RIRQGFEAAL
     Q
//