ENV_HV1B1
ID ENV_HV1B1 Reviewed; 856 AA.
AC P03375; P03376;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Envelope glycoprotein gp160 {ECO:0000255|HAMAP-Rule:MF_04083};
DE AltName: Full=Env polyprotein {ECO:0000255|HAMAP-Rule:MF_04083};
DE Contains:
DE RecName: Full=Surface protein gp120 {ECO:0000255|HAMAP-Rule:MF_04083};
DE Short=SU {ECO:0000255|HAMAP-Rule:MF_04083};
DE AltName: Full=Glycoprotein 120 {ECO:0000255|HAMAP-Rule:MF_04083};
DE Short=gp120 {ECO:0000255|HAMAP-Rule:MF_04083};
DE Contains:
DE RecName: Full=Transmembrane protein gp41 {ECO:0000255|HAMAP-Rule:MF_04083};
DE Short=TM {ECO:0000255|HAMAP-Rule:MF_04083};
DE AltName: Full=Glycoprotein 41 {ECO:0000255|HAMAP-Rule:MF_04083};
DE Short=gp41 {ECO:0000255|HAMAP-Rule:MF_04083};
DE Flags: Precursor;
GN Name=env {ECO:0000255|HAMAP-Rule:MF_04083};
OS Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
OS (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11678;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2578615; DOI=10.1038/313277a0;
RA Ratner L., Haseltine W.A., Patarca R., Livak K.J., Starcich B.R.,
RA Josephs S.F., Doran E.R., Rafalski J.A., Whitehorn E.A., Baumeister K.,
RA Ivanoff L., Petteway S.R. Jr., Pearson M.L., Lautenberger J.A., Papas T.S.,
RA Ghrayeb J., Chang N.T., Gallo R.C., Wong-Staal F.;
RT "Complete nucleotide sequence of the AIDS virus, HTLV-III.";
RL Nature 313:277-284(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate PV22;
RX PubMed=2982104; DOI=10.1038/313450a0;
RA Muesing M.A., Smith D.H., Cabradilla C.D., Benton C.V., Lasky L.A.,
RA Capon D.J.;
RT "Nucleic acid structure and expression of the human AIDS/lymphadenopathy
RT retrovirus.";
RL Nature 313:450-458(1985).
RN [3]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=2450679; DOI=10.1016/0092-8674(88)90487-4;
RA McCune J.M., Rabin L.B., Feinberg M.B., Lieberman M., Kosek J.C.,
RA Reyes G.R., Weissman I.L.;
RT "Endoproteolytic cleavage of gp160 is required for the activation of human
RT immunodeficiency virus.";
RL Cell 53:55-67(1988).
RN [4]
RP PROTEIN SEQUENCE OF C-TERMINUS, DISULFIDE BONDS, GLYCOSYLATION AT ASN-88;
RP ASN-136; ASN-141; ASN-156; ASN-160; ASN-186; ASN-197; ASN-230; ASN-234;
RP ASN-241; ASN-262; ASN-276; ASN-289; ASN-295; ASN-301; ASN-332; ASN-339;
RP ASN-356; ASN-386; ASN-392; ASN-397; ASN-406; ASN-448 AND ASN-463, AND
RP STRUCTURE OF CARBOHYDRATES.
RX PubMed=2355006; DOI=10.1016/s0021-9258(18)86956-3;
RA Leonard C.K., Spellman M.W., Riddle L., Harris R.J., Thomas J.N.,
RA Gregory T.J.;
RT "Assignment of intrachain disulfide bonds and characterization of potential
RT glycosylation sites of the type 1 recombinant human immunodeficiency virus
RT envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells.";
RL J. Biol. Chem. 265:10373-10382(1990).
RN [5]
RP INTERACTION OF GLYCOPROTEIN 120 WITH HOST CD4.
RX PubMed=2214026; DOI=10.1128/jvi.64.11.5585-5593.1990;
RA Crise B., Buonocore L., Rose J.K.;
RT "CD4 is retained in the endoplasmic reticulum by the human immunodeficiency
RT virus type 1 glycoprotein precursor.";
RL J. Virol. 64:5585-5593(1990).
RN [6]
RP INTERACTION OF TRANSMEMBRANE PROTEIN GP41 WITH GALACTOSYL CERAMIDE.
RX PubMed=11342649; DOI=10.4049/jimmunol.166.10.6257;
RA Alfsen A., Iniguez P., Bouguyon E., Bomsel M.;
RT "Secretory IgA specific for a conserved epitope on gp41 envelope
RT glycoprotein inhibits epithelial transcytosis of HIV-1.";
RL J. Immunol. 166:6257-6265(2001).
RN [7]
RP REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY P4HB/PDI.
RX PubMed=11181151; DOI=10.1086/318823;
RA Fenouillet E., Barbouche R., Courageot J., Miquelis R.;
RT "The catalytic activity of protein disulfide isomerase is involved in human
RT immunodeficiency virus envelope-mediated membrane fusion after CD4 cell
RT binding.";
RL J. Infect. Dis. 183:744-752(2001).
RN [8]
RP REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY P4HB/PDI.
RX PubMed=12218052; DOI=10.1074/jbc.m205467200;
RA Barbouche R., Miquelis R., Jones I.M., Fenouillet E.;
RT "Protein-disulfide isomerase-mediated reduction of two disulfide bonds of
RT HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for
RT fusion.";
RL J. Biol. Chem. 278:3131-3136(2003).
RN [9]
RP REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY P4HB/PDI.
RX PubMed=14592831; DOI=10.1182/blood-2003-05-1390;
RA Markovic I., Stantchev T.S., Fields K.H., Tiffany L.J., Tomic M.,
RA Weiss C.D., Broder C.C., Strebel K., Clouse K.A.;
RT "Thiol/disulfide exchange is a prerequisite for CXCR4-tropic HIV-1
RT envelope-mediated T-cell fusion during viral entry.";
RL Blood 103:1586-1594(2004).
RN [10]
RP REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY P4HB/PDI.
RX PubMed=15644496; DOI=10.1124/mol.104.008276;
RA Barbouche R., Lortat-Jacob H., Jones I.M., Fenouillet E.;
RT "Glycosaminoglycans and protein disulfide isomerase-mediated reduction of
RT HIV Env.";
RL Mol. Pharmacol. 67:1111-1118(2005).
RN [11]
RP REVIEW.
RX PubMed=12974773; DOI=10.1034/j.1600-0463.2003.11107803.x;
RA Geijtenbeek T.B., van Kooyk Y.;
RT "Pathogens target DC-SIGN to influence their fate DC-SIGN functions as a
RT pathogen receptor with broad specificity.";
RL APMIS 111:698-714(2003).
RN [12]
RP REVIEW.
RX PubMed=12873764; DOI=10.1016/s0005-2736(03)00161-5;
RA Gallo S.A., Finnegan C.M., Viard M., Raviv Y., Dimitrov A., Rawat S.S.,
RA Puri A., Durell S., Blumenthal R.;
RT "The HIV Env-mediated fusion reaction.";
RL Biochim. Biophys. Acta 1614:36-50(2003).
RN [13]
RP REVIEW.
RX PubMed=15719026; DOI=10.1038/sj.cdd.4401584;
RA Perfettini J.-L., Castedo M., Roumier T., Andreau K., Nardacci R.,
RA Piacentini M., Kroemer G.;
RT "Mechanisms of apoptosis induction by the HIV-1 envelope.";
RL Cell Death Differ. 12:916-923(2005).
RN [14]
RP REVIEW.
RX PubMed=15725757; DOI=10.1089/aid.2005.21.171;
RA Hartley O., Klasse P.J., Sattentau Q.J., Moore J.P.;
RT "V3: HIV's switch-hitter.";
RL AIDS Res. Hum. Retroviruses 21:171-189(2005).
RN [15]
RP REVIEW.
RX PubMed=16114975; DOI=10.2165/00003495-200565130-00002;
RA Reeves J.D., Piefer A.J.;
RT "Emerging drug targets for antiretroviral therapy.";
RL Drugs 65:1747-1766(2005).
RN [16]
RP REVIEW.
RX PubMed=16437164; DOI=10.1038/sj.emboj.7600947;
RA Lusso P.;
RT "HIV and the chemokine system: 10 years later.";
RL EMBO J. 25:447-456(2006).
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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_04083}.
CC -!- SUBUNIT: [Surface protein gp120]: The mature envelope protein (Env)
CC consists of a homotrimer of non-covalently associated gp120-gp41
CC heterodimers. The resulting complex protrudes from the virus surface as
CC a spike. There seems to be as few as 10 spikes on the average virion.
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:0000255|HAMAP-Rule:MF_04083,
CC ECO:0000269|PubMed:2214026}.
CC -!- SUBUNIT: [Transmembrane protein gp41]: The mature envelope protein
CC (Env) consists of a homotrimer of non-covalently associated gp120-gp41
CC heterodimers. The resulting complex protrudes from the virus surface as
CC a spike. There seems to be as few as 10 spikes on the average virion.
CC {ECO:0000255|HAMAP-Rule:MF_04083, ECO:0000269|PubMed:2214026}.
CC -!- SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane
CC {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_04083}.
CC -!- SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane
CC {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane
CC {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane
CC {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein
CC {ECO:0000255|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:0000255|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:0000255|HAMAP-
CC 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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_04083}.
CC -!- DOMAIN: The CD4-binding region is targeted by the antibody b12.
CC {ECO:0000255|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 to
CC hide protein sequence from adaptive immune system. {ECO:0000255|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:0000255|HAMAP-Rule:MF_04083}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC Envelope glycoproteins are synthesized as an 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:0000255|HAMAP-Rule:MF_04083,
CC ECO:0000269|PubMed:12218052, ECO:0000269|PubMed:14592831,
CC ECO:0000269|PubMed:15644496}.
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:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_04083}.
CC -!- SIMILARITY: Belongs to the HIV-1 env protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04083}.
CC -!- WEB RESOURCE: Name=hivdb; Note=HIV drug resistance database;
CC URL="https://hivdb.stanford.edu";
CC -!- WEB RESOURCE: Name=HIV drug resistance mutations;
CC URL="https://www.iasusa.org/content/hiv-drug-resistance-mutations";
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DR EMBL; M15654; AAA44205.1; -; Genomic_RNA.
DR EMBL; K02083; AAB59873.1; -; Genomic_DNA.
DR EMBL; X01762; CAA25903.1; ALT_SEQ; Genomic_RNA.
DR PIR; A03973; VCLJH3.
DR PIR; A03974; VCLJVL.
DR PDB; 2ARI; NMR; -; A=512-541.
DR PDB; 3VGY; X-ray; 2.03 A; C=546-588.
DR PDB; 3VH7; X-ray; 2.02 A; A/C/E=546-588.
DR PDB; 3VU5; X-ray; 2.09 A; A=553-590.
DR PDB; 3VU6; X-ray; 2.32 A; A=553-590.
DR PDB; 3W19; X-ray; 1.28 A; C=553-590.
DR PDB; 6ME1; X-ray; 1.97 A; E/F=512-521.
DR PDBsum; 2ARI; -.
DR PDBsum; 3VGY; -.
DR PDBsum; 3VH7; -.
DR PDBsum; 3VU5; -.
DR PDBsum; 3VU6; -.
DR PDBsum; 3W19; -.
DR PDBsum; 6ME1; -.
DR BMRB; P03375; -.
DR SMR; P03375; -.
DR MINT; P03375; -.
DR ChEMBL; CHEMBL5057; -.
DR iPTMnet; P03375; -.
DR ABCD; P03375; 2 sequenced antibodies.
DR Reactome; R-HSA-5621480; Dectin-2 family.
DR EvolutionaryTrace; P03375; -.
DR Proteomes; UP000007690; Genome.
DR Proteomes; UP000107234; Genome.
DR Proteomes; UP000126245; Genome.
DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0044538; C:host cell periphery; IDA:UniProtKB.
DR GO; GO:0020002; C:host cell plasma membrane; ISS:UniProtKB.
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:0042609; F:CD4 receptor binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
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; ISS:UniProtKB.
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; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0019062; P:virion attachment to host cell; ISS:UniProtKB.
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; 1.
PE 1: Evidence at protein level;
KW 3D-structure; AIDS; Apoptosis;
KW Clathrin-mediated endocytosis of virus by host;
KW Cleavage on pair of basic residues; Coiled coil; Direct protein sequencing;
KW Disulfide bond; Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host endosome; Host membrane; Host-virus interaction;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Viral immunoevasion;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT SIGNAL 1..32
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CHAIN 33..856
FT /note="Envelope glycoprotein gp160"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT /id="PRO_0000239239"
FT CHAIN 33..511
FT /note="Surface protein gp120"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT /id="PRO_0000038371"
FT CHAIN 512..856
FT /note="Transmembrane protein gp41"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT /id="PRO_0000038372"
FT TOPO_DOM 33..684
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT TRANSMEM 685..705
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT TOPO_DOM 706..856
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 131..156
FT /note="V1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 157..196
FT /note="V2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 296..330
FT /note="V3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 364..374
FT /note="CD4-binding loop"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 385..418
FT /note="V4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 461..471
FT /note="V5"
FT REGION 463..471
FT /note="V5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 512..532
FT /note="Fusion peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 574..592
FT /note="Immunosuppression"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 662..683
FT /note="MPER; binding to GalCer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 662..667
FT /note="Involved in GalCer binding"
FT REGION 721..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 633..667
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT MOTIF 712..715
FT /note="YXXL motif; contains endocytosis signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT MOTIF 855..856
FT /note="Di-leucine internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT SITE 511..512
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT LIPID 764
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 674
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT DISULFID 54..74
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT DISULFID 119..205
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT DISULFID 126..196
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT DISULFID 131..157
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT DISULFID 218..247
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT DISULFID 228..239
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT DISULFID 296..331
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT DISULFID 378..445
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT DISULFID 385..418
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:2355006"
FT DISULFID 598..604
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT VARIANT 403
FT /note="K -> E (in strain: Isolate PV22)"
FT VARIANT 423
FT /note="I -> F (in strain: Isolate PV22)"
FT VARIANT 461
FT /note="S -> N (in strain: Isolate PV22)"
FT VARIANT 668
FT /note="S -> N (in strain: Isolate PV22)"
FT VARIANT 673
FT /note="F -> L (in strain: Isolate PV22)"
FT VARIANT 704
FT /note="V -> I (in strain: Isolate PV22)"
FT VARIANT 723
FT /note="I -> T (in strain: Isolate PV22)"
FT VARIANT 737
FT /note="G -> D (in strain: Isolate PV22)"
FT HELIX 516..530
FT /evidence="ECO:0007829|PDB:2ARI"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:2ARI"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:2ARI"
FT HELIX 554..589
FT /evidence="ECO:0007829|PDB:3W19"
SQ SEQUENCE 856 AA; 97225 MW; 0BFFB1A18931BB27 CRC64;
MRVKEKYQHL WRWGWRWGTM LLGMLMICSA TEKLWVTVYY GVPVWKEATT TLFCASDAKA
YDTEVHNVWA THACVPTDPN PQEVVLVNVT ENFNMWKNDM VEQMHEDIIS LWDQSLKPCV
KLTPLCVSLK CTDLKNDTNT NSSSGRMIME KGEIKNCSFN ISTSIRGKVQ KEYAFFYKLD
IIPIDNDTTS YTLTSCNTSV ITQACPKVSF EPIPIHYCAP AGFAILKCNN KTFNGTGPCT
NVSTVQCTHG IRPVVSTQLL LNGSLAEEEV VIRSANFTDN AKTIIVQLNQ SVEINCTRPN
NNTRKSIRIQ RGPGRAFVTI GKIGNMRQAH CNISRAKWNN TLKQIDSKLR EQFGNNKTII
FKQSSGGDPE IVTHSFNCGG EFFYCNSTQL FNSTWFNSTW STKGSNNTEG SDTITLPCRI
KQIINMWQEV GKAMYAPPIS GQIRCSSNIT GLLLTRDGGN SNNESEIFRP GGGDMRDNWR
SELYKYKVVK IEPLGVAPTK AKRRVVQREK RAVGIGALFL GFLGAAGSTM GAASMTLTVQ
ARQLLSGIVQ QQNNLLRAIE AQQHLLQLTV WGIKQLQARI LAVERYLKDQ QLLGIWGCSG
KLICTTAVPW NASWSNKSLE QIWNNMTWME WDREINNYTS LIHSLIEESQ NQQEKNEQEL
LELDKWASLW NWFNITNWLW YIKLFIMIVG GLVGLRIVFA VLSVVNRVRQ GYSPLSFQTH
LPIPRGPDRP EGIEEEGGER DRDRSIRLVN GSLALIWDDL RSLCLFSYHR LRDLLLIVTR
IVELLGRRGW EALKYWWNLL QYWSQELKNS AVSLLNATAI AVAEGTDRVI EVVQGAYRAI
RHIPRRIRQG LERILL
