ENV_HV1BR
ID ENV_HV1BR Reviewed; 861 AA.
AC P03377; Q85582;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 171.
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 BRU/LAI)
OS (HIV-1).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11686;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2981635; DOI=10.1016/0092-8674(85)90303-4;
RA Wain-Hobson S., Sonigo P., Danos O., Cole S., Alizon M.;
RT "Nucleotide sequence of the AIDS virus, LAV.";
RL Cell 40:9-17(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Clone pNL4-3;
RA Buckler C.E.;
RL Submitted (JUL-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE REVISION TO 537 AND 538.
RA Strebel K.J., Martin M.A.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION OF SURFACE PROTEIN GP120 WITH HUMAN CD209/DC-SIGN.
RX PubMed=1518869; DOI=10.1073/pnas.89.17.8356;
RA Curtis B.M., Scharnowske S., Watson A.J.;
RT "Sequence and expression of a membrane-associated C-type lectin that
RT exhibits CD4-independent binding of human immunodeficiency virus envelope
RT glycoprotein gp 120.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8356-8360(1992).
RN [5]
RP INTERACTION OF SURFACE PROTEIN GP120 WITH HOST CD209/DC-SIGN.
RC STRAIN=Clone pNL4-3;
RX PubMed=11312337; DOI=10.1128/jvi.75.10.4664-4672.2001;
RA Pohlmann S., Baribaud F., Lee B., Leslie G.J., Sanchez M.D.,
RA Hiebenthal-Millow K., Munch J., Kirchhoff F., Doms R.W.;
RT "DC-SIGN interactions with human immunodeficiency virus type 1 and 2 and
RT simian immunodeficiency virus.";
RL J. Virol. 75:4664-4672(2001).
RN [6]
RP INTERACTION OF SURFACE PROTEIN GP120 WITH HUMAN CD209/DC-SIGN.
RC STRAIN=Clone pNL4-3;
RX PubMed=11825572; DOI=10.1016/s1074-7613(02)00259-5;
RA Kwon D.S., Gregorio G., Bitton N., Hendrickson W.A., Littman D.R.;
RT "DC-SIGN-mediated internalization of HIV is required for trans-enhancement
RT of T cell infection.";
RL Immunity 16:135-144(2002).
RN [7]
RP REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY P4HB/PDI.
RX PubMed=12218051; DOI=10.1074/jbc.m204547200;
RA Gallina A., Hanley T.M., Mandel R., Trahey M., Broder C.C., Viglianti G.A.,
RA Ryser H.J.;
RT "Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide
RT bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry.";
RL J. Biol. Chem. 277:50579-50588(2002).
RN [8]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN BY HOST FURIN.
RC STRAIN=Clone pNL4-3;
RX PubMed=15371436; DOI=10.1074/jbc.m403394200;
RA Kibler K.V., Miyazato A., Yedavalli V.S.R.K., Dayton A.I., Jacobs B.L.,
RA Dapolito G., Kim S.-J., Jeang K.-T.;
RT "Polyarginine inhibits gp160 processing by furin and suppresses productive
RT human immunodeficiency virus type 1 infection.";
RL J. Biol. Chem. 279:49055-49063(2004).
RN [9]
RP ROLE OF PALMITOYLATION, AND MUTAGENESIS OF CYS-769.
RC STRAIN=Clone pNL4-3;
RX PubMed=15113929; DOI=10.1128/jvi.78.10.5500-5506.2004;
RA Bhattacharya J., Peters P.J., Clapham P.R.;
RT "Human immunodeficiency virus type 1 envelope glycoproteins that lack
RT cytoplasmic domain cysteines: impact on association with membrane lipid
RT rafts and incorporation onto budding virus particles.";
RL J. Virol. 78:5500-5506(2004).
RN [10]
RP REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY HUMAN TXN.
RC STRAIN=Clone pNL4-3;
RX PubMed=16507315; DOI=10.1016/j.virol.2006.01.041;
RA Ou W., Silver J.;
RT "Role of protein disulfide isomerase and other thiol-reactive proteins in
RT HIV-1 envelope protein-mediated fusion.";
RL Virology 350:406-417(2006).
RN [11]
RP DISULFIDE BONDS.
RX PubMed=18653472; DOI=10.1091/mbc.e07-12-1282;
RA van Anken E., Sanders R.W., Liscaljet I.M., Land A., Bontjer I.,
RA Tillemans S., Nabatov A.A., Paxton W.A., Berkhout B., Braakman I.;
RT "Only five of 10 strictly conserved disulfide bonds are essential for
RT folding and eight for function of the HIV-1 envelope glycoprotein.";
RL Mol. Biol. Cell 19:4298-4309(2008).
RN [12]
RP INTERACTION OF GP120 WITH HUMAN ITGA4/ITGB7 HETERODIMER, AND MUTAGENESIS OF
RP 184-LEU-ASP-185.
RC STRAIN=Clone pNL4-3;
RX PubMed=18264102; DOI=10.1038/ni1566;
RA Arthos J., Cicala C., Martinelli E., Macleod K., Van Ryk D., Wei D.,
RA Xiao Z., Veenstra T.D., Conrad T.P., Lempicki R.A., McLaughlin S.,
RA Pascuccio M., Gopaul R., McNally J., Cruz C.C., Censoplano N., Chung E.,
RA Reitano K.N., Kottilil S., Goode D.J., Fauci A.S.;
RT "HIV-1 envelope protein binds to and signals through integrin alpha4beta7,
RT the gut mucosal homing receptor for peripheral T cells.";
RL Nat. Immunol. 9:301-309(2008).
RN [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 537-670.
RX PubMed=11026535; DOI=10.1016/s0968-0896(00)00155-3;
RA Zhou G., Ferrer M., Chopra R., Kapoor T.M., Strassmaier T., Weissenhorn W.,
RA Skehel J.J., Oprian D., Schreiber S.L., Harrison S.C., Wiley D.C.;
RT "The structure of an HIV-1 specific cell entry inhibitor in complex with
RT the HIV-1 gp41 trimeric core.";
RL Bioorg. Med. Chem. 8:2219-2227(2000).
RN [20]
RP STRUCTURE BY FTIR OF 517-539.
RX PubMed=11853678; DOI=10.1016/s0005-2736(01)00443-6;
RA Gordon L.M., Mobley P.W., Pilpa R., Sherman M.A., Waring A.J.;
RT "Conformational mapping of the N-terminal peptide of HIV-1 gp41 in membrane
RT environments using (13)C-enhanced Fourier transform infrared
RT spectroscopy.";
RL Biochim. Biophys. Acta 1559:96-120(2002).
RN [21]
RP STRUCTURE BY FTIR OF 517-539.
RX PubMed=15044732; DOI=10.1110/ps.03407704;
RA Gordon L.M., Mobley P.W., Lee W., Eskandari S., Kaznessis Y.N.,
RA Sherman M.A., Waring A.J.;
RT "Conformational mapping of the N-terminal peptide of HIV-1 gp41 in lipid
RT detergent and aqueous environments using 13C-enhanced Fourier transform
RT infrared spectroscopy.";
RL Protein Sci. 13:1012-1030(2004).
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:11312337, ECO:0000269|PubMed:11825572,
CC ECO:0000269|PubMed:1518869, ECO:0000269|PubMed:18264102}.
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:11312337,
CC ECO:0000269|PubMed:11825572, ECO:0000269|PubMed:1518869,
CC ECO:0000269|PubMed:18264102}.
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 ECO:0000269|PubMed:15113929}.
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:15371436, ECO:0000269|PubMed:16507315}.
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; K02013; AAB59751.1; -; Genomic_RNA.
DR EMBL; A04321; CAA00352.1; -; Unassigned_RNA.
DR EMBL; M19921; AAA44992.2; -; Genomic_RNA.
DR PIR; A03975; VCLJLV.
DR PDB; 1ENV; X-ray; 2.60 A; A=546-593, A=633-670.
DR PDB; 1ERF; IR; -; A=517-539.
DR PDB; 1FAV; X-ray; 3.00 A; A=546-595, C=639-670.
DR PDB; 1JD8; NMR; -; A=600-612.
DR PDB; 1P5A; IR; -; A=517-539.
DR PDB; 1U6U; NMR; -; A=310-326.
DR PDB; 1U6V; NMR; -; A=310-326.
DR PDB; 2ZZO; X-ray; 2.20 A; C=633-666, N=551-586.
DR PDB; 3G9R; X-ray; 2.00 A; A/B/C/D/E/F=667-689.
DR PDB; 3MNW; X-ray; 2.20 A; P=657-676.
DR PDB; 3VGX; X-ray; 1.74 A; C=558-595, D=626-657.
DR PDB; 3VTP; X-ray; 1.90 A; C=555-595, D=631-666.
DR PDB; 5WES; X-ray; 2.71 A; P=316-320.
DR PDB; 5WET; X-ray; 2.64 A; P=316-321.
DR PDB; 5WEU; X-ray; 1.58 A; P=316-325.
DR PDB; 6R2G; X-ray; 1.90 A; C=632-666.
DR PDBsum; 1ENV; -.
DR PDBsum; 1ERF; -.
DR PDBsum; 1FAV; -.
DR PDBsum; 1JD8; -.
DR PDBsum; 1P5A; -.
DR PDBsum; 1U6U; -.
DR PDBsum; 1U6V; -.
DR PDBsum; 2ZZO; -.
DR PDBsum; 3G9R; -.
DR PDBsum; 3MNW; -.
DR PDBsum; 3VGX; -.
DR PDBsum; 3VTP; -.
DR PDBsum; 5WES; -.
DR PDBsum; 5WET; -.
DR PDBsum; 5WEU; -.
DR PDBsum; 6R2G; -.
DR BMRB; P03377; -.
DR SMR; P03377; -.
DR IntAct; P03377; 1.
DR BindingDB; P03377; -.
DR ChEMBL; CHEMBL5826; -.
DR PRIDE; P03377; -.
DR ABCD; P03377; 62 sequenced antibodies.
DR Reactome; R-HSA-5621480; Dectin-2 family.
DR EvolutionaryTrace; P03377; -.
DR Proteomes; UP000007692; Genome.
DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
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: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; Disulfide bond;
KW 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..861
FT /note="Envelope glycoprotein gp160"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT /id="PRO_0000239474"
FT CHAIN 33..516
FT /note="Surface protein gp120"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT /id="PRO_0000038388"
FT CHAIN 517..861
FT /note="Transmembrane protein gp41"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT /id="PRO_0000038389"
FT TOPO_DOM 33..689
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT TRANSMEM 690..710
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT TOPO_DOM 711..861
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 131..161
FT /note="V1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 162..201
FT /note="V2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 301..335
FT /note="V3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 369..379
FT /note="CD4-binding loop"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 390..423
FT /note="V4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 466..476
FT /note="V5"
FT REGION 468..476
FT /note="V5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 517..537
FT /note="Fusion peptide"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 579..597
FT /note="Immunosuppression"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 667..688
FT /note="MPER; binding to GalCer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT REGION 723..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 638..672
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT MOTIF 184..186
FT /note="Putative binding site to alpha-4/beta-7 integrin"
FT MOTIF 717..720
FT /note="YXXL motif; contains endocytosis signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT MOTIF 860..861
FT /note="Di-leucine internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT COMPBIAS 732..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 516..517
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT LIPID 769
FT /note="S-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT LIPID 842
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 CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 468
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 621
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 642
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083"
FT CARBOHYD 679
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:18653472"
FT DISULFID 119..210
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:18653472"
FT DISULFID 126..201
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:18653472"
FT DISULFID 131..162
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:18653472"
FT DISULFID 223..252
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:18653472"
FT DISULFID 233..244
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:18653472"
FT DISULFID 301..336
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:18653472"
FT DISULFID 383..450
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:18653472"
FT DISULFID 390..423
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:18653472"
FT DISULFID 603..609
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083,
FT ECO:0000269|PubMed:18653472"
FT VARIANT 135..137
FT /note="GNA -> KND (in strain: Clone pNL4-3)"
FT VARIANT 143..147
FT /note="Missing (in strain: Clone pNL4-3)"
FT VARIANT 151..153
FT /note="EMM -> RMI (in strain: Clone pNL4-3)"
FT VARIANT 172
FT /note="G -> D (in strain: Clone pNL4-3)"
FT VARIANT 187
FT /note="I -> V (in strain: Clone pNL4-3)"
FT VARIANT 192..193
FT /note="Missing (in strain: Clone pNL4-3)"
FT VARIANT 197..199
FT /note="TLT -> RLI (in strain: Clone pNL4-3)"
FT VARIANT 274
FT /note="E -> D (in strain: Clone pNL4-3)"
FT VARIANT 295
FT /note="Q -> T (in strain: Clone pNL4-3)"
FT VARIANT 538
FT /note="R -> A (in strain: Clone pNL4-3)"
FT VARIANT 552
FT /note="G -> D (in strain: Clone pNL4-3)"
FT VARIANT 689
FT /note="I -> L (in strain: Clone pNL4-3)"
FT VARIANT 728
FT /note="T -> I (in strain: Clone pNL4-3)"
FT VARIANT 818
FT /note="S -> N (in strain: Clone pNL4-3)"
FT VARIANT 838..842
FT /note="VQGAC -> LQAAY (in strain: Clone pNL4-3)"
FT MUTAGEN 184..185
FT /note="LD->AA: Partial loss of CD4-independent binding."
FT /evidence="ECO:0000269|PubMed:18264102"
FT MUTAGEN 769
FT /note="C->F: Almost no effect on virions assembly and
FT infectivity."
FT /evidence="ECO:0000269|PubMed:15113929"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:1U6U"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:1U6U"
FT HELIX 559..594
FT /evidence="ECO:0007829|PDB:3VGX"
FT HELIX 606..614
FT /evidence="ECO:0007829|PDB:6R2G"
FT HELIX 633..655
FT /evidence="ECO:0007829|PDB:3VGX"
FT HELIX 668..689
FT /evidence="ECO:0007829|PDB:3G9R"
SQ SEQUENCE 861 AA; 97488 MW; 04DE2B4D4E4FD63A CRC64;
MRVKEKYQHL WRWGWKWGTM LLGILMICSA TEKLWVTVYY GVPVWKEATT TLFCASDAKA
YDTEVHNVWA THACVPTDPN PQEVVLVNVT ENFNMWKNDM VEQMHEDIIS LWDQSLKPCV
KLTPLCVSLK CTDLGNATNT NSSNTNSSSG EMMMEKGEIK NCSFNISTSI RGKVQKEYAF
FYKLDIIPID NDTTSYTLTS CNTSVITQAC PKVSFEPIPI HYCAPAGFAI LKCNNKTFNG
TGPCTNVSTV QCTHGIRPVV STQLLLNGSL AEEEVVIRSA NFTDNAKTII VQLNQSVEIN
CTRPNNNTRK SIRIQRGPGR AFVTIGKIGN MRQAHCNISR AKWNATLKQI ASKLREQFGN
NKTIIFKQSS GGDPEIVTHS FNCGGEFFYC NSTQLFNSTW FNSTWSTEGS NNTEGSDTIT
LPCRIKQFIN MWQEVGKAMY APPISGQIRC SSNITGLLLT RDGGNNNNGS EIFRPGGGDM
RDNWRSELYK YKVVKIEPLG VAPTKAKRRV VQREKRAVGI GALFLGFLGA AGSTMGARSM
TLTVQARQLL SGIVQQQNNL LRAIEAQQHL LQLTVWGIKQ LQARILAVER YLKDQQLLGI
WGCSGKLICT TAVPWNASWS NKSLEQIWNN MTWMEWDREI NNYTSLIHSL IEESQNQQEK
NEQELLELDK WASLWNWFNI TNWLWYIKIF IMIVGGLVGL RIVFAVLSIV NRVRQGYSPL
SFQTHLPTPR GPDRPEGIEE EGGERDRDRS IRLVNGSLAL IWDDLRSLCL FSYHRLRDLL
LIVTRIVELL GRRGWEALKY WWNLLQYWSQ ELKNSAVSLL NATAIAVAEG TDRVIEVVQG
ACRAIRHIPR RIRQGLERIL L
