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P03377 (ENV_HV1BR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Envelope glycoprotein gp160
Alternative name(s):
Env polyprotein

Cleaved into the following 2 chains:

  1. Surface protein gp120
    Short name=SU
    Alternative name(s):
    Glycoprotein 120
    Short name=gp120
  2. Transmembrane protein gp41
    Short name=TM
    Alternative name(s):
    Glycoprotein 41
    Short name=gp41
Gene names
Name:env
OrganismHuman immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI) (HIV-1) [Complete proteome]
Taxonomic identifier11686 [NCBI]
Taxonomic lineageVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length861 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 to maintain the highly conserved coreceptor-binding site in a cryptic conformation, protected from neutralizing antibodies. Since CD4 also displays a binding site for the disulfide-isomerase P4HB/PDI, a P4HB/PDI-CD4-CXCR4-gp120 complex may form. In that complex, P4HB/PDI could reach and reduce gp120 disulfide bonds, causing major conformational changes in gp120. TXN, another PDI family member could also be involved in disulfide rearrangements in Env during fusion. These changes are transmitted to the transmembrane protein gp41 and are thought to activate its fusogenic potential by unmasking its fusion peptide. Ref.6

Surface protein gp120 (SU) may target the virus to gut-associated lymphoid tissue (GALT) by binding host ITGA4/ITGB7 (alpha-4/beta-7 integrins), a complex that mediates T-cell migration to the GALT. Interaction between gp120 and ITGA4/ITGB7 would allow the virus to enter GALT early in the infection, infecting and killing most of GALT's resting CD4+ T-cells. This T-cell depletion is believed to be the major insult to the host immune system leading to AIDS By similarity. Ref.6

The surface protein gp120 is a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. DCs are professional antigen presenting cells, critical for host immunity by inducing specific immune responses against a broad variety of pathogens. They act as sentinels in various tissues where they take up antigen, process it, and present it to T-cells following migration to lymphoid organs. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. Virion capture also seems to lead to MHC-II-restricted viral antigen presentation, and probably to the activation of HIV-specific CD4+ cells By similarity. Ref.6

The transmembrane protein gp41 (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm By similarity. Ref.6

The envelope glyprotein gp160 precursor down-modulates cell surface CD4 antigen by interacting with it in the endoplasmic reticulum and blocking its transport to the cell surface By similarity. Ref.6

The gp120-gp41 heterodimer seems to contribute to T-cell depletion during HIV-1 infection. The envelope glycoproteins expressed on the surface of infected cells induce apoptosis through an interaction with uninfected cells expressing the receptor (CD4) and the coreceptors CXCR4 or CCR5. This type of bystander killing may be obtained by at least three distinct mechanisms. First, the interaction between the 2 cells can induce cellular fusion followed by nuclear fusion within the syncytium. Syncytia are condemned to die from apoptosis. Second, the 2 interacting cells may not fuse entirely and simply exchange plasma membrane lipids, after a sort of hemifusion process, followed by rapid death. Third, it is possible that virus-infected cells, on the point of undergoing apoptosis, fuse with CD4-expressing cells, in which case apoptosis is rapidly transmitted from one cell to the other and thus occurs in a sort of contagious fashion By similarity. Ref.6

The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves By similarity. Ref.6

Subunit structure

The mature envelope protein (Env) consists of a homotrimer of non-covalently associated gp120-gp41 heterodimers. The resulting complex protrudes from the virus surface as a spike. There seems to be as few as 10 spikes on the average virion. Surface protein gp120 interacts with human CD4, CCR5 and CXCR4, to form a P4HB/PDI-CD4-CXCR4-gp120 complex. Gp120 also interacts with the C-type lectins CD209/DC-SIGN and CLEC4M/DC-SIGNR (collectively referred to as DC-SIGN(R)). Gp120 and gp41 interact with GalCer. Gp120 interacts with human ITGA4/ITGB7 complex; on CD4+ T-cells, this interaction results in rapid activation of integrin ITGAL/LFA-1, which facilitate efficient cell-to-cell spreading of HIV-1. Gp120 interacts with cell-associated heparan sulfate; this interaction increases virus infectivity on permissive cells and may be involved in infection of CD4- cells By similarity. Ref.4 Ref.5 Ref.6 Ref.12

Subcellular location

Transmembrane protein gp41: Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein. Host endosome membrane; Single-pass type I membrane protein Potential. Note: It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag.

Surface protein gp120: Virion membrane; Peripheral membrane protein. Host cell membrane; Peripheral membrane protein. Host endosome membrane; Peripheral membrane protein Potential. Note: The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag.

Domain

The YXXL motif is involved in determining the exact site of viral release at the surface of infected mononuclear cells and promotes endocytosis. YXXL and di-leucine endocytosis motifs interact directly or indirectly with the clathrin adapter complexes, opperate independently, and their activities are not additive By similarity.

The 17 amino acids long immunosuppressive region is present in many retroviral envelope proteins. Synthetic peptides derived from this relatively conserved sequence inhibit immune function in vitro and in vivo By similarity.

Some of the most genetically diverse regions of the viral genome are present in Env. They are called variable regions 1 through 5 (V1 through V5). Coreceptor usage of gp120 is determined mainly by the primary structure of the third variable region (V3) in the outer domain of gp120. The sequence of V3 determines which coreceptor, CCR5 and/or CXCR4 (corresponding to R5/macrophage, X4/T cell and R5X4/T cell and macrophage tropism), is used to trigger the fusion potential of the Env complex, and hence which cells the virus can infect. Binding to CCR5 involves a region adjacent in addition to V3.

Post-translational modification

Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as a inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. About 2 of the 9 disulfide bonds of gp41 are reduced by P4HB/PDI, following binding to CD4 receptor By similarity.

Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic cleavage) is essential for their association with host cell membrane lipid rafts. Palmitoylation is therefore required for envelope trafficking to classical lipid rafts, but not for viral replication. Ref.9

Miscellaneous

Inhibitors targeting HIV-1 viral envelope proteins are used as antiretroviral drugs. Attachment of virions to the cell surface via non-specific interactions and CD4 binding can be blocked by inhibitors that include cyanovirin-N, cyclotriazadisulfonamide analogs, PRO 2000, TNX 355 and PRO 542. In addition, BMS 806 can block CD4-induced conformational changes. Env interactions with the coreceptor molecules can be targeted by CCR5 antagonists including SCH-D, maraviroc (UK 427857) and aplaviroc (GW 873140), and the CXCR4 antagonist AMD 070. Fusion of viral and cellular membranes can be inhibited by peptides such as enfuvirtide and tifuvirtide (T 1249). Resistance to inhibitors associated with mutations in Env are observed. Most of the time, single mutations confer only a modest reduction in drug susceptibility. Combination of several mutations is usually required to develop a high-level drug resistance.

HIV-1 lineages are divided in three main groups, M (for Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast majority of strains found worldwide belong to the group M. Group O seems to be endemic to and largely confined to Cameroon and neighboring countries in West Central Africa, where these viruses represent a small minority of HIV-1 strains. The group N is represented by a limited number of isolates from Cameroonian persons. The group M is further subdivided in 9 clades or subtypes (A to D, F to H, J and K).

Sequence similarities

Belongs to the lentiviruses env family.

Ontologies

Keywords
   Biological processApoptosis
Clathrin-mediated endocytosis of virus by host
Fusion of virus membrane with host endosomal membrane
Fusion of virus membrane with host membrane
Host-virus interaction
Viral attachment to host cell
Viral immunoevasion
Viral penetration into host cytoplasm
Virus endocytosis by host
Virus entry into host cell
   Cellular componentHost cell membrane
Host endosome
Host membrane
Membrane
Viral envelope protein
Virion
   DiseaseAIDS
   DomainCoiled coil
Signal
Transmembrane
Transmembrane helix
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

clathrin-mediated endocytosis of virus by host cell

Inferred from electronic annotation. Source: UniProtKB-KW

evasion or tolerance by virus of host immune response

Inferred from electronic annotation. Source: UniProtKB-KW

fusion of virus membrane with host endosome membrane

Inferred from electronic annotation. Source: UniProtKB-KW

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

host cell plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

viral envelope

Inferred from electronic annotation. Source: UniProtKB-KW

virion membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionstructural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 By similarity
Chain33 – 861829Envelope glycoprotein gp160
PRO_0000239474
Chain33 – 516484Surface protein gp120
PRO_0000038388
Chain517 – 861345Transmembrane protein gp41
PRO_0000038389

Regions

Topological domain33 – 689657Extracellular Potential
Transmembrane690 – 71021Helical; Potential
Topological domain711 – 861151Cytoplasmic Potential
Region131 – 16131V1
Region162 – 20140V2
Region301 – 33535V3
Region369 – 37911CD4-binding loop By similarity
Region390 – 42334V4
Region466 – 47611V5
Region517 – 53721Fusion peptide Potential
Region581 – 59717Immunosuppression By similarity
Region667 – 68822MPER; binding to GalCer By similarity
Region667 – 6726Involved in GalCer binding By similarity
Coiled coil638 – 67235 Potential
Motif184 – 1863Putative binding site to alpha-4/beta-7 integrin
Motif717 – 7204YXXL motif; contains endocytosis signal By similarity
Motif860 – 8612Di-leucine internalization motif By similarity
Compositional bias465 – 4684Poly-Asn

Sites

Site516 – 5172Cleavage; by host furin

Amino acid modifications

Lipidation7691S-palmitoyl cysteine; by host By similarity
Lipidation8421S-palmitoyl cysteine; by host By similarity
Glycosylation881N-linked (GlcNAc...); by host Potential
Glycosylation1361N-linked (GlcNAc...); by host Potential
Glycosylation1411N-linked (GlcNAc...); by host Potential
Glycosylation1461N-linked (GlcNAc...); by host Potential
Glycosylation1611N-linked (GlcNAc...); by host Potential
Glycosylation1651N-linked (GlcNAc...); by host Potential
Glycosylation1911N-linked (GlcNAc...); by host Potential
Glycosylation2021N-linked (GlcNAc...); by host Potential
Glycosylation2351N-linked (GlcNAc...); by host Potential
Glycosylation2391N-linked (GlcNAc...); by host Potential
Glycosylation2461N-linked (GlcNAc...); by host Potential
Glycosylation2671N-linked (GlcNAc...); by host Potential
Glycosylation2811N-linked (GlcNAc...); by host Potential
Glycosylation2941N-linked (GlcNAc...); by host Potential
Glycosylation3001N-linked (GlcNAc...); by host Potential
Glycosylation3061N-linked (GlcNAc...); by host Potential
Glycosylation3371N-linked (GlcNAc...); by host Potential
Glycosylation3441N-linked (GlcNAc...); by host Potential
Glycosylation3611N-linked (GlcNAc...); by host Potential
Glycosylation3911N-linked (GlcNAc...); by host Potential
Glycosylation3971N-linked (GlcNAc...); by host Potential
Glycosylation4021N-linked (GlcNAc...); by host Potential
Glycosylation4111N-linked (GlcNAc...); by host Potential
Glycosylation4531N-linked (GlcNAc...); by host Potential
Glycosylation4681N-linked (GlcNAc...); by host Potential
Glycosylation6161N-linked (GlcNAc...); by host Potential
Glycosylation6211N-linked (GlcNAc...); by host Potential
Glycosylation6301N-linked (GlcNAc...); by host Potential
Glycosylation6421N-linked (GlcNAc...); by host Potential
Glycosylation6791N-linked (GlcNAc...); by host Potential
Disulfide bond54 ↔ 74 Ref.7 Ref.10 Ref.11
Disulfide bond119 ↔ 210 Ref.7 Ref.10 Ref.11
Disulfide bond126 ↔ 201 Ref.7 Ref.10 Ref.11
Disulfide bond131 ↔ 162 Ref.7 Ref.10 Ref.11
Disulfide bond223 ↔ 252 Ref.7 Ref.10 Ref.11
Disulfide bond233 ↔ 244 Ref.7 Ref.10 Ref.11
Disulfide bond301 ↔ 336 Ref.7 Ref.10 Ref.11
Disulfide bond383 ↔ 450 Ref.7 Ref.10 Ref.11
Disulfide bond390 ↔ 423 Ref.7 Ref.10 Ref.11
Disulfide bond603 ↔ 609 Ref.7 Ref.10 Ref.11

Natural variations

Natural variant135 – 1373GNA → KND in strain: Clone pNL4-3.
Natural variant143 – 1475Missing in strain: Clone pNL4-3.
Natural variant151 – 1533EMM → RMI in strain: Clone pNL4-3.
Natural variant1721G → D in strain: Clone pNL4-3.
Natural variant1871I → V in strain: Clone pNL4-3.
Natural variant192 – 1932Missing in strain: Clone pNL4-3.
Natural variant197 – 1993TLT → RLI in strain: Clone pNL4-3.
Natural variant2741E → D in strain: Clone pNL4-3.
Natural variant2951Q → T in strain: Clone pNL4-3.
Natural variant5381R → A in strain: Clone pNL4-3.
Natural variant5521G → D in strain: Clone pNL4-3.
Natural variant6891I → L in strain: Clone pNL4-3.
Natural variant7281T → I in strain: Clone pNL4-3.
Natural variant8181S → N in strain: Clone pNL4-3.
Natural variant838 – 8425VQGAC → LQAAY in strain: Clone pNL4-3.

Experimental info

Mutagenesis184 – 1852LD → AA: Partial loss of CD4-independent binding. Ref.12
Mutagenesis7691C → F: Almost no effect on virions assembly and infectivity. Ref.9 Ref.12

Secondary structure

........... 861
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P03377 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 04DE2B4D4E4FD63A

FASTA86197,488
        10         20         30         40         50         60 
MRVKEKYQHL WRWGWKWGTM LLGILMICSA TEKLWVTVYY GVPVWKEATT TLFCASDAKA 

        70         80         90        100        110        120 
YDTEVHNVWA THACVPTDPN PQEVVLVNVT ENFNMWKNDM VEQMHEDIIS LWDQSLKPCV 

       130        140        150        160        170        180 
KLTPLCVSLK CTDLGNATNT NSSNTNSSSG EMMMEKGEIK NCSFNISTSI RGKVQKEYAF 

       190        200        210        220        230        240 
FYKLDIIPID NDTTSYTLTS CNTSVITQAC PKVSFEPIPI HYCAPAGFAI LKCNNKTFNG 

       250        260        270        280        290        300 
TGPCTNVSTV QCTHGIRPVV STQLLLNGSL AEEEVVIRSA NFTDNAKTII VQLNQSVEIN 

       310        320        330        340        350        360 
CTRPNNNTRK SIRIQRGPGR AFVTIGKIGN MRQAHCNISR AKWNATLKQI ASKLREQFGN 

       370        380        390        400        410        420 
NKTIIFKQSS GGDPEIVTHS FNCGGEFFYC NSTQLFNSTW FNSTWSTEGS NNTEGSDTIT 

       430        440        450        460        470        480 
LPCRIKQFIN MWQEVGKAMY APPISGQIRC SSNITGLLLT RDGGNNNNGS EIFRPGGGDM 

       490        500        510        520        530        540 
RDNWRSELYK YKVVKIEPLG VAPTKAKRRV VQREKRAVGI GALFLGFLGA AGSTMGARSM 

       550        560        570        580        590        600 
TLTVQARQLL SGIVQQQNNL LRAIEAQQHL LQLTVWGIKQ LQARILAVER YLKDQQLLGI 

       610        620        630        640        650        660 
WGCSGKLICT TAVPWNASWS NKSLEQIWNN MTWMEWDREI NNYTSLIHSL IEESQNQQEK 

       670        680        690        700        710        720 
NEQELLELDK WASLWNWFNI TNWLWYIKIF IMIVGGLVGL RIVFAVLSIV NRVRQGYSPL 

       730        740        750        760        770        780 
SFQTHLPTPR GPDRPEGIEE EGGERDRDRS IRLVNGSLAL IWDDLRSLCL FSYHRLRDLL 

       790        800        810        820        830        840 
LIVTRIVELL GRRGWEALKY WWNLLQYWSQ ELKNSAVSLL NATAIAVAEG TDRVIEVVQG 

       850        860 
ACRAIRHIPR RIRQGLERIL L 

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References

[1]"Nucleotide sequence of the AIDS virus, LAV."
Wain-Hobson S., Sonigo P., Danos O., Cole S., Alizon M.
Cell 40:9-17(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]Buckler C.E.
Submitted (JUL-1989) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Clone pNL4-3.
[3]Strebel K.J., Martin M.A.
Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 537 AND 538.
[4]"Sequence and expression of a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp 120."
Curtis B.M., Scharnowske S., Watson A.J.
Proc. Natl. Acad. Sci. U.S.A. 89:8356-8360(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION OF SURFACE PROTEIN GP120 WITH HUMAN CD209/DC-SIGN.
[5]"DC-SIGN interactions with human immunodeficiency virus type 1 and 2 and simian immunodeficiency virus."
Pohlmann S., Baribaud F., Lee B., Leslie G.J., Sanchez M.D., Hiebenthal-Millow K., Munch J., Kirchhoff F., Doms R.W.
J. Virol. 75:4664-4672(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION OF SURFACE PROTEIN GP120 WITH HOST CD209/DC-SIGN.
Strain: Clone pNL4-3.
[6]"DC-SIGN-mediated internalization of HIV is required for trans-enhancement of T cell infection."
Kwon D.S., Gregorio G., Bitton N., Hendrickson W.A., Littman D.R.
Immunity 16:135-144(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION OF SURFACE PROTEIN GP120 WITH HUMAN CD209/DC-SIGN, ROLE IN TRANS INFECTION.
Strain: Clone pNL4-3.
[7]"Inhibitors of protein-disulfide isomerase prevent cleavage of disulfide bonds in receptor-bound glycoprotein 120 and prevent HIV-1 entry."
Gallina A., Hanley T.M., Mandel R., Trahey M., Broder C.C., Viglianti G.A., Ryser H.J.
J. Biol. Chem. 277:50579-50588(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY P4HB/PDI.
[8]"Polyarginine inhibits gp160 processing by furin and suppresses productive human immunodeficiency virus type 1 infection."
Kibler K.V., Miyazato A., Yedavalli V.S.R.K., Dayton A.I., Jacobs B.L., Dapolito G., Kim S.-J., Jeang K.-T.
J. Biol. Chem. 279:49055-49063(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN BY HOST FURIN.
Strain: Clone pNL4-3.
[9]"Human immunodeficiency virus type 1 envelope glycoproteins that lack cytoplasmic domain cysteines: impact on association with membrane lipid rafts and incorporation onto budding virus particles."
Bhattacharya J., Peters P.J., Clapham P.R.
J. Virol. 78:5500-5506(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE OF PALMITOYLATION, MUTAGENESIS OF CYS-769.
Strain: Clone pNL4-3.
[10]"Role of protein disulfide isomerase and other thiol-reactive proteins in HIV-1 envelope protein-mediated fusion."
Ou W., Silver J.
Virology 350:406-417(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY HUMAN TXN.
Strain: Clone pNL4-3.
[11]"Only five of 10 strictly conserved disulfide bonds are essential for folding and eight for function of the HIV-1 envelope glycoprotein."
van Anken E., Sanders R.W., Liscaljet I.M., Land A., Bontjer I., Tillemans S., Nabatov A.A., Paxton W.A., Berkhout B., Braakman I.
Mol. Biol. Cell 19:4298-4309(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[12]"HIV-1 envelope protein binds to and signals through integrin alpha4beta7, the gut mucosal homing receptor for peripheral T cells."
Arthos J., Cicala C., Martinelli E., Macleod K., Van Ryk D., Wei D., Xiao Z., Veenstra T.D., Conrad T.P., Lempicki R.A., McLaughlin S., Pascuccio M., Gopaul R., McNally J., Cruz C.C., Censoplano N., Chung E., Reitano K.N. expand/collapse author list , Kottilil S., Goode D.J., Fauci A.S.
Nat. Immunol. 9:301-309(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION OF GP120 WITH HUMAN ITGA4/ITGB7 HETERODIMER, MUTAGENESIS OF 184-LEU-ASP-185.
Strain: Clone pNL4-3.
[13]"Pathogens target DC-SIGN to influence their fate DC-SIGN functions as a pathogen receptor with broad specificity."
Geijtenbeek T.B., van Kooyk Y.
APMIS 111:698-714(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[14]"The HIV Env-mediated fusion reaction."
Gallo S.A., Finnegan C.M., Viard M., Raviv Y., Dimitrov A., Rawat S.S., Puri A., Durell S., Blumenthal R.
Biochim. Biophys. Acta 1614:36-50(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[15]"Mechanisms of apoptosis induction by the HIV-1 envelope."
Perfettini J.-L., Castedo M., Roumier T., Andreau K., Nardacci R., Piacentini M., Kroemer G.
Cell Death Differ. 12:916-923(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[16]"V3: HIV's switch-hitter."
Hartley O., Klasse P.J., Sattentau Q.J., Moore J.P.
AIDS Res. Hum. Retroviruses 21:171-189(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[17]"Emerging drug targets for antiretroviral therapy."
Reeves J.D., Piefer A.J.
Drugs 65:1747-1766(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[18]"HIV and the chemokine system: 10 years later."
Lusso P.
EMBO J. 25:447-456(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[19]"The structure of an HIV-1 specific cell entry inhibitor in complex with the HIV-1 gp41 trimeric core."
Zhou G., Ferrer M., Chopra R., Kapoor T.M., Strassmaier T., Weissenhorn W., Skehel J.J., Oprian D., Schreiber S.L., Harrison S.C., Wiley D.C.
Bioorg. Med. Chem. 8:2219-2227(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 537-670.
[20]"Conformational mapping of the N-terminal peptide of HIV-1 gp41 in membrane environments using (13)C-enhanced Fourier transform infrared spectroscopy."
Gordon L.M., Mobley P.W., Pilpa R., Sherman M.A., Waring A.J.
Biochim. Biophys. Acta 1559:96-120(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY FTIR OF 517-539.
[21]"Conformational mapping of the N-terminal peptide of HIV-1 gp41 in lipid detergent and aqueous environments using 13C-enhanced Fourier transform infrared spectroscopy."
Gordon L.M., Mobley P.W., Lee W., Eskandari S., Kaznessis Y.N., Sherman M.A., Waring A.J.
Protein Sci. 13:1012-1030(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY FTIR OF 517-539.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02013 Genomic RNA. Translation: AAB59751.1.
A04321 Unassigned RNA. Translation: CAA00352.1.
M19921 Genomic RNA. Translation: AAA44992.2.
PIRVCLJLV. A03975.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ENVX-ray2.60A546-670[»]
1ERFinfrared-A517-539[»]
1FAVX-ray3.00A546-595[»]
C641-670[»]
1P5Ainfrared-A517-539[»]
1U6UNMR-A310-326[»]
1U6VNMR-A310-326[»]
2ZZOX-ray2.20C633-666[»]
N551-586[»]
3G9RX-ray2.00A/B/C/D/E/F667-689[»]
3MNWX-ray2.20P657-676[»]
3VGXX-ray1.74C558-595[»]
D626-657[»]
3VTPX-ray1.90C555-595[»]
D631-666[»]
ProteinModelPortalP03377.
SMRP03377. Positions 84-133, 200-497, 537-670.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP03377.
ChEMBLCHEMBL5826.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.170.40.20. 2 hits.
InterProIPR000777. HIV1_GP160.
IPR000328. Retroviral_envelope_protein.
[Graphical view]
PfamPF00516. GP120. 1 hit.
PF00517. GP41. 1 hit.
[Graphical view]
SUPFAMSSF56502. SSF56502. 3 hits.
ProtoNetSearch...

Other

EvolutionaryTraceP03377.

Entry information

Entry nameENV_HV1BR
AccessionPrimary (citable) accession number: P03377
Secondary accession number(s): Q85582
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references