P03375 (ENV_HV1B1) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Human immunodeficiency virus type 1 group M subtype B (isolate BH10) (HIV-1) [Complete proteome]

Taxonomic identifier

11678 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Lentivirus › Primate lentivirus group › Human immunodeficiency virus 1 › HIV-1 unknown group

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	856 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.5 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.5 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.5 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.5 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.5 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.5 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.5
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.5 Ref.6
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. Ref.4 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 By similarity.
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).

Ontologies

Keywords
Biological process	Apoptosis 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 component	Host cell membrane Host endosome Host membrane Membrane Viral envelope protein Virion
Disease	AIDS
Domain	Coiled coil Signal Transmembrane Transmembrane helix
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW entry into host cell Traceable author statement. Source: Reactome evasion or tolerance by virus of host immune response Inferred from electronic annotation. Source: UniProtKB-KW innate immune response Traceable author statement. Source: Reactome viral attachment to host cell Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell via clathrin-mediated endocytosis Inferred from electronic annotation. Source: UniProtKB-KW viral reproduction Traceable author statement. Source: Reactome
Cellular_component	host cell endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW viral envelope Traceable author statement. Source: Reactome virion membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

By similarity

Chain

33 – 856

824

Envelope glycoprotein gp160

PRO_0000239239

Chain

33 – 511

479

Surface protein gp120 By similarity

PRO_0000038371

Chain

512 – 856

345

Transmembrane protein gp41 By similarity

PRO_0000038372

Regions

Topological domain

33 – 684

652

Extracellular Potential

Transmembrane

685 – 705

21

Helical; Potential

Topological domain

706 – 856

151

Cytoplasmic Potential

Region

131 – 156

26

V1

Region

157 – 196

40

V2

Region

296 – 330

35

V3

Region

364 – 374

11

CD4-binding loop By similarity

Region

385 – 418

34

V4

Region

461 – 471

11

V5

Region

512 – 532

21

Fusion peptide Potential

Region

576 – 592

17

Immunosuppression By similarity

Region

662 – 683

22

MPER; binding to GalCer By similarity

Region

662 – 667

6

Involved in GalCer binding

Coiled coil

633 – 667

35

Potential

Motif

712 – 715

4

YXXL motif; contains endocytosis signal By similarity

Motif

855 – 856

2

Di-leucine internalization motif By similarity

Sites

Site

511 – 512

2

Cleavage; by host furin By similarity

Amino acid modifications

Lipidation

764

1

S-palmitoyl cysteine; by host By similarity

Glycosylation

88

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

136

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

141

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

156

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

160

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

186

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

197

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

230

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

234

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

241

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

262

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

276

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

289

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

295

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

301

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

332

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

339

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

356

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

386

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

392

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

397

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

406

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

448

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

463

1

N-linked (GlcNAc...); by host Ref.4

Glycosylation

611

1

N-linked (GlcNAc...); by host Potential

Glycosylation

616

1

N-linked (GlcNAc...); by host Potential

Glycosylation

625

1

N-linked (GlcNAc...); by host Potential

Glycosylation

637

1

N-linked (GlcNAc...); by host Potential

Glycosylation

674

1

N-linked (GlcNAc...); by host Potential

Disulfide bond

54 ↔ 74

Ref.4 Ref.7 Ref.8 Ref.9 Ref.10

Disulfide bond

119 ↔ 205

Ref.4 Ref.7 Ref.8 Ref.9 Ref.10

Disulfide bond

126 ↔ 196

Ref.4 Ref.7 Ref.8 Ref.9 Ref.10

Disulfide bond

131 ↔ 157

Ref.4 Ref.7 Ref.8 Ref.9 Ref.10

Disulfide bond

218 ↔ 247

Ref.4 Ref.7 Ref.8 Ref.9 Ref.10

Disulfide bond

228 ↔ 239

Ref.4 Ref.7 Ref.8 Ref.9 Ref.10

Disulfide bond

296 ↔ 331

Ref.4 Ref.7 Ref.8 Ref.9 Ref.10

Disulfide bond

378 ↔ 445

Ref.4 Ref.7 Ref.8 Ref.9 Ref.10

Disulfide bond

385 ↔ 418

Ref.4 Ref.7 Ref.8 Ref.9 Ref.10

Natural variations

Natural variant

403

1

K → E in strain: Isolate PV22.

Natural variant

423

1

I → F in strain: Isolate PV22.

Natural variant

461

1

S → N in strain: Isolate PV22.

Natural variant

668

1

S → N in strain: Isolate PV22.

Natural variant

673

1

F → L in strain: Isolate PV22.

Natural variant

704

1

V → I in strain: Isolate PV22.

Natural variant

723

1

I → T in strain: Isolate PV22.

Natural variant

737

1

G → D in strain: Isolate PV22.

Secondary structure

1

.

.

.

.

.

.

.

.

856

Helix Strand Turn

Details...

Helix

516 – 530

15

Turn

531 – 533

3

Beta strand

536 – 538

3

Helix

546 – 588

43

Sequences

	Sequence		Length	Mass (Da)
	P03375 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 0BFFB1A18931BB27	FASTA	856	97,225
	10 20 30 40 50 60 MRVKEKYQHL WRWGWRWGTM LLGMLMICSA TEKLWVTVYY GVPVWKEATT TLFCASDAKA 70 80 90 100 110 120 YDTEVHNVWA THACVPTDPN PQEVVLVNVT ENFNMWKNDM VEQMHEDIIS LWDQSLKPCV 130 140 150 160 170 180 KLTPLCVSLK CTDLKNDTNT NSSSGRMIME KGEIKNCSFN ISTSIRGKVQ KEYAFFYKLD 190 200 210 220 230 240 IIPIDNDTTS YTLTSCNTSV ITQACPKVSF EPIPIHYCAP AGFAILKCNN KTFNGTGPCT 250 260 270 280 290 300 NVSTVQCTHG IRPVVSTQLL LNGSLAEEEV VIRSANFTDN AKTIIVQLNQ SVEINCTRPN 310 320 330 340 350 360 NNTRKSIRIQ RGPGRAFVTI GKIGNMRQAH CNISRAKWNN TLKQIDSKLR EQFGNNKTII 370 380 390 400 410 420 FKQSSGGDPE IVTHSFNCGG EFFYCNSTQL FNSTWFNSTW STKGSNNTEG SDTITLPCRI 430 440 450 460 470 480 KQIINMWQEV GKAMYAPPIS GQIRCSSNIT GLLLTRDGGN SNNESEIFRP GGGDMRDNWR 490 500 510 520 530 540 SELYKYKVVK IEPLGVAPTK AKRRVVQREK RAVGIGALFL GFLGAAGSTM GAASMTLTVQ 550 560 570 580 590 600 ARQLLSGIVQ QQNNLLRAIE AQQHLLQLTV WGIKQLQARI LAVERYLKDQ QLLGIWGCSG 610 620 630 640 650 660 KLICTTAVPW NASWSNKSLE QIWNNMTWME WDREINNYTS LIHSLIEESQ NQQEKNEQEL 670 680 690 700 710 720 LELDKWASLW NWFNITNWLW YIKLFIMIVG GLVGLRIVFA VLSVVNRVRQ GYSPLSFQTH 730 740 750 760 770 780 LPIPRGPDRP EGIEEEGGER DRDRSIRLVN GSLALIWDDL RSLCLFSYHR LRDLLLIVTR 790 800 810 820 830 840 IVELLGRRGW EALKYWWNLL QYWSQELKNS AVSLLNATAI AVAEGTDRVI EVVQGAYRAI 850 RHIPRRIRQG LERILL

References

[1]	"Complete nucleotide sequence of the AIDS virus, HTLV-III." Ratner L., Haseltine W.A., Patarca R., Livak K.J., Starcich B.R., Josephs S.F., Doran E.R., Rafalski J.A., Whitehorn E.A., Baumeister K., Ivanoff L., Petteway S.R. Jr., Pearson M.L., Lautenberger J.A., Papas T.S., Ghrayeb J., Chang N.T., Gallo R.C., Wong-Staal F. Nature 313:277-284(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Nucleic acid structure and expression of the human AIDS/lymphadenopathy retrovirus." Muesing M.A., Smith D.H., Cabradilla C.D., Benton C.V., Lasky L.A., Capon D.J. Nature 313:450-458(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Isolate PV22.
[3]	"Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus." McCune J.M., Rabin L.B., Feinberg M.B., Lieberman M., Kosek J.C., Reyes G.R., Weissman I.L. Cell 53:55-67(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[4]	"Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells." Leonard C.K., Spellman M.W., Riddle L., Harris R.J., Thomas J.N., Gregory T.J. J. Biol. Chem. 265:10373-10382(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF C-TERMINUS, DISULFIDE BONDS, GLYCOSYLATION AT ASN-88; ASN-136; ASN-141; ASN-156; ASN-160; ASN-186; ASN-197; ASN-230; ASN-234; ASN-241; ASN-262; ASN-276; ASN-289; ASN-295; ASN-301; ASN-332; ASN-339; ASN-356; ASN-386; ASN-392; ASN-397; ASN-406; ASN-448 AND ASN-463, STRUCTURE OF CARBOHYDRATES.
[5]	"CD4 is retained in the endoplasmic reticulum by the human immunodeficiency virus type 1 glycoprotein precursor." Crise B., Buonocore L., Rose J.K. J. Virol. 64:5585-5593(1990) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION OF ENVELOPE GLYCOPROTEIN GP160 WITH CD4.
[6]	"Secretory IgA specific for a conserved epitope on gp41 envelope glycoprotein inhibits epithelial transcytosis of HIV-1." Alfsen A., Iniguez P., Bouguyon E., Bomsel M. J. Immunol. 166:6257-6265(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION OF TRANSMEMBRANE PROTEIN GP41 WITH GALACTOSYL CERAMIDE.
[7]	"The catalytic activity of protein disulfide isomerase is involved in human immunodeficiency virus envelope-mediated membrane fusion after CD4 cell binding." Fenouillet E., Barbouche R., Courageot J., Miquelis R. J. Infect. Dis. 183:744-752(2001) [PubMed] [Europe PMC] [Abstract] Cited for: REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY P4HB/PDI.
[8]	"Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion." Barbouche R., Miquelis R., Jones I.M., Fenouillet E. J. Biol. Chem. 278:3131-3136(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY P4HB/PDI.
[9]	"Thiol/disulfide exchange is a prerequisite for CXCR4-tropic HIV-1 envelope-mediated T-cell fusion during viral entry." Markovic I., Stantchev T.S., Fields K.H., Tiffany L.J., Tomic M., Weiss C.D., Broder C.C., Strebel K., Clouse K.A. Blood 103:1586-1594(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY P4HB/PDI.
[10]	"Glycosaminoglycans and protein disulfide isomerase-mediated reduction of HIV Env." Barbouche R., Lortat-Jacob H., Jones I.M., Fenouillet E. Mol. Pharmacol. 67:1111-1118(2005) [PubMed] [Europe PMC] [Abstract] Cited for: REDUCTION OF SURFACE PROTEIN GP120 DISULFIDE BONDS BY P4HB/PDI.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"Emerging drug targets for antiretroviral therapy." Reeves J.D., Piefer A.J. Drugs 65:1747-1766(2005) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[16]	"HIV and the chemokine system: 10 years later." Lusso P. EMBO J. 25:447-456(2006) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
+	Additional computationally mapped references.

Web resources

hivdb

HIV drug resistance database

BioAfrica: HIV bioinformatics in Africa

HIV drug resistance mutations

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M15654 Genomic RNA. Translation: AAA44205.1.
K02083 Genomic DNA. Translation: AAB59873.1.
X01762 Genomic RNA. Translation: CAA25903.1. Sequence problems.

PIR

VCLJH3. A03973.
VCLJVL. A03974.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ARI	NMR	-	A	512-541	[»]
3VGY	X-ray	2.03	C	546-588	[»]
3VH7	X-ray	2.02	A/C/E	546-588	[»]
3VU5	X-ray	2.09	A	553-590	[»]
3VU6	X-ray	2.32	A	553-590	[»]

ProteinModelPortal

P03375.

SMR

P03375. Positions 83-127, 195-492, 512-665.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_6900. Immune System.

Family and domain databases

Gene3D

2.170.40.20. 2 hits.

InterPro

IPR000777. HIV1_GP160.
IPR000328. Retroviral_envelope_protein.
[Graphical view]

Pfam

PF00516. GP120. 1 hit.
PF00517. GP41. 1 hit.
[Graphical view]

SUPFAM

SSF56502. GP120. 1 hit.

ProtoNet

Search...

Other

ChEMBL

CHEMBL5057.

EvolutionaryTrace

P03375.

PMAP-CutDB

P03376.

Entry information

Entry name

ENV_HV1B1

Accession

Primary (citable) accession number: P03375
Secondary accession number(s): P03376

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program