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Protein

Envelope glycoprotein gp160

Gene

env

Organism
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Envelope glycoprotein gp160: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41.UniRule annotation2 Publications
Surface protein gp120: 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. Acts as 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. 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.UniRule annotation2 Publications
Transmembrane protein gp41: 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.UniRule annotation2 Publications

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.UniRule annotation
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).UniRule annotation

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • structural molecule activity Source: InterPro

GO - Biological processi

  • actin filament reorganization Source: UniProtKB
  • clathrin-dependent endocytosis of virus by host cell Source: UniProtKB
  • entry into host cell Source: Reactome
  • evasion or tolerance by virus of host immune response Source: UniProtKB-KW
  • fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
  • fusion of virus membrane with host plasma membrane Source: UniProtKB
  • positive regulation of establishment of T cell polarity Source: UniProtKB
  • positive regulation of plasma membrane raft polarization Source: UniProtKB
  • positive regulation of receptor clustering Source: UniProtKB
  • stimulatory C-type lectin receptor signaling pathway Source: Reactome
  • viral life cycle Source: Reactome
  • viral protein processing Source: UniProtKB
  • virion assembly Source: Reactome
  • virion attachment to host cell Source: UniProtKB

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-HSA-1462054. Alpha-defensins.
R-HSA-162588. Budding and maturation of HIV virion.
R-HSA-171286. Synthesis and processing of ENV and VPU.
R-HSA-173107. Binding and entry of HIV virion.
R-HSA-175474. Assembly Of The HIV Virion.
R-HSA-5621480. Dectin-2 family.

Protein family/group databases

TCDBi1.G.16.1.3. the human immunodeficiency virus type 1 (hiv-1) fusion peptide (hiv-fp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein gp160UniRule annotation
Alternative name(s):
Env polyproteinUniRule annotation
Cleaved into the following 2 chains:
Surface protein gp120UniRule annotation
Short name:
SUUniRule annotation
Alternative name(s):
Glycoprotein 120UniRule annotation
Short name:
gp120UniRule annotation
Transmembrane protein gp41UniRule annotation
Short name:
TMUniRule annotation
Alternative name(s):
Glycoprotein 41UniRule annotation
Short name:
gp41UniRule annotation
Gene namesi
Name:envUniRule annotation
OrganismiHuman immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Taxonomic identifieri11706 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000105453 Componenti: Genome
  • UP000002241 Componenti: Genome

Subcellular locationi

Surface protein gp120 :
  • Virion membrane UniRule annotation; Peripheral membrane protein UniRule annotation
  • Host cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation
  • Host endosome membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • 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.UniRule annotation
Transmembrane protein gp41 :
  • Virion membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Host cell membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • Host endosome membrane UniRule annotation; Single-pass type I membrane protein UniRule annotation
  • 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.UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini33 – 684ExtracellularUniRule annotationAdd BLAST652
Transmembranei685 – 705HelicalUniRule annotationAdd BLAST21
Topological domaini706 – 856CytoplasmicUniRule annotationAdd BLAST151

GO - Cellular componenti

  • cytosol Source: Reactome
  • endoplasmic reticulum membrane Source: Reactome
  • Golgi membrane Source: Reactome
  • host cell endosome membrane Source: UniProtKB-SubCell
  • host cell plasma membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • viral envelope Source: Reactome
  • virion Source: UniProtKB
  • virion membrane Source: UniProtKB-SubCell

Keywords - Cellular componenti

Host cell membrane, Host endosome, Host membrane, Membrane, Viral envelope protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi764C → S: Complete loss of palmitoylation, decreased association with host cell membrane lipid rafts, decreased incorporation onto virions and severe reduction of infectivity; when associated with S-837. 1 Publication1
Mutagenesisi837C → S: Complete loss of palmitoylation, decreased association with host cell membrane lipid rafts, decreased incorporation onto virions and severe reduction of infectivity; when associated with S-764. 1 Publication1

Keywords - Diseasei

AIDS

Chemistry databases

ChEMBLiCHEMBL3520.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32UniRule annotationAdd BLAST32
ChainiPRO_000023924033 – 856Envelope glycoprotein gp160UniRule annotationAdd BLAST824
ChainiPRO_000003842733 – 511Surface protein gp120UniRule annotationAdd BLAST479
ChainiPRO_0000038428512 – 856Transmembrane protein gp41UniRule annotationAdd BLAST345

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi54 ↔ 74UniRule annotation
Glycosylationi88N-linked (GlcNAc...) asparagine; by hostUniRule annotation2 Publications1
Disulfide bondi119 ↔ 205UniRule annotation
Disulfide bondi126 ↔ 196UniRule annotation
Disulfide bondi131 ↔ 157UniRule annotation
Glycosylationi136N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi141N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi156N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication1
Glycosylationi160N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication1
Glycosylationi186N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi197N-linked (GlcNAc...) asparagine; by hostUniRule annotation4 Publications1
Disulfide bondi218 ↔ 247UniRule annotation
Disulfide bondi228 ↔ 239UniRule annotation
Glycosylationi230N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi234N-linked (GlcNAc...) asparagine; by hostUniRule annotation3 Publications1
Glycosylationi241N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi262N-linked (GlcNAc...) asparagine; by hostUniRule annotation5 Publications1
Glycosylationi276N-linked (GlcNAc...) asparagine; by hostUniRule annotation4 Publications1
Glycosylationi289N-linked (GlcNAc...) asparagine; by hostUniRule annotation3 Publications1
Glycosylationi295N-linked (GlcNAc...) asparagine; by hostUniRule annotation4 Publications1
Disulfide bondi296 ↔ 331UniRule annotation
Glycosylationi301N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi332N-linked (GlcNAc...) asparagine; by hostUniRule annotation3 Publications1
Glycosylationi339N-linked (GlcNAc...) asparagine; by hostUniRule annotation3 Publications1
Glycosylationi356N-linked (GlcNAc...) asparagine; by hostUniRule annotationCombined sources2 Publications1
Disulfide bondi378 ↔ 445UniRule annotation
Disulfide bondi385 ↔ 418UniRule annotation
Glycosylationi386N-linked (GlcNAc...) asparagine; by hostUniRule annotation3 Publications1
Glycosylationi392N-linked (GlcNAc...) asparagine; by hostUniRule annotation4 Publications1
Glycosylationi397N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi406N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi448N-linked (GlcNAc...) asparagine; by hostUniRule annotation4 Publications1
Glycosylationi463N-linked (GlcNAc...) asparagine; by hostUniRule annotation2 Publications1
Disulfide bondi598 ↔ 604UniRule annotation
Glycosylationi611N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication1
Glycosylationi616N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi624N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi637N-linked (GlcNAc...) asparagine; by hostUniRule annotation1 Publication1
Glycosylationi674N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Lipidationi764S-palmitoyl cysteine; by hostUniRule annotation1 Publication1
Lipidationi837S-palmitoyl cysteine; by hostUniRule annotation1 Publication1

Post-translational modificationi

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.UniRule annotation1 Publication
Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system.UniRule annotation2 Publications
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.UniRule annotation2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei511 – 512Cleavage; by host furinUniRule annotation2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

PTM databases

iPTMnetiP04578.
SwissPalmiP04578.

Interactioni

Subunit structurei

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 host CD4, CCR5 and CXCR4. 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 host ITGA4/ITGB7 complex; on CD4+ T-cells, this interaction results in rapid activation of integrin ITGAL/LFA-1, which facilitates 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.UniRule annotation3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi1205544. 155 interactors.
DIPiDIP-58525N.
IntActiP04578. 155 interactors.
MINTiMINT-7968605.

Chemistry databases

BindingDBiP04578.

Structurei

Secondary structure

1856
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi84 – 86Combined sources3
Beta strandi91 – 94Combined sources4
Turni95 – 98Combined sources4
Turni100 – 103Combined sources4
Helixi108 – 110Combined sources3
Beta strandi112 – 114Combined sources3
Beta strandi120 – 122Combined sources3
Beta strandi199 – 202Combined sources4
Beta strandi210 – 212Combined sources3
Beta strandi223 – 228Combined sources6
Beta strandi235 – 247Combined sources13
Beta strandi251 – 254Combined sources4
Beta strandi256 – 262Combined sources7
Beta strandi267 – 269Combined sources3
Beta strandi271 – 273Combined sources3
Beta strandi277 – 279Combined sources3
Beta strandi284 – 297Combined sources14
Turni312 – 314Combined sources3
Beta strandi330 – 334Combined sources5
Helixi335 – 352Combined sources18
Beta strandi358 – 361Combined sources4
Helixi369 – 372Combined sources4
Beta strandi374 – 378Combined sources5
Beta strandi381 – 385Combined sources5
Helixi388 – 390Combined sources3
Beta strandi393 – 395Combined sources3
Beta strandi413 – 417Combined sources5
Beta strandi420 – 425Combined sources6
Beta strandi427 – 430Combined sources4
Beta strandi432 – 434Combined sources3
Turni440 – 442Combined sources3
Beta strandi444 – 456Combined sources13
Beta strandi463 – 470Combined sources8
Helixi475 – 483Combined sources9
Beta strandi486 – 490Combined sources5
Helixi549 – 577Combined sources29
Helixi583 – 594Combined sources12
Helixi595 – 601Combined sources7
Turni602 – 605Combined sources4
Helixi626 – 628Combined sources3
Helixi629 – 650Combined sources22
Helixi657 – 667Combined sources11
Helixi672 – 674Combined sources3
Helixi675 – 683Combined sources9
Helixi690 – 693Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AIKX-ray2.00C628-661[»]
N546-581[»]
1DF4X-ray1.45A546-579[»]
A628-655[»]
1DF5X-ray2.70A546-579[»]
A628-655[»]
1DLBX-ray2.00A546-579[»]
A628-655[»]
1G9MX-ray2.20G83-127[»]
G195-297[»]
G330-492[»]
1GC1X-ray2.50G83-127[»]
G195-297[»]
G330-396[»]
G410-492[»]
1GZLX-ray1.80A/B565-581[»]
C/D628-639[»]
1K33X-ray1.75A546-579[»]
A628-655[»]
1K34X-ray1.88A546-579[»]
A628-655[»]
1MZINMR-A659-671[»]
1OPNmodel-G156-492[»]
1OPTmodel-G156-492[»]
1OPWmodel-G156-492[»]
1RZJX-ray2.20G195-492[»]
2CMRX-ray2.00A543-662[»]
2ME1NMR-A657-683[»]
2MG1NMR-A683-704[»]
2MG2NMR-A675-693[»]
2MG3NMR-A675-693[»]
2NY7X-ray2.30G83-492[»]
2PV6NMR-A662-683[»]
2XRAX-ray2.30A543-662[»]
3D0VX-ray2.05C660-670[»]
3DNLelectron microscopy20.00A/D/G90-124[»]
B/E/H198-297[»]
B/E/H330-396[»]
C/F/I410-492[»]
3DNNelectron microscopy20.00A/D/G90-124[»]
B/E/H198-297[»]
B/E/H330-396[»]
C/F/I410-492[»]
3DNOelectron microscopy20.00A/D/G90-124[»]
B/E/H198-297[»]
B/E/H330-396[»]
C/F/I410-492[»]
3DROX-ray3.90P659-671[»]
3IDXX-ray2.50G83-492[»]
3IDYX-ray3.20A/G83-492[»]
3J70electron microscopy-D/P/U31-500[»]
3MNZX-ray1.80P653-671[»]
3TYGX-ray3.25A254-297[»]
A330-401[»]
3VIEX-ray1.80A/C/E546-581[»]
4JPJX-ray2.50A/B/C/D254-399[»]
4JPKX-ray2.40A254-399[»]
4YDVX-ray2.70P/Q596-606[»]
4ZTOX-ray2.30P/Q430-444[»]
5BN0X-ray2.80A/C/D627-661[»]
B/E/N546-581[»]
5C0RX-ray3.19A546-577[»]
A628-654[»]
5C0SX-ray4.30A546-577[»]
A630-654[»]
5CILX-ray1.81P671-683[»]
5CINX-ray1.70P671-683[»]
5CMUX-ray2.11A/B/C546-635[»]
5CMZX-ray2.57A/C546-590[»]
5CN0X-ray1.90A546-581[»]
5DD0X-ray2.49P660-670[»]
5GHWX-ray2.40P664-690[»]
5H0NX-ray2.80A/C/E/G/I/K536-581[»]
5HFLX-ray2.29A/B/C/D/E/F546-581[»]
5HM1X-ray2.96D/E/F582-596[»]
5IVXX-ray2.10P311-320[»]
5KA5X-ray1.80A543-582[»]
A625-661[»]
5KA6X-ray1.85A/B/C543-582[»]
A/B/C625-661[»]
5X08X-ray1.49P671-683[»]
DisProtiDP00976.
ProteinModelPortaliP04578.
SMRiP04578.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04578.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni131 – 156V1UniRule annotationAdd BLAST26
Regioni157 – 196V2UniRule annotationAdd BLAST40
Regioni296 – 330V3UniRule annotationAdd BLAST35
Regioni364 – 374CD4-binding loopUniRule annotationAdd BLAST11
Regioni385 – 418V4UniRule annotationAdd BLAST34
Regioni461 – 471V5Add BLAST11
Regioni463 – 471V5UniRule annotation9
Regioni512 – 532Fusion peptideUniRule annotationAdd BLAST21
Regioni574 – 592ImmunosuppressionUniRule annotation1 PublicationAdd BLAST19
Regioni662 – 683MPER; binding to GalCerUniRule annotationAdd BLAST22

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili633 – 667UniRule annotationAdd BLAST35

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi712 – 715YXXL motif; contains endocytosis signalUniRule annotation4
Motifi855 – 856Di-leucine internalization motifUniRule annotation2

Domaini

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.UniRule annotation1 Publication
The membrane proximal external region (MPER) present in gp41 is a tryptophan-rich region recognized by the antibodies 2F5, Z13, and 4E10. MPER seems to play a role in fusion.UniRule annotation1 Publication
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.UniRule annotation1 Publication
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.UniRule annotation1 Publication
The CD4-binding region is targeted by the antibody b12.UniRule annotation1 Publication

Sequence similaritiesi

Belongs to the HIV-1 env protein family.UniRule annotation

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK19287.
OrthoDBiVOG09000036.

Family and domain databases

CDDicd09909. HIV-1-like_HR1-HR2. 1 hit.
Gene3Di2.170.40.20. 2 hits.
HAMAPiMF_04083. HIV_ENV. 1 hit.
InterProiView protein in InterPro
IPR036377. Gp120_core_sf.
IPR000328. GP41-like.
IPR000777. HIV1_Gp120.
PfamiView protein in Pfam
PF00516. GP120. 1 hit.
PF00517. GP41. 1 hit.
SUPFAMiSSF56502. SSF56502. 3 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04578-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVKEKYQHL WRWGWRWGTM LLGMLMICSA TEKLWVTVYY GVPVWKEATT
60 70 80 90 100
TLFCASDAKA YDTEVHNVWA THACVPTDPN PQEVVLVNVT ENFNMWKNDM
110 120 130 140 150
VEQMHEDIIS LWDQSLKPCV KLTPLCVSLK CTDLKNDTNT NSSSGRMIME
160 170 180 190 200
KGEIKNCSFN ISTSIRGKVQ KEYAFFYKLD IIPIDNDTTS YKLTSCNTSV
210 220 230 240 250
ITQACPKVSF EPIPIHYCAP AGFAILKCNN KTFNGTGPCT NVSTVQCTHG
260 270 280 290 300
IRPVVSTQLL LNGSLAEEEV VIRSVNFTDN AKTIIVQLNT SVEINCTRPN
310 320 330 340 350
NNTRKRIRIQ RGPGRAFVTI GKIGNMRQAH CNISRAKWNN TLKQIASKLR
360 370 380 390 400
EQFGNNKTII FKQSSGGDPE IVTHSFNCGG EFFYCNSTQL FNSTWFNSTW
410 420 430 440 450
STEGSNNTEG SDTITLPCRI KQIINMWQKV GKAMYAPPIS GQIRCSSNIT
460 470 480 490 500
GLLLTRDGGN SNNESEIFRP GGGDMRDNWR SELYKYKVVK IEPLGVAPTK
510 520 530 540 550
AKRRVVQREK RAVGIGALFL GFLGAAGSTM GAASMTLTVQ ARQLLSGIVQ
560 570 580 590 600
QQNNLLRAIE AQQHLLQLTV WGIKQLQARI LAVERYLKDQ QLLGIWGCSG
610 620 630 640 650
KLICTTAVPW NASWSNKSLE QIWNHTTWME WDREINNYTS LIHSLIEESQ
660 670 680 690 700
NQQEKNEQEL LELDKWASLW NWFNITNWLW YIKLFIMIVG GLVGLRIVFA
710 720 730 740 750
VLSIVNRVRQ GYSPLSFQTH LPTPRGPDRP EGIEEEGGER DRDRSIRLVN
760 770 780 790 800
GSLALIWDDL RSLCLFSYHR LRDLLLIVTR IVELLGRRGW EALKYWWNLL
810 820 830 840 850
QYWSQELKNS AVSLLNATAI AVAEGTDRVI EVVQGACRAI RHIPRRIRQG

LERILL
Length:856
Mass (Da):97,213
Last modified:July 15, 1999 - v2
Checksum:i6FAB16AF85107FE0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K03455 Genomic RNA. Translation: AAB50262.1.
AF038399 Genomic DNA. Translation: AAB99976.1.
AF033819 Genomic RNA. Translation: AAC82596.1.
RefSeqiNP_057856.1. NC_001802.1.

Genome annotation databases

GeneIDi155971.
KEGGivg:155971.

Similar proteinsi

Entry informationi

Entry nameiENV_HV1H2
AccessioniPrimary (citable) accession number: P04578
Secondary accession number(s): O09779
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: July 15, 1999
Last modified: November 22, 2017
This is version 162 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families