UniProtKB - Q70626 (ENV_HV1LW)
Envelope glycoprotein gp160
env
Functioni
Miscellaneous
GO - Molecular functioni
- structural molecule activity Source: UniProtKB-UniRule
GO - Biological processi
- actin filament reorganization Source: UniProtKB-UniRule
- clathrin-dependent endocytosis of virus by host cell Source: UniProtKB
- fusion of virus membrane with host endosome membrane Source: UniProtKB-UniRule
- fusion of virus membrane with host plasma membrane Source: UniProtKB
- mitigation of host immune response by virus Source: UniProtKB-UniRule
- positive regulation of establishment of T cell polarity Source: UniProtKB-UniRule
- positive regulation of plasma membrane raft polarization Source: UniProtKB-UniRule
- positive regulation of receptor clustering Source: UniProtKB-UniRule
- stimulatory C-type lectin receptor signaling pathway Source: Reactome
- viral protein processing Source: UniProtKB
- virion attachment to host cell Source: UniProtKB
Keywordsi
Enzyme and pathway databases
Reactomei | R-HSA-5621480, Dectin-2 family |
Names & Taxonomyi
Protein namesi | Recommended name: Envelope glycoprotein gp160UniRule annotationAlternative name(s): Env polyproteinUniRule annotation Cleaved into the following 2 chains: Alternative name(s): Glycoprotein 120UniRule annotation Short name: gp120UniRule annotation Alternative name(s): Glycoprotein 41UniRule annotation Short name: gp41UniRule annotation |
Gene namesi | Name:envUniRule annotation |
Organismi | Human immunodeficiency virus type 1 group M subtype B (isolate LW123) (HIV-1) |
Taxonomic identifieri | 82834 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Pararnavirae › Artverviricota › Revtraviricetes › Ortervirales › Retroviridae › Orthoretrovirinae › Lentivirus › |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] |
Subcellular locationi
- 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
- 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 33 – 684 | ExtracellularUniRule annotationAdd BLAST | 652 | |
Transmembranei | 685 – 705 | HelicalUniRule annotationAdd BLAST | 21 | |
Topological domaini | 706 – 856 | CytoplasmicUniRule annotationAdd BLAST | 151 |
GO - Cellular componenti
- host cell endosome membrane Source: UniProtKB-SubCell
- host cell plasma membrane Source: UniProtKB
- integral component of membrane Source: UniProtKB-UniRule
- viral envelope Source: UniProtKB-KW
- virion Source: UniProtKB
- virion membrane Source: UniProtKB-SubCell
Keywords - Cellular componenti
Host cell membrane, Host endosome, Host membrane, Membrane, Viral envelope protein, VirionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 32 | UniRule annotationAdd BLAST | 32 | |
ChainiPRO_0000239467 | 33 – 856 | Envelope glycoprotein gp160UniRule annotationAdd BLAST | 824 | |
ChainiPRO_0000038373 | 33 – 511 | Surface protein gp120UniRule annotationAdd BLAST | 479 | |
ChainiPRO_0000038374 | 512 – 856 | Transmembrane protein gp41UniRule annotationAdd BLAST | 345 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 54 ↔ 74 | UniRule annotation | ||
Glycosylationi | 88 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Disulfide bondi | 119 ↔ 205 | UniRule annotation | ||
Disulfide bondi | 126 ↔ 196 | UniRule annotation | ||
Disulfide bondi | 131 ↔ 157 | UniRule annotation | ||
Glycosylationi | 136 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 141 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 156 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 160 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 186 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 197 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Disulfide bondi | 218 ↔ 247 | UniRule annotation | ||
Disulfide bondi | 228 ↔ 239 | UniRule annotation | ||
Glycosylationi | 230 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 234 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 241 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 262 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 276 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 289 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 295 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Disulfide bondi | 296 ↔ 331 | UniRule annotation | ||
Glycosylationi | 301 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 332 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 339 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 356 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Disulfide bondi | 378 ↔ 445 | UniRule annotation | ||
Disulfide bondi | 385 ↔ 418 | UniRule annotation | ||
Glycosylationi | 386 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 392 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 397 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 406 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 448 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 463 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Disulfide bondi | 598 ↔ 604 | UniRule annotation | ||
Glycosylationi | 611 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 616 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 624 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 637 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Glycosylationi | 674 | N-linked (GlcNAc...) asparagine; by hostUniRule annotation | 1 | |
Lipidationi | 764 | S-palmitoyl cysteine; by hostUniRule annotation | 1 | |
Lipidationi | 837 | S-palmitoyl cysteine; by hostUniRule annotation | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 511 – 512 | Cleavage; by host furinUniRule annotation | 2 |
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Lipoprotein, PalmitatePTM databases
GlyConnecti | 150, 20 N-Linked glycans |
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.
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 annotationThe 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.
UniRule annotationStructurei
Secondary structure
3D structure databases
SMRi | Q70626 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q70626 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 131 – 156 | V1UniRule annotationAdd BLAST | 26 | |
Regioni | 157 – 196 | V2UniRule annotationAdd BLAST | 40 | |
Regioni | 296 – 330 | V3UniRule annotationAdd BLAST | 35 | |
Regioni | 364 – 374 | CD4-binding loopUniRule annotationAdd BLAST | 11 | |
Regioni | 385 – 418 | V4UniRule annotationAdd BLAST | 34 | |
Regioni | 461 – 471 | V5Add BLAST | 11 | |
Regioni | 463 – 471 | V5UniRule annotation | 9 | |
Regioni | 512 – 532 | Fusion peptideUniRule annotationAdd BLAST | 21 | |
Regioni | 574 – 592 | ImmunosuppressionUniRule annotationAdd BLAST | 19 | |
Regioni | 662 – 683 | MPER; binding to GalCerUniRule annotationAdd BLAST | 22 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 633 – 667 | UniRule annotationAdd BLAST | 35 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 855 – 856 | Di-leucine internalization motifUniRule annotation | 2 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 460 – 463 | Poly-Asn | 4 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Coiled coil, Signal, Transmembrane, Transmembrane helixFamily and domain databases
CDDi | cd09909, HIV-1-like_HR1-HR2, 1 hit |
Gene3Di | 2.170.40.20, 2 hits |
HAMAPi | MF_04083, HIV_ENV, 1 hit |
InterProi | View protein in InterPro IPR036377, Gp120_core_sf IPR037527, Gp160 IPR000328, GP41-like IPR000777, HIV1_Gp120 |
Pfami | View protein in Pfam PF00516, GP120, 1 hit PF00517, GP41, 1 hit |
SUPFAMi | SSF56502, SSF56502, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MRVKEKYQHL RRWGWRWGTM LLGMLMICSA TEKLWVTVYY GVPVWKEATT
60 70 80 90 100
TLFCASDAKA YDTEVHNVWA THACVPTDPN PQEVVLVNVT ENFNMWKNDM
110 120 130 140 150
VEQMHEDIIS LWDQSLKPCV KLTPLCVSLK CTDLKNDTNT NSSSGGMIME
160 170 180 190 200
KGEIKNCSFN ISTSIRGKVQ KEYAFFYKHD IIPIDNDTTS YTLTSCNTSV
210 220 230 240 250
ITQACPKVSF EPIPIHYCAP AGFAILKCNN KTFNGTGPCT NVSTVQCTHG
260 270 280 290 300
IKPVVSTQLL LNGSLAEEEV VIRSANLTDN VKTIIVQLNQ SVEINCTRPN
310 320 330 340 350
NNTRKRIRIQ RGPGRTFVTI GKIGNMRQAH CNISRAKWNN TLKQIASKLR
360 370 380 390 400
EQYGNNKTII FKQSSGGDLE IVTHSFNCGG EFFYCNSTQL FNSTWFNSTW
410 420 430 440 450
STEGSNNTEG SDTITLPCRI KQIINMWQEV GKAMYAPPIS GQIRCSSNIT
460 470 480 490 500
GLLLTRDGGN NNNGSEIFRP 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 YIKIFIMIVG GLVGLRIVFA
710 720 730 740 750
VLSIVNRVRQ GHSPLSFQTH LPTPGGPDRP EGIEEEGGER DRDRSIRLVN
760 770 780 790 800
GSLALIWDDL RSLCLFSYHR LRDLLLIVTR IVELLGRRGW EALKYWWNLL
810 820 830 840 850
QYWSQELKNS AVSLLNATAI AVAEGTDRVI EVVQGACRAI RHIPRRIRQG
LERILL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U12055 Genomic RNA Translation: AAA76690.1 |
Similar proteinsi
Cross-referencesi
Web resourcesi
hivdb HIV drug resistance database |
BioAfrica: HIV bioinformatics in Africa |
HIV drug resistance mutations |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U12055 Genomic RNA Translation: AAA76690.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1IF3 | model | - | A/B/C | 540-665 | [»] | |
2X7R | X-ray | 2.00 | A/D/N | 528-581 | [»] | |
B/C/E | 629-683 | [»] | ||||
2Z2T | X-ray | 2.10 | A/B/C | 546-581 | [»] | |
3AHA | X-ray | 1.70 | A/C/E | 548-581 | [»] | |
B/D/F | 628-660 | [»] | ||||
3CP1 | X-ray | 2.00 | A | 536-663 | [»] | |
3CYO | X-ray | 2.10 | A | 536-663 | [»] | |
3GWO | X-ray | 1.65 | A/B | 630-683 | [»] | |
3H00 | X-ray | 2.20 | A/B/C/D | 636-674 | [»] | |
3H01 | X-ray | 1.70 | A/B | 630-683 | [»] | |
4I48 | X-ray | 2.80 | C | 192-200 | [»] | |
5HFM | X-ray | 2.30 | A/B/C/D/E/F | 539-581 | [»] | |
SMRi | Q70626 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
PTM databases
GlyConnecti | 150, 20 N-Linked glycans |
Enzyme and pathway databases
Reactomei | R-HSA-5621480, Dectin-2 family |
Miscellaneous databases
EvolutionaryTracei | Q70626 |
Family and domain databases
CDDi | cd09909, HIV-1-like_HR1-HR2, 1 hit |
Gene3Di | 2.170.40.20, 2 hits |
HAMAPi | MF_04083, HIV_ENV, 1 hit |
InterProi | View protein in InterPro IPR036377, Gp120_core_sf IPR037527, Gp160 IPR000328, GP41-like IPR000777, HIV1_Gp120 |
Pfami | View protein in Pfam PF00516, GP120, 1 hit PF00517, GP41, 1 hit |
SUPFAMi | SSF56502, SSF56502, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ENV_HV1LW | |
Accessioni | Q70626Primary (citable) accession number: Q70626 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1998 |
Last sequence update: | November 1, 1996 | |
Last modified: | February 10, 2021 | |
This is version 143 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families