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Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]

 ENV_HV2D2               Reviewed;         859 AA.
P15831;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
25-OCT-2017, entry version 114.
RecName: Full=Envelope glycoprotein gp160;
AltName: Full=Env polyprotein;
Contains:
RecName: Full=Surface protein gp120;
Short=SU;
AltName: Full=Glycoprotein 120;
Short=gp120;
Contains:
RecName: Full=Transmembrane protein gp41;
Short=TM;
AltName: Full=Glycoprotein 41;
Short=gp41;
Flags: Precursor;
Name=env;
Human immunodeficiency virus type 2 subtype B (isolate D205) (HIV-2).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Primate lentivirus group.
NCBI_TaxID=11716;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Dietrich U.;
Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-207.
PubMed=2594088; DOI=10.1038/342948a0;
Dietrich U., Adamski M., Kreutz R., Seipp A., Kuehnel H.,
Ruebsamen-Waigmann H.;
"A highly divergent HIV-2-related isolate.";
Nature 342:948-950(1989).
[3]
REVIEW.
PubMed=12029140;
Reeves J.D., Doms R.W.;
"Human immunodeficiency virus type 2.";
J. Gen. Virol. 83:1253-1265(2002).
-!- 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 (By
similarity). {ECO:0000250}.
-!- FUNCTION: 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).
{ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: 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.
{ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: 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).
{ECO:0000250}.
-!- SUBUNIT: 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
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Transmembrane protein gp41: Virion membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Host cell membrane {ECO:0000250}; Single-pass type I membrane
protein {ECO:0000250}. Host endosome membrane {ECO:0000305};
Single-pass type I membrane protein {ECO:0000305}. 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. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Surface protein gp120: Virion membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host
cell membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}. Host endosome membrane {ECO:0000305}; Peripheral
membrane protein {ECO:0000305}. 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 (By similarity). {ECO:0000250}.
-!- DOMAIN: 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. Binding to CCR5 involves a region
adjacent in addition to V3 (By similarity). {ECO:0000250}.
-!- DOMAIN: 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). {ECO:0000250}.
-!- PTM: 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 (By similarity). {ECO:0000250}.
-!- PTM: 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). {ECO:0000250}.
-!- MISCELLANEOUS: Some HIV-2 isolates have been described that can
infect cells independently of CD4, using CXCR4 as primary
receptor. These isolates may have an exposed coreceptor binding
site.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X61240; CAA43572.1; -; Genomic_DNA.
PIR; S08442; S08442.
PIR; S24571; S24571.
ProteinModelPortal; P15831; -.
PRIDE; P15831; -.
GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0039587; P:suppression by virus of host tetherin activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd09909; HIV-1-like_HR1-HR2; 1.
Gene3D; 2.170.40.20; -; 2.
InterPro; IPR036377; Gp120_core_sf.
InterPro; IPR000328; GP41-like.
InterPro; IPR000777; HIV1_Gp120.
Pfam; PF00516; GP120; 1.
Pfam; PF00517; GP41; 1.
SUPFAM; SSF56502; SSF56502; 3.
3: Inferred from homology;
AIDS; Apoptosis; Clathrin-mediated endocytosis of virus by host;
Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host cell membrane; Host endosome; Host membrane;
Host-virus interaction;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host tetherin by virus; Lipoprotein; Membrane;
Palmitate; Signal; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral envelope protein;
Viral immunoevasion; Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 859 Envelope glycoprotein gp160.
/FTId=PRO_0000239498.
CHAIN 24 513 Surface protein gp120. {ECO:0000250}.
/FTId=PRO_0000038439.
CHAIN 514 859 Transmembrane protein gp41.
{ECO:0000250}.
/FTId=PRO_0000038440.
TOPO_DOM 24 678 Extracellular. {ECO:0000255}.
TRANSMEM 679 699 Helical. {ECO:0000255}.
TOPO_DOM 700 859 Cytoplasmic. {ECO:0000255}.
REGION 113 163 V1.
REGION 164 205 V2.
REGION 305 337 V3.
REGION 399 422 V4.
REGION 465 471 V5.
REGION 514 534 Fusion peptide. {ECO:0000255}.
REGION 577 593 Immunosuppression. {ECO:0000250}.
REGION 659 680 MPER; binding to GalCer. {ECO:0000250}.
COILED 626 647 {ECO:0000255}.
MOTIF 709 712 YXXV motif; contains endocytosis signal.
{ECO:0000250}.
MOTIF 858 859 Di-leucine internalization motif.
{ECO:0000250}.
COMPBIAS 126 129 Poly-Thr.
COMPBIAS 551 555 Poly-Gln.
SITE 513 514 Cleavage; by host furin. {ECO:0000250}.
LIPID 775 775 S-palmitoyl cysteine; by host.
{ECO:0000250}.
CARBOHYD 37 37 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 70 70 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 112 112 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 150 150 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 165 165 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 191 191 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 206 206 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 238 238 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 241 241 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 248 248 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 272 272 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 278 278 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 289 289 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 310 310 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 343 343 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 367 367 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 400 400 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 450 450 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 464 464 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 468 468 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 613 613 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 622 622 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 638 638 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 44 57 {ECO:0000250}.
DISULFID 101 214 {ECO:0000250}.
DISULFID 108 205 {ECO:0000250}.
DISULFID 113 164 {ECO:0000250}.
DISULFID 227 257 {ECO:0000250}.
DISULFID 237 249 {ECO:0000250}.
DISULFID 305 338 {ECO:0000250}.
DISULFID 392 449 {ECO:0000250}.
DISULFID 399 422 {ECO:0000250}.
SEQUENCE 859 AA; 98607 MW; 35BC963848733E10 CRC64;
MAYFSSRLPI ALLLIGISGF VCKQYVTVFY GIPAWRNATV PLICATTNRD TWGTVQCLPD
NGDYTEIRLN ITEAFDAWDN TVTQQAVDDV WRLFETSIKP CVKLTPLCVA MNCSKTETNP
GNASSTTTTK PTTTSRGLKT INETDPCIKN DSCTGLGEEE IMQCNFSMTG LRRDELKQYK
DTWYSEDLEC NNTRKYTSRC YIRTCNTTII QESCDKHYWD SLRFRYCAPP GFFLLRCNDT
NYSGFMPNCS KVVASSCTRM METQSSTWFG FNGTRAENRT YIYWHEKDNR TIISLNTYYN
LSIHCKRPGN KTVVPIRTVS GLLFHSQPIN KRPRQAWCWF KGNWTEAIKE VKRTIIKHPR
YKGGAKNITS VKLVSEHGKG SDPETTYMWT NCRGEFLYCN MTWFLNWVEN KTNTTRRNYA
PCHIRQIINT WHKVGKNIYL PPREGELSCN STVTSLIANI NSDNSTTNIS VSAEVSELYR
LELGDYKLVE ITPIGFAPTD VRRYSSVKPR NKRGVMVLGF LGFLAMAGSA MGATSLTLSA
QSRTLLAGIV QQQQQPVDVV KRQQELLRLT VWGTKNLQAR VTAIEKYLKD QAQLNSWGCA
FRQVCHTTVP WPNETLTPNW NNMTWQQWEK QVHFLDANIT ALLEEAQIQQ EKNMYELQKI
NSWDVFGNWF DLTSWIKYIH LGLYIVAGLV VLRIVVYIVQ MLARLRKGYR PVFSSPPSYT
QQIPIRKDRG QPANEETEEG GGNDGDYRSW PWQIEYIHFL LRQLRNLLIW LYNGCRTLLL
KTFQILHQIS TNLQPLRLPV AYLQYGISWF QEALRAAARA TGETLASAGE TLWEALRRAA
RAIIAIPRRI RQGLELTLL


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