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ENV_HV2CA
ID   ENV_HV2CA               Reviewed;         859 AA.
AC   P24105;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   23-FEB-2022, entry version 117.
DE   RecName: Full=Envelope glycoprotein gp160;
DE   AltName: Full=Env polyprotein;
DE   Contains:
DE     RecName: Full=Surface protein gp120;
DE              Short=SU;
DE     AltName: Full=Glycoprotein 120;
DE              Short=gp120;
DE   Contains:
DE     RecName: Full=Transmembrane protein gp41;
DE              Short=TM;
DE     AltName: Full=Glycoprotein 41;
DE              Short=gp41;
DE   Flags: Precursor;
GN   Name=env;
OS   Human immunodeficiency virus type 2 subtype A (isolate CAM2) (HIV-2).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX   NCBI_TaxID=11715;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2005437; DOI=10.1099/0022-1317-72-3-721;
RA   Tristem M., Hill F., Karpas A.;
RT   "Nucleotide sequence of a Guinea-Bissau-derived human immunodeficiency
RT   virus type 2 proviral clone (HIV-2CAM2).";
RL   J. Gen. Virol. 72:721-724(1991).
RN   [2]
RP   REVIEW.
RX   PubMed=12029140; DOI=10.1099/0022-1317-83-6-1253;
RA   Reeves J.D., Doms R.W.;
RT   "Human immunodeficiency virus type 2.";
RL   J. Gen. Virol. 83:1253-1265(2002).
CC   -!- FUNCTION: The surface protein gp120 (SU) attaches the virus to the host
CC       lymphoid cell by binding to the primary receptor CD4. This interaction
CC       induces a structural rearrangement creating a high affinity binding
CC       site for a chemokine coreceptor like CXCR4 and/or CCR5. This peculiar 2
CC       stage receptor-interaction strategy allows gp120 to maintain the highly
CC       conserved coreceptor-binding site in a cryptic conformation, protected
CC       from neutralizing antibodies. Since CD4 also displays a binding site
CC       for the disulfide-isomerase P4HB/PDI, a P4HB/PDI-CD4-CXCR4-gp120
CC       complex may form. In that complex, P4HB/PDI could reach and reduce
CC       gp120 disulfide bonds, causing major conformational changes in gp120.
CC       TXN, another PDI family member could also be involved in disulfide
CC       rearrangements in Env during fusion. These changes are transmitted to
CC       the transmembrane protein gp41 and are thought to activate its
CC       fusogenic potential by unmasking its fusion peptide (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: The surface protein gp120 is a ligand for CD209/DC-SIGN and
CC       CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs),
CC       and on endothelial cells of liver sinusoids and lymph node sinuses.
CC       These interactions allow capture of viral particles at mucosal surfaces
CC       by these cells and subsequent transmission to permissive cells. DCs are
CC       professional antigen presenting cells, critical for host immunity by
CC       inducing specific immune responses against a broad variety of
CC       pathogens. They act as sentinels in various tissues where they take up
CC       antigen, process it, and present it to T-cells following migration to
CC       lymphoid organs. HIV subverts the migration properties of dendritic
CC       cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission
CC       to permissive T-cells occurs either in trans (without DCs infection,
CC       through viral capture and transmission), or in cis (following DCs
CC       productive infection, through the usual CD4-gp120 interaction), thereby
CC       inducing a robust infection. In trans infection, bound virions remain
CC       infectious over days and it is proposed that they are not degraded, but
CC       protected in non-lysosomal acidic organelles within the DCs close to
CC       the cell membrane thus contributing to the viral infectious potential
CC       during DCs' migration from the periphery to the lymphoid tissues. On
CC       arrival at lymphoid tissues, intact virions recycle back to DCs' cell
CC       surface allowing virus transmission to CD4+ T-cells. Virion capture
CC       also seems to lead to MHC-II-restricted viral antigen presentation, and
CC       probably to the activation of HIV-specific CD4+ cells (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: The transmembrane protein gp41 (TM) acts as a class I viral
CC       fusion protein. Under the current model, the protein has at least 3
CC       conformational states: pre-fusion native state, pre-hairpin
CC       intermediate state, and post-fusion hairpin state. During fusion of
CC       viral and target intracellular membranes, the coiled coil regions
CC       (heptad repeats) assume a trimer-of-hairpins structure, positioning the
CC       fusion peptide in close proximity to the C-terminal region of the
CC       ectodomain. The formation of this structure appears to drive apposition
CC       and subsequent fusion of viral and target cell membranes. Complete
CC       fusion occurs in host cell endosomes and is dynamin-dependent, however
CC       some lipid transfer might occur at the plasma membrane. The virus
CC       undergoes clathrin-dependent internalization long before endosomal
CC       fusion, thus minimizing the surface exposure of conserved viral
CC       epitopes during fusion and reducing the efficacy of inhibitors
CC       targeting these epitopes. Membranes fusion leads to delivery of the
CC       nucleocapsid into the cytoplasm (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: The envelope glycoprotein gp160 precursor down-modulates cell
CC       surface CD4 antigen by interacting with it in the endoplasmic reticulum
CC       and blocking its transport to the cell surface. {ECO:0000250}.
CC   -!- FUNCTION: The gp120-gp41 heterodimer seems to contribute to T-cell
CC       depletion during HIV-1 infection. The envelope glycoproteins expressed
CC       on the surface of infected cells induce apoptosis through an
CC       interaction with uninfected cells expressing the receptor (CD4) and the
CC       coreceptors CXCR4 or CCR5. This type of bystander killing may be
CC       obtained by at least three distinct mechanisms. First, the interaction
CC       between the 2 cells can induce cellular fusion followed by nuclear
CC       fusion within the syncytium. Syncytia are condemned to die from
CC       apoptosis. Second, the 2 interacting cells may not fuse entirely and
CC       simply exchange plasma membrane lipids, after a sort of hemifusion
CC       process, followed by rapid death. Third, it is possible that virus-
CC       infected cells, on the point of undergoing apoptosis, fuse with CD4-
CC       expressing cells, in which case apoptosis is rapidly transmitted from
CC       one cell to the other and thus occurs in a sort of contagious fashion
CC       (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: The gp120-gp41 heterodimer allows rapid transcytosis of the
CC       virus through CD4 negative cells such as simple epithelial monolayers
CC       of the intestinal, rectal and endocervical epithelial barriers. Both
CC       gp120 and gp41 specifically recognize glycosphingolipids galactosyl-
CC       ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the
CC       lipid rafts structures of epithelial cells. Binding to these
CC       alternative receptors allows the rapid transcytosis of the virus
CC       through the epithelial cells. This transcytotic vesicle-mediated
CC       transport of virions from the apical side to the basolateral side of
CC       the epithelial cells does not involve infection of the cells themselves
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: [Surface protein gp120]: The mature envelope protein (Env)
CC       consists of a homotrimer of non-covalently associated gp120-gp41
CC       heterodimers. The resulting complex protrudes from the virus surface as
CC       a spike. There seems to be as few as 10 spikes on the average virion.
CC       Interacts with human CD4, CCR5 and CXCR4, to form a P4HB/PDI-CD4-CXCR4-
CC       gp120 complex. Gp120 also interacts with the C-type lectins CD209/DC-
CC       SIGN and CLEC4M/DC-SIGNR (collectively referred to as DC-SIGN(R)).
CC       Gp120 and gp41 interact with GalCer (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: [Transmembrane protein gp41]: The mature envelope protein
CC       (Env) consists of a homotrimer of non-covalently associated gp120-gp41
CC       heterodimers. The resulting complex protrudes from the virus surface as
CC       a spike. There seems to be as few as 10 spikes on the average virion.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host
CC       cell membrane {ECO:0000250}; Single-pass type I membrane protein
CC       {ECO:0000250}. Host endosome membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Note=It is probably concentrated at the
CC       site of budding and incorporated into the virions possibly by contacts
CC       between the cytoplasmic tail of Env and the N-terminus of Gag.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host cell
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Host
CC       endosome membrane {ECO:0000305}; Peripheral membrane protein
CC       {ECO:0000305}. Note=The surface protein is not anchored to the viral
CC       envelope, but associates with the extravirion surface through its
CC       binding to TM. It is probably concentrated at the site of budding and
CC       incorporated into the virions possibly by contacts between the
CC       cytoplasmic tail of Env and the N-terminus of Gag (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: Some of the most genetically diverse regions of the viral
CC       genome are present in Env. They are called variable regions 1 through 5
CC       (V1 through V5). Coreceptor usage of gp120 is determined mainly by the
CC       primary structure of the third variable region (V3) in the outer domain
CC       of gp120. Binding to CCR5 involves a region adjacent in addition to V3
CC       (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The 17 amino acids long immunosuppressive region is present in
CC       many retroviral envelope proteins. Synthetic peptides derived from this
CC       relatively conserved sequence inhibit immune function in vitro and in
CC       vivo (By similarity). {ECO:0000250}.
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC       Envelope glycoproteins are synthesized as an inactive precursor that is
CC       heavily N-glycosylated and processed likely by host cell furin in the
CC       Golgi to yield the mature SU and TM proteins. The cleavage site between
CC       SU and TM requires the minimal sequence [KR]-X-[KR]-R (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Palmitoylation of the transmembrane protein and of Env polyprotein
CC       (prior to its proteolytic cleavage) is essential for their association
CC       with host cell membrane lipid rafts. Palmitoylation is therefore
CC       required for envelope trafficking to classical lipid rafts, but not for
CC       viral replication (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: Some HIV-2 isolates have been described that can infect
CC       cells independently of CD4, using CXCR4 as primary receptor. These
CC       isolates may have an exposed coreceptor binding site.
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DR   EMBL; D00835; BAA00716.1; -; Genomic_DNA.
DR   PIR; F38475; VCLJCT.
DR   PRIDE; P24105; -.
DR   Proteomes; UP000007421; Genome.
DR   GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0039587; P:suppression by virus of host tetherin activity; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   CDD; cd09909; HIV-1-like_HR1-HR2; 1.
DR   Gene3D; 2.170.40.20; -; 2.
DR   InterPro; IPR036377; Gp120_core_sf.
DR   InterPro; IPR000328; GP41-like.
DR   InterPro; IPR000777; HIV1_Gp120.
DR   Pfam; PF00516; GP120; 1.
DR   Pfam; PF00517; GP41; 1.
DR   SUPFAM; SSF56502; SSF56502; 1.
PE   3: Inferred from homology;
KW   AIDS; Apoptosis; Clathrin-mediated endocytosis of virus by host;
KW   Cleavage on pair of basic residues; Coiled coil; Disulfide bond;
KW   Fusion of virus membrane with host endosomal membrane;
KW   Fusion of virus membrane with host membrane; Glycoprotein;
KW   Host cell membrane; Host endosome; Host membrane; Host-virus interaction;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host tetherin by virus; Lipoprotein; Membrane; Palmitate;
KW   Signal; Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW   Viral envelope protein; Viral immunoevasion;
KW   Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW   Virus entry into host cell.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..859
FT                   /note="Envelope glycoprotein gp160"
FT                   /id="PRO_0000239497"
FT   CHAIN           25..512
FT                   /note="Surface protein gp120"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038437"
FT   CHAIN           513..859
FT                   /note="Transmembrane protein gp41"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000038438"
FT   TOPO_DOM        25..680
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        681..701
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        702..859
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          114..159
FT                   /note="V1"
FT   REGION          160..204
FT                   /note="V2"
FT   REGION          304..337
FT                   /note="V3"
FT   REGION          397..420
FT                   /note="V4"
FT   REGION          463..470
FT                   /note="V5"
FT   REGION          513..533
FT                   /note="Fusion peptide"
FT                   /evidence="ECO:0000255"
FT   REGION          576..592
FT                   /note="Immunosuppression"
FT                   /evidence="ECO:0000250"
FT   REGION          658..679
FT                   /note="MPER; binding to GalCer"
FT                   /evidence="ECO:0000250"
FT   REGION          726..745
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          625..646
FT                   /evidence="ECO:0000255"
FT   MOTIF           708..711
FT                   /note="YXXV motif; contains endocytosis signal"
FT                   /evidence="ECO:0000250"
FT   MOTIF           858..859
FT                   /note="Di-leucine internalization motif"
FT                   /evidence="ECO:0000250"
FT   SITE            512..513
FT                   /note="Cleavage; by host furin"
FT                   /evidence="ECO:0000250"
FT   LIPID           774
FT                   /note="S-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        115
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        176
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        195
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        271
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        309
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        398
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        411
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        448
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        463
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        467
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        612
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        621
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        637
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        45..58
FT                   /evidence="ECO:0000250"
FT   DISULFID        102..213
FT                   /evidence="ECO:0000250"
FT   DISULFID        109..204
FT                   /evidence="ECO:0000250"
FT   DISULFID        114..160
FT                   /evidence="ECO:0000250"
FT   DISULFID        226..256
FT                   /evidence="ECO:0000250"
FT   DISULFID        236..248
FT                   /evidence="ECO:0000250"
FT   DISULFID        304..338
FT                   /evidence="ECO:0000250"
FT   DISULFID        390..447
FT                   /evidence="ECO:0000250"
FT   DISULFID        397..420
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   859 AA;  99018 MW;  6F54913F206B26C3 CRC64;
     MERGRNQLLI AILLASACLI YCRQQYVTVF YGVPAWKNAS IPLFCATKNR DTWGTIQCLP
     DNDDYQEIPL NVTEAFDAWD NTITEQAIED VWNLFETSIK PCVKLTPLCV AMKCNISTSD
     TTMIRTTTPS TAKEAPISDN SPCIRTNNCS GLEEEKIVKC HFNMTGLERD KKKQYNETWY
     SSDVVCDNST DQTTNETTCY MNHCNTSVIT ESCDKHYWDA MRFRYCAPPG FAILRCNDTK
     YSGFAPNCSK VVASTCTRMM ETQTSTWFGF NGTRAENRTY IYWHGKDNRT IISLNKHYNL
     SMYCRRPGNK TVVPITLMSG QRFHSRPIIN KRPRQAWCWF KGNWTEAMQE VKQTLAEHPR
     YKGTKNITDI TFKAPERGSD PEVTYMWSNC RGEFFYCNMT WFLNWVENKP NTTKRNYAPC
     HIRQIINTWH KVGKNVYLPP REGELTCNST VTSIIANIDE RDNQTTNITF SADVAELYRL
     ELGDYKLVEI TPIGFAPTSQ KRYSPAHGRP KRGAFVLGFL GFLTTAGVAM GTASLTLSAQ
     SRTLLAGIVQ QQQQLLDVVK RQQELLRLTV WGTKILQARV TAIEKYLKDQ AQLNSWGCAF
     RQVCHTTVPW ANESLTPDWN NMTWQEWEQK VRYLEANISQ SLEEAQLQQE KNMYELQKLN
     NWDVFTNWFD LTSWISYIQY GVYIVVGIIV LRIVIYVVQM LSRLRKGYRP VFSSSPGYIQ
     QIHIHKDPEQ PASEETEEDV GGNGGDRSWP WQIEYIHFLI RQLIRLLTGL YNICRNLLSR
     IFQTLQPILQ NLRDWLRPKV AFLQYGCEWI QEAFQAAARA ARETLAGACR DVWGMLQRIG
     RGILAVPRRI RQGAELALL
 
 
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