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Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 32) (gp32)]

 ENV_SIVG1               Reviewed;         854 AA.
Q02837;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
23-MAY-2018, entry version 104.
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 32;
Short=gp32;
Flags: Precursor;
Name=env;
Simian immunodeficiency virus agm.grivet (isolate AGM gr-1)
(SIV-agm.gri) (Simian immunodeficiency virus African green monkey
grivet).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Lentivirus; Primate lentivirus group.
NCBI_TaxID=31684;
NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2024476; DOI=10.1016/0042-6822(91)90689-9;
Fomsgaard A., Hirsch V.M., Allan J.S., Johnson P.R.;
"A highly divergent proviral DNA clone of SIV from a distinct species
of African green monkey.";
Virology 182:397-402(1991).
-!- 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 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. 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: 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). {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. SIV
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 SIV-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. 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 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.
Surface protein gp120 interacts with host CD4 and CCR5 (By
similarity). Gp120 also interacts with the C-type lectins
CD209/DC-SIGN and CLEC4M/DC-SIGNR (collectively referred to as DC-
SIGN(R)) (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) (By similarity). {ECO:0000250}.
-!- DOMAIN: The YXXL motif is involved in determining the exact site
of viral release at the surface of infected mononuclear cells and
promotes endocytosis. {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}.
-!- MISCELLANEOUS: This is an African green monkey isolate.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M66437; AAA91928.1; -; Genomic_DNA.
EMBL; M58410; AAA47591.1; -; Genomic_RNA.
RefSeq; NP_054372.1; NC_001549.1.
ProteinModelPortal; Q02837; -.
PRIDE; Q02837; -.
GeneID; 1490007; -.
KEGG; vg:1490007; -.
KO; K19287; -.
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:0039663; P:membrane fusion involved in viral entry into host cell; 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;
Apoptosis; Cleavage on pair of basic residues; Coiled coil;
Disulfide bond; Fusion of virus membrane with host membrane;
Glycoprotein; Host cell membrane; Host endosome; Host membrane;
Host-virus interaction; Membrane; Signal; Transmembrane;
Transmembrane helix; Viral attachment to host cell;
Viral envelope protein; Viral penetration into host cytoplasm; Virion;
Virus entry into host cell.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 854 Envelope glycoprotein gp160.
/FTId=PRO_0000239507.
CHAIN 21 522 Surface protein gp120. {ECO:0000250}.
/FTId=PRO_0000038460.
CHAIN 523 854 Transmembrane protein gp41.
{ECO:0000250}.
/FTId=PRO_0000038461.
TOPO_DOM 21 705 Extracellular. {ECO:0000255}.
TRANSMEM 706 726 Helical. {ECO:0000255}.
TOPO_DOM 727 854 Cytoplasmic. {ECO:0000255}.
REGION 111 153 V1.
REGION 154 198 V2.
REGION 300 332 V3.
REGION 389 430 V4.
REGION 473 481 V5.
REGION 523 543 Fusion peptide. {ECO:0000255}.
REGION 586 602 Immunosuppression. {ECO:0000250}.
REGION 667 688 MPER; binding to GalCer. {ECO:0000250}.
COILED 633 672 {ECO:0000255}.
MOTIF 717 720 YXXL motif; contains endocytosis signal.
{ECO:0000250}.
COMPBIAS 571 574 Poly-Gln.
COMPBIAS 744 747 Poly-Ser.
SITE 522 523 Cleavage; by host furin. {ECO:0000255}.
CARBOHYD 35 35 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 153 153 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 168 168 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 182 182 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 199 199 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 244 244 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 255 255 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 265 265 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 283 283 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 305 305 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 355 355 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 400 400 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 409 409 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 458 458 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 472 472 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 478 478 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 630 630 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 646 646 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 42 55 {ECO:0000250}.
DISULFID 99 207 {ECO:0000250}.
DISULFID 106 198 {ECO:0000250}.
DISULFID 111 154 {ECO:0000250}.
DISULFID 220 250 {ECO:0000250}.
DISULFID 230 242 {ECO:0000250}.
DISULFID 300 333 {ECO:0000250}.
DISULFID 382 457 {ECO:0000250}.
DISULFID 389 430 {ECO:0000250}.
SEQUENCE 854 AA; 96856 MW; 5919CA6C9622912F CRC64;
MGRLLIKILI IAIGISIGIG NLYVTVFYGI PVWKNSTVQA FCMTPNTNMW ATTNCIPDDH
DNTEVPLNIT EAFEAWDNPL VKQAESNIHL LFEQTMRPCV KLSPICIKMS CVELNGTATT
KATTTATTTM TTPCQNCSTE QIEGEMAEEP ASNCTFAIAG YQRDVKKNYS MTWYDQELVC
NNKTGSEKGS KDCYMIHCND SVIKEACDKT YWDTLRVRYC APAGYALLKC NDKDYRGFAP
KCKNVSVVHC TRLINTTITT GIGLNGSRSE NRTEIWQKGG NDNDTVIIKL NKFYNLTVRC
RRPGNKTVLP VTIMAGLVFH SQKYNTRLKQ AWCHFQGDWK GAWKEVREEV KKVKNLTEVS
IENIHLRRIW GDPESANFWF NCQGEFFYCK MDWFINYLNN RTEDAEGTNR TCDKGKPGPG
PCVQRTYVAC HIRQVVNDWY TVSKKVYAPP REGHLECNSS VTALYVAIDY NNKSGPINVT
LSPQVRSIWA YELGDYKLVE ITPIGFAPTD VRRYTGPTRE KRVPFVLGFL GFLGAAGTAM
GAAATTLTVQ SRHLLAGILQ QQKNLLAAVE QQQQLLKLTI WGVKNLNARV TALEKYLEDQ
ARLNSWGCAW KQVCHTTVPW KYNNTPKWDN MTWLEWERQI NALEGNITQL LEEAQNQESK
NLDLYQKLDD WSGFWSWFSL STWLGYVKIG FLVIVIILGL RFAWVLWGCI RNIRQGYNPL
PQIHIHSSAE RPDNGGGQDR GGESSSSKLI RLQEESSTPS RINNWWLNFK SCSLRIRTWC
YNICLTLLIF IRTAVGYLQY GLQQLQEAAT GLAQALARAA REAWGRLGAI VRSAYRAVIN
SPRRVRQGLE KVLG


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