ID J9XVC2_SIV Unreviewed; 887 AA. AC J9XVC2; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 24-JUL-2024, entry version 61. DE RecName: Full=Envelope glycoprotein gp160 {ECO:0000256|RuleBase:RU363095}; DE Contains: DE RecName: Full=Surface protein gp120 {ECO:0000256|RuleBase:RU363095}; DE Short=SU {ECO:0000256|RuleBase:RU363095}; DE AltName: Full=Glycoprotein 120 {ECO:0000256|RuleBase:RU363095}; DE Short=gp120 {ECO:0000256|RuleBase:RU363095}; DE Contains: DE RecName: Full=Transmembrane protein gp41 {ECO:0000256|RuleBase:RU363095}; DE Short=TM {ECO:0000256|RuleBase:RU363095}; OS Simian immunodeficiency virus - sm. OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus; OC Simian immunodeficiency virus. OX NCBI_TaxID=11712 {ECO:0000313|EMBL:AFS33706.1}; RN [1] {ECO:0000313|EMBL:AFS33706.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=783 {ECO:0000313|EMBL:AFS33706.1}; RX PubMed=23035225; DOI=10.1128/JVI.02174-12; RA Dang Q., Whitted S., Goeken R.M., Brenchley J.M., Matsuda K., Brown C.R., RA Lafont B.A., Starost M.F., Iyengar R., Plishka R.J., Buckler-White A., RA Hirsch V.M.; RT "Development of neurological disease is associated with increased immune RT activation in simian immunodeficiency virus-infected macaques."; RL J. Virol. 86:13795-13799(2012). CC -!- FUNCTION: Surface protein gp120 (SU) may target the virus to gut- CC associated lymphoid tissue (GALT) by binding host ITGA4/ITGB7 (alpha- CC 4/beta-7 integrins), a complex that mediates T-cell migration to the CC GALT. Interaction between gp120 and ITGA4/ITGB7 would allow the virus CC to enter GALT early in the infection, infecting and killing most of CC GALT's resting CD4+ T-cells. This T-cell depletion is believed to be CC the major insult to the host immune system leading to AIDS. CC {ECO:0000256|ARBA:ARBA00037206}. 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. CC {ECO:0000256|ARBA:ARBA00037137}. 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 CC themselves. {ECO:0000256|ARBA:ARBA00037366}. 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 CCR5. This peculiar 2 stage CC receptor-interaction strategy allows gp120 to maintain the highly CC conserved coreceptor-binding site in a cryptic conformation, protected CC from neutralizing antibodies. These changes are transmitted to the CC transmembrane protein gp41 and are thought to activate its fusogenic CC potential by unmasking its fusion peptide. CC {ECO:0000256|ARBA:ARBA00037419}. 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. The virus undergoes clathrin- CC dependent internalization long before endosomal fusion, thus minimizing CC the surface exposure of conserved viral epitopes during fusion and CC reducing the efficacy of inhibitors targeting these epitopes. Membranes CC fusion leads to delivery of the nucleocapsid into the cytoplasm. CC {ECO:0000256|ARBA:ARBA00037086}. CC -!- SUBUNIT: The mature envelope protein (Env) consists of a homotrimer of CC non-covalently associated gp120-gp41 heterodimers. The resulting CC complex protrudes from the virus surface as a spike. Interacts with CC host CD4 and CCR5 (By similarity). Gp120 also interacts with the C-type CC lectins CD209/DC-SIGN and CLEC4M/DC-SIGNR (collectively referred to as CC DC-SIGN(R)). {ECO:0000256|ARBA:ARBA00038686}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cell CC membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane CC protein {ECO:0000256|ARBA:ARBA00004251}. Endosome membrane CC {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004481}. Endosome membrane CC {ECO:0000256|ARBA:ARBA00004530}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004530}. Host cell membrane CC {ECO:0000256|ARBA:ARBA00004505}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004505}. Host cell membrane CC {ECO:0000256|ARBA:ARBA00004402}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004402}. Host endosome membrane CC {ECO:0000256|ARBA:ARBA00004433}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004433}. Host endosome membrane CC {ECO:0000256|ARBA:ARBA00004578}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004578}. Membrane CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004170}. Membrane CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479}. Virion membrane CC {ECO:0000256|ARBA:ARBA00004650}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004650}. Virion membrane CC {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004563}. 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. {ECO:0000256|RuleBase:RU363095}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JQ686972; AFS33706.1; -; Genomic_RNA. 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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0039663; P:membrane fusion involved in viral entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0046718; P:symbiont entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule. DR CDD; cd09909; HIV-1-like_HR1-HR2; 1. DR Gene3D; 1.10.287.210; -; 1. DR Gene3D; 2.170.40.20; Human immunodeficiency virus 1, Gp160, envelope glycoprotein; 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; gp120 core; 1. DR SUPFAM; SSF58069; Virus ectodomain; 1. PE 4: Predicted; KW Apoptosis {ECO:0000256|ARBA:ARBA00022703, ECO:0000256|RuleBase:RU363095}; KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685, KW ECO:0000256|RuleBase:RU363095}; KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|RuleBase:RU363095}; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511, KW ECO:0000256|RuleBase:RU363095}; KW Host endosome {ECO:0000256|ARBA:ARBA00023046, KW ECO:0000256|RuleBase:RU363095}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870, KW ECO:0000256|RuleBase:RU363095}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581, KW ECO:0000256|RuleBase:RU363095}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363095}; KW Transmembrane {ECO:0000256|RuleBase:RU363095}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363095}; KW Viral attachment to host cell {ECO:0000256|RuleBase:RU363095}; KW Viral envelope protein {ECO:0000256|RuleBase:RU363095, KW ECO:0000313|EMBL:AFS33706.1}; KW Viral penetration into host cytoplasm {ECO:0000256|RuleBase:RU363095}; KW Virion {ECO:0000256|ARBA:ARBA00022844, ECO:0000256|RuleBase:RU363095}; KW Virus entry into host cell {ECO:0000256|RuleBase:RU363095}. FT TRANSMEM 698..719 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363095" FT DOMAIN 24..532 FT /note="Human immunodeficiency virus 1 envelope glycoprotein FT Gp120" FT /evidence="ECO:0000259|Pfam:PF00516" FT DOMAIN 551..746 FT /note="Retroviral envelope protein GP41-like" FT /evidence="ECO:0000259|Pfam:PF00517" FT REGION 744..767 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 645..672 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 748..764 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 887 AA; 102186 MW; 1B26ACDC118B61CF CRC64; MGCLGNQLLI ALLLVSVLEI WCVQYVTVFY GVPAWKNATI PLFCATRNRD TWGTTQCLPD NDDYSELAVN ITEAFDAWDN TVTEQAIEDV WNLFETSIKP CVKLTPLCIA MRCNKTETDR WGLTGEAGTA TTTKSTTSPT TTTVTPKVIN EGDSCIKNDS CAGLEQEPMI GCKFNMTGLK RDKKTEYNET WYARDLICEQ SANESESKCY MQHCNTSVIQ ESCDKHYWDA IRFRYCAPPG YALLRCNDSN YSGFAPNCSK VVVSSCTRMM ETQTSTWFGF NGTRAENRTY IYWHGNSNRT IISLNKFYNL TMKCRRPGNK TVLPVTIMSG LVFHSQPINE RPKQAWCRFG GNWSEAIQEV KETLVKHPRY TGTNETRKIN LTAPAGGDPE VTFMWTNCRG EFLYCKMNWF LNWVEDRDQN GSRWKQQKNS EQQKRNYVPC HIRQIINTWH KVGKNVYLPP REGDLTCNST VTSLIAEIDW INNNETNITM SAEVAQLYRL ELGDYKLVEI TPIGLAPTNV RRYTTTGASR NKXGVFVLGF LGFLATAGSA MGAASLTLSA QSRTLLAGIV QQQQQLLDVV KRQQELLRLT VWGTKNLQTR VTAIEKYLKD QAQLNSWGCA FRQVCHTTVQ WPNNSLVPNW NNMTWQEWER QVDFLEANIT QLLEEAQIQQ EKNMYELQKL NSWDIFGNWF DLTSWLRYIQ YGVLIVLGVV GLRIVIYVVQ MLARLRQGYR PVFSPPPVYV QQIPIHKDQE PPTKEGEEGE GGDRGGSKSW PWQIEYIHFL IRQLIRLLTW LFSSCRDWLL RIYQTLQPVL QRLSRTLQRV REVIRIERAY LQYGWSYFQE AAQAWWRFAR ETLASAWRDI WETLGRVGRG ILAIPRRVRQ GLELTLL //