ID J9XVC2_SIV Unreviewed; 887 AA. AC J9XVC2; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 12-OCT-2022, entry version 54. 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. 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 -!- 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. CC {ECO:0000256|RuleBase:RU363095}. 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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:0039663; P:membrane fusion involved in viral entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0046718; P:viral 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; 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 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}; Coiled coil {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|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="GP120" FT /evidence="ECO:0000259|Pfam:PF00516" FT DOMAIN 551..746 FT /note="GP41" 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 //