ID   W6A110_9PLVG            Unreviewed;       854 AA.
AC   W6A110;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   25-OCT-2017, entry version 32.
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};
GN   Name=env {ECO:0000313|EMBL:AHI49131.1};
OS   Simian-Human immunodeficiency virus.
OC   Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
OC   Lentivirus; Primate lentivirus group;
OC   unclassified Primate lentivirus group.
OX   NCBI_TaxID=57667 {ECO:0000313|EMBL:AHI49131.1};
RN   [1] {ECO:0000313|EMBL:AHI49131.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ba-L {ECO:0000313|EMBL:AHI49131.1};
RX   PubMed=23966410; DOI=10.1128/JVI.01361-13;
RA   Klein K., Veazey R.S., Warrier R., Hraber P., Doyle-Meyers L.A.,
RA   Buffa V., Liao H.X., Haynes B.F., Shaw G.M., Shattock R.J.;
RT   "Neutralizing IgG at the portal of infection mediates protection
RT   against vaginal simian/human immunodeficiency virus challenge.";
RL   J. Virol. 87:11604-11616(2013).
CC   -!- SUBUNIT: The mature envelope protein (Env) consists of a
CC       homotrimer of non-covalently associated gp120-gp41 heterodimers.
CC       The resulting complex protrudes from the virus surface as a spike.
CC       {ECO:0000256|RuleBase:RU363095}.
CC   -!- SUBCELLULAR LOCATION: Host cell membrane
CC       {ECO:0000256|SAAS:SAAS00937286}; Peripheral membrane protein
CC       {ECO:0000256|SAAS:SAAS00937286}.
CC   -!- SUBCELLULAR LOCATION: Host cell membrane
CC       {ECO:0000256|SAAS:SAAS00936930}; Single-pass type I membrane
CC       protein {ECO:0000256|SAAS:SAAS00936930}.
CC   -!- SUBCELLULAR LOCATION: Host endosome membrane
CC       {ECO:0000256|SAAS:SAAS00937040}; Single-pass type I membrane
CC       protein {ECO:0000256|SAAS:SAAS00937040}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane
CC       {ECO:0000256|SAAS:SAAS00796993}; Single-pass type I membrane
CC       protein {ECO:0000256|SAAS:SAAS00796993}.
CC   -!- DOMAIN: The 17 amino acids long immunosuppressive region is
CC       present in many retroviral envelope proteins. Synthetic peptides
CC       derived from this relatively conserved sequence inhibit immune
CC       function in vitro and in vivo. {ECO:0000256|RuleBase:RU363095}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|RuleBase:RU363095}.
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DR   EMBL; KF734097; AHI49117.1; -; Other_DNA.
DR   EMBL; KF734099; AHI49118.1; -; Other_DNA.
DR   EMBL; KF734100; AHI49119.1; -; Other_DNA.
DR   EMBL; KF734103; AHI49120.1; -; Other_DNA.
DR   EMBL; KF734104; AHI49121.1; -; Other_DNA.
DR   EMBL; KF734106; AHI49123.1; -; Other_DNA.
DR   EMBL; KF734109; AHI49125.1; -; Other_DNA.
DR   EMBL; KF734110; AHI49126.1; -; Other_DNA.
DR   EMBL; KF734111; AHI49127.1; -; Other_DNA.
DR   EMBL; KF734116; AHI49130.1; -; Other_DNA.
DR   EMBL; KF734117; AHI49131.1; -; Other_DNA.
DR   EMBL; KF734118; AHI49132.1; -; Other_DNA.
DR   EMBL; KF734120; AHI49134.1; -; Other_DNA.
DR   EMBL; KF734150; AHI49160.1; -; Other_DNA.
DR   EMBL; KF734151; AHI49161.1; -; Other_DNA.
DR   EMBL; KF734152; AHI49162.1; -; Other_DNA.
DR   EMBL; KF734155; AHI49165.1; -; Other_DNA.
DR   EMBL; KF734156; AHI49166.1; -; Other_DNA.
DR   EMBL; KF734157; AHI49167.1; -; Other_DNA.
DR   EMBL; KF734158; AHI49168.1; -; Other_DNA.
DR   EMBL; KF734159; AHI49169.1; -; Other_DNA.
DR   EMBL; KF734163; AHI49172.1; -; Other_DNA.
DR   EMBL; KF734166; AHI49175.1; -; Other_DNA.
DR   EMBL; KF734167; AHI49176.1; -; Other_DNA.
DR   EMBL; KF734169; AHI49178.1; -; Other_DNA.
DR   EMBL; KF734174; AHI49182.1; -; Other_DNA.
DR   EMBL; KF734177; AHI49185.1; -; Other_DNA.
DR   EMBL; KF734178; AHI49186.1; -; Other_DNA.
DR   EMBL; KF734179; AHI49187.1; -; Other_DNA.
DR   EMBL; KF734181; AHI49188.1; -; Other_DNA.
DR   EMBL; KF734183; AHI49189.1; -; Other_DNA.
DR   EMBL; KF734184; AHI49190.1; -; Other_DNA.
DR   EMBL; KF734324; AHI49309.1; -; Other_DNA.
DR   EMBL; KF734325; AHI49310.1; -; Other_DNA.
DR   EMBL; KF734331; AHI49315.1; -; Other_DNA.
DR   EMBL; KF734335; AHI49317.1; -; Other_DNA.
DR   EMBL; KF734337; AHI49319.1; -; Other_DNA.
DR   EMBL; KF734344; AHI49326.1; -; Other_DNA.
DR   EMBL; KF734354; AHI49335.1; -; Other_DNA.
DR   EMBL; KF734356; AHI49337.1; -; Other_DNA.
DR   EMBL; KF734357; AHI49338.1; -; Other_DNA.
DR   EMBL; KF734358; AHI49339.1; -; Other_DNA.
DR   EMBL; KF734361; AHI49342.1; -; Other_DNA.
DR   EMBL; KF734366; AHI49347.1; -; Other_DNA.
DR   EMBL; KF734367; AHI49348.1; -; Other_DNA.
DR   EMBL; KF734368; AHI49349.1; -; Other_DNA.
DR   EMBL; KF734369; AHI49350.1; -; Other_DNA.
DR   EMBL; KF734372; AHI49352.1; -; Other_DNA.
DR   EMBL; KF734374; AHI49354.1; -; Other_DNA.
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:0039663; P:membrane fusion involved in 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; 2.
PE   4: Predicted;
KW   Apoptosis {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00936854};
KW   Cleavage on pair of basic residues {ECO:0000256|RuleBase:RU363095};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00881052};
KW   Fusion of virus membrane with host membrane
KW   {ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00487637};
KW   Host cell membrane {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00936840};
KW   Host endosome {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00936869};
KW   Host membrane {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00937255};
KW   Host-virus interaction {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00797036};
KW   Membrane {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00797370};
KW   Transmembrane {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00797262};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00797734};
KW   Viral attachment to host cell {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00797747};
KW   Viral envelope protein {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00797156, ECO:0000313|EMBL:AHI49131.1};
KW   Viral penetration into host cytoplasm {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00132213};
KW   Virion {ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00796948};
KW   Virus entry into host cell {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00797206}.
FT   TRANSMEM    510    533       Helical. {ECO:0000256|RuleBase:RU363095}.
FT   TRANSMEM    676    697       Helical. {ECO:0000256|RuleBase:RU363095}.
FT   DOMAIN       33    509       GP120. {ECO:0000259|Pfam:PF00516}.
FT   DOMAIN      528    717       GP41. {ECO:0000259|Pfam:PF00517}.
SQ   SEQUENCE   854 AA;  96972 MW;  F4A7CB534239E931 CRC64;
     MRVTEIRKSY QHWWRWGIML LGILMICNAE EKLWVTVYYG VPVWKEATTT LFCASDAKAY
     DTEEHNVWAT HACVPTDPNP QEVELKNVTE NFNMWKNNMV EQMHEDIISL WDQSLKPCVK
     LTPLCVTLNC TDLRNATNGN DTNTTSSSRG MVGGGEMKNC SFNITTNIRG KVQKEYALFY
     KLDIAPIDNN SNNRYRLISC NTSVITQACP KVSFEPIPIH YCAPAGFAIL KCKDKKFNGK
     GPCTNVSTVQ CTHGIRPVVS TQLLLNGSLA EEEVVIRSAN FADNAKIIIV QLNESVEINC
     TRPNNNTRKS IHIGPGRAFY TTGEIIGDIR QAHCNLSRAK WNDTLNKIVI KLREQFGNKT
     IVFKHSSGGD PEIVTHSFNC GGEFFYCDST QLFNSTWNVT EESNNTVENN TITLPCRIKQ
     IINMWQEVGR AMYAPPIRGQ IRCSSNITGL LLTRDGGPED NKTEVFRPGG GDMRDNWRSE
     LYKYKVVKIE PLGVAPTKAK RRVVQREKRA VGIGAVFLGF LGAAGSTMGA AAMTLTVQAR
     LLLSGIVQQQ NNLLRAIEAQ QHLLQLTVWG VKQLQARVLA VERYLRDQQL LGIWGCSGKL
     ICTTAVPWNA SWSNKSLNKI WDNMTWIEWD REINNYTSII YSLIEESQNQ QEKNEQELLE
     LDKWASLWNW FDITKWLWYI KIFIMIVGGL IGLRIVFSVL SIVNRVRQGY SPLSFQTHLP
     ASRGPDRPGG IEEEGGERDR DRSGPLVNGF LALIWVDLRS LFLFSYHRLR DLLLIVIRIV
     ELLGRRGWEV LKYWWNLLQY WSQELKNSAV SLLNATAVAV AEGTDRVIEV LQRAVRAILH
     IPRRIRQGLE RALL
//