ID   A0A0K1SD39_9HIV1        Unreviewed;       845 AA.
AC   A0A0K1SD39;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   30-NOV-2016, entry version 12.
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:AKV72548.1};
OS   Human immunodeficiency virus 1.
OC   Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
OC   Lentivirus; Primate lentivirus group.
OX   NCBI_TaxID=11676 {ECO:0000313|EMBL:AKV72548.1};
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1] {ECO:0000313|EMBL:AKV72548.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CH0457_w04_e14 {ECO:0000313|EMBL:AKV72548.1};
RX   PubMed=26355218; DOI=10.1016/j.chom.2015.08.006;
RA   Moody M.A., Gao F., Gurley T.C., Amos J.D., Kumar A., Hora B.,
RA   Marshall D.J., Whitesides J.F., Xia S.M., Parks R., Lloyd K.E.,
RA   Hwang K.K., Lu X., Bonsignori M., Finzi A., Vandergrift N.A.,
RA   Alam S.M., Ferrari G., Shen X., Tomaras G.D., Kamanga G., Cohen M.S.,
RA   Sam N.E., Kapiga S., Gray E.S., Tumba N.L., Morris L.,
RA   Zolla-Pazner S., Gorny M.K., Mascola J.R., Hahn B.H., Shaw G.M.,
RA   Sodroski J.G., Liao H.X., Montefiori D.C., Hraber P.T., Korber B.T.,
RA   Haynes B.F.;
RT   "Strain-Specific V3 and CD4 Binding Site Autologous HIV-1 Neutralizing
RT   Antibodies Select Neutralization-Resistant Viruses.";
RL   Cell Host Microbe 18:354-362(2015).
RN   [2] {ECO:0000313|EMBL:AKV72548.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CH0457_w04_e14 {ECO:0000313|EMBL:AKV72548.1};
RA   Hoefler B.C., Straight P.D.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:SAAS00595638}; Single-pass type I membrane
CC       protein {ECO:0000256|SAAS:SAAS00595638}.
CC   -!- SUBCELLULAR LOCATION: Host endosome membrane
CC       {ECO:0000256|SAAS:SAAS00595816}; Single-pass type I membrane
CC       protein {ECO:0000256|SAAS:SAAS00595816}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane
CC       {ECO:0000256|SAAS:SAAS00595588}; Single-pass type I membrane
CC       protein {ECO:0000256|SAAS:SAAS00595588}.
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; KT220838; AKV72548.1; -; 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: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-KW.
DR   CDD; cd09909; HIV-1-like_HR1-HR2; 1.
DR   Gene3D; 2.170.40.20; -; 2.
DR   InterPro; IPR000328; GP41-like.
DR   InterPro; IPR000777; HIV1_GP160.
DR   Pfam; PF00516; GP120; 2.
DR   Pfam; PF00517; GP41; 1.
DR   SUPFAM; SSF56502; SSF56502; 2.
PE   4: Predicted;
KW   Apoptosis {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00491382};
KW   Cleavage on pair of basic residues {ECO:0000256|RuleBase:RU363095};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00487956};
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:SAAS00491210};
KW   Host endosome {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00491443};
KW   Host membrane {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00493156};
KW   Host-virus interaction {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00490508};
KW   Membrane {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00491184};
KW   Transmembrane {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00491847};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00490549};
KW   Viral attachment to host cell {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00490424};
KW   Viral envelope protein {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00490691, ECO:0000313|EMBL:AKV72548.1};
KW   Viral penetration into host cytoplasm {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00486890};
KW   Virion {ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00491099};
KW   Virus entry into host cell {ECO:0000256|RuleBase:RU363095,
KW   ECO:0000256|SAAS:SAAS00490724}.
FT   TRANSMEM     13     41       Helical. {ECO:0000256|RuleBase:RU363095}.
FT   TRANSMEM    494    517       Helical. {ECO:0000256|RuleBase:RU363095}.
FT   TRANSMEM    660    687       Helical. {ECO:0000256|RuleBase:RU363095}.
FT   DOMAIN       33    141       GP120. {ECO:0000259|Pfam:PF00516}.
FT   DOMAIN      141    493       GP120. {ECO:0000259|Pfam:PF00516}.
FT   DOMAIN      512    702       GP41. {ECO:0000259|Pfam:PF00517}.
SQ   SEQUENCE   845 AA;  95863 MW;  07DECD935EEB4505 CRC64;
     MKVMEILRKW KHWWIWGILG FWMLLISNVM GNLWVTVYYG VPVWREAKTT LFCASDAKAY
     EREVHNVWAT HACVPTDPNP QEMRLENVTE NFNMWKNDMV DQMHEDIISL WDQSLKPCVK
     LTPLCVTLRC ENATYNDTNY KNITDGEVMN CSFNITTEIR DKRRKESALF YRVDIVPLDN
     NSAEYRLINC KTSSLTQACP KISFDPIPIH YCAPAGYAIL KCNNKTFNGT GPCNSVSTVQ
     CTHGIKPVVS TQLLLNGSLA EEDIIIRSEN LTDNAKIIIV HLNKSVEIRC TRPGNNTRKS
     VRIGPGQTFY ATGEIIGDIR KAHCNISRSK WNEALERISN KLEAHFPNKT IQFNSSSGGD
     LEITTHSFNC RGEFFYCNTS KLFNNNRTSN NSSYITIPCK IKQIINMWQK VGKAMYAPPI
     AGNITCTSNI TGILSTRDGG NNSDSDPETF RPTGGDMRDN WRSELYKYKV VEVEPLGIAP
     TGAKRRVVER QKRAVGMGAM FLGFLGAAGS TMGAASITLT VQARQLLSGI VQQQSNLLRA
     IEAQQHILQL TVWGIKQLQT RILAIERYLK DQQLLGIWGC SGKLICTTSV PWNSSWSNKS
     ESEIWNNMTW MQWDKEISNY TNTIYRLLEE SQNQQEKNEQ DLLALDSWKN LWSWFSITNW
     LWYIKIFIMI VGGLIGLRII FAILSIVNRV RQGYSPLSFQ TLTPNPRGPD RLGRIEEGGG
     EQDNARSTRL VSGFLALAWD DLRSLFLFSY HRLRDFTLIV VGGGELLGRS SLRGLQKGWE
     TLKYLGNLVQ YWGLELKRSA ISLLDTIAIA TAEGTDRIIE LVQRICRAIC NVPTRIRQGF
     EAALQ
//