ID V9PM76_SIV Unreviewed; 887 AA.
AC V9PM76;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
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:AHA32603.1};
OS Simian immunodeficiency virus (SIV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11723 {ECO:0000313|EMBL:AHA32603.1};
OH NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1] {ECO:0000313|EMBL:AHA32603.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SIVsmE660 {ECO:0000313|EMBL:AHA32603.1};
RX PubMed=24352234;
RA Roederer M., Keele B.F., Schmidt S.D., Mason R.D., Welles H.C., Fischer W.,
RA Labranche C., Foulds K.E., Louder M.K., Yang Z.Y., Todd J.P., Buzby A.P.,
RA Mach L.V., Shen L., Seaton K.E., Ward B.M., Bailer R.T., Gottardo R.,
RA Gu W., Ferrari G., Alam S.M., Denny T.N., Montefiori D.C., Tomaras G.D.,
RA Korber B.T., Nason M.C., Seder R.A., Koup R.A., Letvin N.L., Rao S.S.,
RA Nabel G.J., Mascola J.R.;
RT "Immunological and virological mechanisms of vaccine-mediated protection
RT against SIV and HIV.";
RL Nature 0:0-0(2013).
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}.
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DR EMBL; KF603037; AHA32603.1; -; 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: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; 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}; 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:AHA32603.1};
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..533
FT /note="Human immunodeficiency virus 1 envelope glycoprotein
FT Gp120"
FT /evidence="ECO:0000259|Pfam:PF00516"
FT DOMAIN 551..745
FT /note="Retroviral envelope protein GP41-like"
FT /evidence="ECO:0000259|Pfam:PF00517"
FT REGION 745..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 645..672
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 750..764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 887 AA; 102150 MW; 7DEAA132D593ED65 CRC64;
MGCLGNQLLI ALLLVSALEI YCVQYVTVFY GVPAWKNATI PLFCTTRNRD TWGTTQCLPD
NDDYSELAIS ITEAFDAWNN TVTEQAIEDV WNLFETSIKP CVKLTPLCIA MRCNKTETDR
WGLTRNAGTT TTTTTTTTAA TPSVAENVIN ESNPCIKNNS CAGLEQEPMI GCKFNMTGLK
RDKRIEYNET WYSRDLICEQ SANESESKCY MHHGNTSVIQ ESCDKHYWDA IRFRYCAPPG
YALLRCNDSN YSGFAPNCSK VVVSSCTRMM ETQTSTWFGF NGTRAENRTY IYWHGKSNRT
IISLNKYYNL TMRCKRPGNK TVLPVTIMSG LVFHSQPINE RPKQAWCWFG GSWKEAIQEV
KETLVKHPRY TGTNDTRKIN LTAPAGGDPE VTFMWTNCRG EFLYCKMNWF LNWVEDRDQK
SSRWRQQNTR ERQKKNYVPC HIRQIINTWH KVGKNVYLPP REGDLTCNST VTSLIAEIDW
TNNNETNITM SAEVAELYRL ELGDYKLVEI TPIGLAPTSV RRYTTTGASR NKRGVFVLGF
LGFLATAGSA MGAASLTLSA QSRTLLAGIV QQQQQLLDVV KRQQELLRLT VWGTKNLQTR
VTAIEKYLKD QAQLNSWGCA FRQVCHTTVP WPNETLVPNW SNMTWQEWER QVDFLEANIT
QLLEEAQIQQ EKNMYELQKL NSWDIFGNWF DLTSWIRYIQ YGVLIVLGVV GLRIVIYVVQ
MLARLRQGYR PVFSSPPAYV QQIPIHKGQE PPTKEGEEGE GGDRGGNRSW PWQIEYIHFL
IRQLIRLLTW LFSSCRDWLL RIYQVLQPVL QSLSTTSQRV REVIRIGIAY LQYGWRYFQE
AVQAWWKFAR ETLASAWRDI WETLGRVGRG ILAIPRRVRQ GLELTLL
//
