ID C4NL92_SIV Unreviewed; 887 AA.
AC C4NL92;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
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:ACQ87456.1};
OS Simian immunodeficiency virus (SIV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11723 {ECO:0000313|EMBL:ACQ87456.1};
OH NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1] {ECO:0000313|EMBL:ACQ87456.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CG7V.RU.D3 {ECO:0000313|EMBL:ACQ87456.1};
RX PubMed=19414559; DOI=10.1084/jem.20082831;
RA Keele B.F., Li H., Learn G.H., Hraber P., Giorgi E.E., Grayson T., Sun C.,
RA Chen Y., Yeh W.W., Letvin N.L., Mascola J.R., Nabel G.J., Haynes B.F.,
RA Bhattacharya T., Perelson A.S., Korber B.T., Hahn B.H., Shaw G.M.;
RT "Low-dose rectal inoculation of rhesus macaques by SIVsmE660 or SIVmac251
RT recapitulates human mucosal infection by HIV-1.";
RL J. Exp. Med. 206:1117-1134(2009).
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; FJ578494; ACQ87456.1; -; Genomic_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: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:ACQ87456.1};
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..767
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; 102181 MW; C3F12609BEE8CA91 CRC64;
MGCLGNQLLI ALLLVSALEI YCVQYVTVFY GVPAWKNATI PLFCATKNRD TWGTTQCLPD
NDDYSELAIS ITEAFDAWNN TVTEQAIEDV WNLFETSIKP CVKLTPLCIA MRCNKTETDR
WGLTRNAGTT TTTTTTTTAA TPSVAENVIN ESNPCIKNNS CAGLEQEPMI GCKFNMTGLK
RDKRIEYNET WYSRDLICEQ SANESESKCY MHHCNTSVIQ ESCDKHYWDA IRFRYCAPPG
YALLRCNDSN YSGFAPNCSK VVVSSCTRMM ETQTSTWFGF NGTRAENRTY IYWHGKSNRT
IISLNKYYNL TMRCRRPGNK TVLPVTIMSG LVFHSQPINE RPKQAWCWFG GSWKEAIQEV
KETLVKHPRY TGTNDTKKIN LTAPAGGDPE VTFMWTNCRG EFLYCKMNWF LNWVEDRDQK
SSRWRQQNTR ERQKKNYVPC HIRQIINTWH KVGKNVYLPP REGDLTCNST VTSLIAEIDW
TNNNETNITM SAEVAELYRL ELGDYKLVEI TPIGLAPTSV RRYTTTGASR NKRGVFVLGF
LGFLATAGSA MGAASLTLSA QSRTLLVGIV QQQQQLLDVV KRQQELLRLT VWGTKNLQTR
VTAIEKYLKD QAQLNSWGCA FRQVCHTTVP WPNETLVPNW SNMTWQEWER QVDFLEANIT
QLLEEAQIQQ EKNMYELQKL NSWDIFGNWF DLTSWIRYIQ YGVLIVLGVV GLRIVIYVVQ
MLARLRQGYR PVFSSPPAYV QQIPIHKGQE PPTKEGEEGE GGDRGGSRSW PWQIEYIHFL
IRQLIRLLTW LFSSCRDWLL RTYQILQPVL QSLSTTLQRV REVIRIGIAY LQYGWRYFQE
AVQAWWKFAR ETLASAWRDI WETLGRVGRG ILAIPRRIRQ GLEITLL
//
