ID D1G711_SIV Unreviewed; 885 AA.
AC D1G711;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
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:ACY94205.1};
OS Simian immunodeficiency virus (SIV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11723 {ECO:0000313|EMBL:ACY94205.1};
OH NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1] {ECO:0000313|EMBL:ACY94205.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R02012.d15.A18 {ECO:0000313|EMBL:ACY94205.1};
RA Keele B.F.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; FJ706878; ACY94205.1; -; 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:ACY94205.1};
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 696..717
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363095"
FT DOMAIN 24..531
FT /note="Human immunodeficiency virus 1 envelope glycoprotein
FT Gp120"
FT /evidence="ECO:0000259|Pfam:PF00516"
FT DOMAIN 549..743
FT /note="Retroviral envelope protein GP41-like"
FT /evidence="ECO:0000259|Pfam:PF00517"
FT REGION 743..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 643..670
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 748..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 885 AA; 102022 MW; 1A344E0746ED0929 CRC64;
MGCLGNQLLI ALLLVSALEI YCVQYVTVFY GVPAWKNATI PLFCTTRNRD TWGTTQCLPD
NDDYSELAIN ITEAFDAWNN TVTEQAIEDV WNLFETSIKP CVKLTPLCIA MRCNKTETDR
WGLTRNAGTT TTTTTTAATP SVAENVINES NPCIKNNSCA GLEQEPMIGC KFNMTGLKRD
KRIEYNETWY SRDLICEQSA NESESKCYMH HCNTSVIQES CDKHYWDAIR FRYCAPPGYA
LLRCNDSNYS GFAPNCSKVV VSSCTRIMET QTSTWFGFNG TRAENRTYIY WHGKSNRTII
SLNKYYNLTM RCRRPGNKTV LPVTIMSGLV FHSQPINERP KQAWCWFGGS WKEAIQEVKE
TLVKHPRYTG TNDTKKINLT APAGGDPEVT FMWTNCRGEF LYCKMNWFLN WVEDRDQKSS
RWRQQNTRER QKKNYVPCHI RQIINTWHKV GKNVYLPPRE GDLTCNSTVT SLIAEIDWTN
NNETNITMSA EVAELYRLEL GDYKLVEITP IGLAPTSVRR YTTTGASRNK RGVFVLGFLG
FLATAGSAMG AASLTLSAQS RTLLAGIVQQ QQQLLDVVKR QQELLRLTVW GTKNLQTRVT
AIEKYLKDQA QLNSWGCAFR QVCHTTVPWP NETLVPNWSN MTWQEWERQV DFLEANITQL
LEEAQIQQEK NMYELQKLNS WDIFGNWFDL TSWIRYIQYG VLIVLGVVGL RIVIYVVQML
ARLRQGYRPV FSSPPAYVQQ IPIHKGQEPP TKEGEEGEGG DRGGSRSWPW QIEYIHFLIR
QLIRLLTWLF SSCRDWLLRT YQILQPVLQS LSTTLQRVRE VIRIGIAYLQ YGWRYFQEAV
QAWWKFARET LASAWRDIWE TLGRVGRGIL AIPRRIRQGF ELALL
//
