ID C4NPU9_SIV Unreviewed; 886 AA.
AC C4NPU9;
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:ACQ88713.1};
OS Simian immunodeficiency virus (SIV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11723 {ECO:0000313|EMBL:ACQ88713.1};
OH NCBI_TaxID=9527; Cercopithecidae (Old World monkeys).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1] {ECO:0000313|EMBL:ACQ88713.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CP3C.PK.A7 {ECO:0000313|EMBL:ACQ88713.1};
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; FJ578815; ACQ88713.1; -; 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:ACQ88713.1};
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 697..718
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363095"
FT DOMAIN 24..532
FT /note="Human immunodeficiency virus 1 envelope glycoprotein
FT Gp120"
FT /evidence="ECO:0000259|Pfam:PF00516"
FT DOMAIN 550..744
FT /note="Retroviral envelope protein GP41-like"
FT /evidence="ECO:0000259|Pfam:PF00517"
FT REGION 744..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 644..671
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 749..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 102164 MW; A43F265B774DC8E5 CRC64;
MGCLGNQLLI ALLLVSALEI YCVQYVTVFY GVPAWKNATI PLFCTTRNRD TWGTTQCLPD
NDDYSELAIN ITEAFDAWNN TVTEQAIEDV WNLFETSIKP CVKLTPLCIA MRCNKTETDR
WGLTRNAGTT TTSTTTTAAT PSVAENVINE SNPCIKNNNC AGLEQEPMIG CKFNMTGLKR
DKRIEYNETW YSRDLICEQS ANESESKCYM HHCNTSVIQE SCDKHYWDAI RFRYCAPPGY
ALLRCNDSNY SGFAPNCSKV VVSSCTRMME TQTSTWFGFN GTRAENRTYI YWHGKSNRTI
ISLNKYYNLT MRCRRPGNKT VLPVTIMSGL VFHSQPINER PKQAWCWFGG SWKEAIQEVR
ETLVKHPRYT GTNDTKKINL TAPAGGDPEV TFMWTNCRGE FLYCKMNWFL NWVEDRDQKS
SRWRQQNTKE RQKKNYVPCH IRQIINTWHK VGKNVYLPPR EGDLTCNSTV TSLIAEIDWT
NNNETNITMS AEVAELYRLE LGDYKLVEIT PIGLAPTSVR RYTTTGASRN KRGVFVLGFL
GFLATAGSAM GAASLTLSAQ SRTLLAGIVQ QQQQLLDVVK RQQELLRLTV WGTKNLQTRV
TAIEKYLKDQ AQLNSWGCAF RQVCHTTVPW PNETLVPNWS NMTWQEWERQ VDFLEANITQ
LLEEAQIQQE KNMYELQKLN SWDIFGNWFD LTSWIRYIQY GVLIVLGVVG LRIVIYVVQM
LARLRQGYRP VFSSPPAYVQ QIPIHKGQEP PTKEGEEGEG GDRGGSRSWP WQIEYIHFLI
RQLIRLLTWL FSSCRDWLLR TYQILQPVLQ SLSTTLRRVR EVIRIGIAYL QYGWRYFQEA
VQAWWKFARE TLASAWRDIW ETLGRVGRGI LAIPRRVRQG LELTLL
//
