ID Q45FU5_SIV Unreviewed; 879 AA.
AC Q45FU5;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 109.
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:AAZ52605.1};
OS Simian immunodeficiency virus - mac.
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus;
OC Simian immunodeficiency virus.
OX NCBI_TaxID=11711 {ECO:0000313|EMBL:AAZ52605.1};
RN [1] {ECO:0000313|EMBL:AAZ52605.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16798669; DOI=10.1080/13550280600654565;
RA Chen M.F., Westmoreland S., Ryzhova E.V., Martin-Garcia J., Soldan S.S.,
RA Lackner A., Gonzalez-Scarano F.;
RT "Simian immunodeficiency virus envelope compartmentalizes in brain regions
RT independent of neuropathology.";
RL J. Neurovirol. 12:73-89(2006).
CC -!- FUNCTION: Surface protein gp120 (SU) may target the virus to gut-
CC associated lymphoid tissue (GALT) by binding host ITGA4/ITGB7 (alpha-
CC 4/beta-7 integrins), a complex that mediates T-cell migration to the
CC GALT. Interaction between gp120 and ITGA4/ITGB7 would allow the virus
CC to enter GALT early in the infection, infecting and killing most of
CC GALT's resting CD4+ T-cells. This T-cell depletion is believed to be
CC the major insult to the host immune system leading to AIDS.
CC {ECO:0000256|ARBA:ARBA00037206}.
CC -!- FUNCTION: The envelope glycoprotein gp160 precursor down-modulates cell
CC surface CD4 antigen by interacting with it in the endoplasmic reticulum
CC and blocking its transport to the cell surface.
CC {ECO:0000256|ARBA:ARBA00037137}.
CC -!- FUNCTION: The gp120-gp41 heterodimer allows rapid transcytosis of the
CC virus through CD4 negative cells such as simple epithelial monolayers
CC of the intestinal, rectal and endocervical epithelial barriers. Both
CC gp120 and gp41 specifically recognize glycosphingolipids galactosyl-
CC ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the
CC lipid rafts structures of epithelial cells. Binding to these
CC alternative receptors allows the rapid transcytosis of the virus
CC through the epithelial cells. This transcytotic vesicle-mediated
CC transport of virions from the apical side to the basolateral side of
CC the epithelial cells does not involve infection of the cells
CC themselves. {ECO:0000256|ARBA:ARBA00037366}.
CC -!- FUNCTION: The surface protein gp120 (SU) attaches the virus to the host
CC lymphoid cell by binding to the primary receptor CD4. This interaction
CC induces a structural rearrangement creating a high affinity binding
CC site for a chemokine coreceptor like CCR5. This peculiar 2 stage
CC receptor-interaction strategy allows gp120 to maintain the highly
CC conserved coreceptor-binding site in a cryptic conformation, protected
CC from neutralizing antibodies. These changes are transmitted to the
CC transmembrane protein gp41 and are thought to activate its fusogenic
CC potential by unmasking its fusion peptide.
CC {ECO:0000256|ARBA:ARBA00037419}.
CC -!- FUNCTION: The transmembrane protein gp41 (TM) acts as a class I viral
CC fusion protein. Under the current model, the protein has at least 3
CC conformational states: pre-fusion native state, pre-hairpin
CC intermediate state, and post-fusion hairpin state. During fusion of
CC viral and target intracellular membranes, the coiled coil regions
CC (heptad repeats) assume a trimer-of-hairpins structure, positioning the
CC fusion peptide in close proximity to the C-terminal region of the
CC ectodomain. The formation of this structure appears to drive apposition
CC and subsequent fusion of viral and target cell membranes. Complete
CC fusion occurs in host cell endosomes. The virus undergoes clathrin-
CC dependent internalization long before endosomal fusion, thus minimizing
CC the surface exposure of conserved viral epitopes during fusion and
CC reducing the efficacy of inhibitors targeting these epitopes. Membranes
CC fusion leads to delivery of the nucleocapsid into the cytoplasm.
CC {ECO:0000256|ARBA:ARBA00037086}.
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. Interacts with
CC host CD4 and CCR5 (By similarity). Gp120 also interacts with the C-type
CC lectins CD209/DC-SIGN and CLEC4M/DC-SIGNR (collectively referred to as
CC DC-SIGN(R)). {ECO:0000256|ARBA:ARBA00038686}.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU363095}.
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DR EMBL; DQ136227; AAZ52605.1; -; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, 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:AAZ52605.1};
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 6..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363095"
FT TRANSMEM 527..548
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363095"
FT TRANSMEM 690..711
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363095"
FT DOMAIN 24..525
FT /note="Human immunodeficiency virus 1 envelope glycoprotein
FT Gp120"
FT /evidence="ECO:0000259|Pfam:PF00516"
FT DOMAIN 543..737
FT /note="Retroviral envelope protein GP41-like"
FT /evidence="ECO:0000259|Pfam:PF00517"
FT COILED 637..664
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 879 AA; 100834 MW; 81F32BBA98246657 CRC64;
MGCLGNQLLI AILLLSVYGI YCTLYVTVFY GVPAWRNATI PLFCATKNRD AWGTTQCLPD
NDDYSEMALN VTESFDAWNN TVTEQAIEDV WQLFETSIKP CVKLSPLCIT MRCNKSETGR
RGLTKSITTT ASTTSTTASA EVDMVNETSS CIAQDNCTGL EQEQMISCKF NMTGLKRDKK
KEYNETWYSA DLVCEQGNNT GNESRCYMNH CNTSVIQESC DKHCWDAIRF RYCAPPGYAL
LRCNGTNYSG FMPKCSKVVV SSCTRMMETQ TSTWFGFNGT RAENRTYIYW HGRDNRTIIS
LNKYYNLTMK CRRPGNKTVL PVTIMSGLVF HSQPINDRPR QAWCRFGGKW KDAIKEVKQT
IVKHPRYTGT NDTDKINLTA PGGGDPEVTF MWTNCRGEFL YCKMNWFLNW VEDRNTTNQK
PNEQHKRNYV PCHIRQIINT WHKVGRNVYL PPREGDLTCN STVTSLIANI DWIDGNQTNI
TMSAEVAELY RLELGDYKLV EITPIGLAPT HVKRYTTGGT SRNKRGVFVL GFLGFLATAG
SAMGAASLTL TAQSRTLLAG IVQQQQQLLD VVKRQQELLR LTVWGTKNLQ TRVTAIEKYL
KDQAQLNAWG CAFRQVCHTT VPWPNASLTP DWNNETWQEW ERKVDLLEEN ITALLEEAQI
QQEKNMYELQ KLNSWDVFGN WFDLASWIKY IQYGVYIVVG VILLRIVIYI VQMLAKLRQG
YRPVFSSPPS YFQQTHIQQD PALPTREGKE GDGGEGGGNS SWPWQIEYIH FLIRQLIRLL
TWLFSNCRTL LSRVYQILQP IFQRLSATLQ RIREVFRTEL TYLQYGWSYF HEAVQAGWRS
TTETLASAWG DLWETLRRGG RWILAIPRRI RQGLELTLL
//
