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Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41); Surface protein gp120 (SU) (Glycoprotein 120) (gp120)]

 D7R5J3_9HIV1            Unreviewed;       841 AA.
D7R5J3;
10-AUG-2010, integrated into UniProtKB/TrEMBL.
10-AUG-2010, sequence version 1.
18-JUL-2018, entry version 60.
RecName: Full=Envelope glycoprotein gp160 {ECO:0000256|RuleBase:RU363095};
Contains:
RecName: Full=Surface protein gp120 {ECO:0000256|RuleBase:RU363095};
Short=SU {ECO:0000256|RuleBase:RU363095};
AltName: Full=Glycoprotein 120 {ECO:0000256|RuleBase:RU363095};
Short=gp120 {ECO:0000256|RuleBase:RU363095};
Contains:
RecName: Full=Transmembrane protein gp41 {ECO:0000256|RuleBase:RU363095};
Short=TM {ECO:0000256|RuleBase:RU363095};
Name=env {ECO:0000313|EMBL:ADH82016.1};
Human immunodeficiency virus 1.
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
NCBI_TaxID=11676 {ECO:0000313|EMBL:ADH82016.1};
NCBI_TaxID=9606; Homo sapiens (Human).
[1] {ECO:0000313|EMBL:ADH82016.1}
NUCLEOTIDE SEQUENCE.
STRAIN=34M.BML.240 {ECO:0000313|EMBL:ADH82016.1};
PubMed=20422033; DOI=10.1371/journal.pone.0010213;
Heath L., Conway S., Jones L., Semrau K., Nakamura K., Walter J.,
Decker W.D., Hong J., Chen T., Heil M., Sinkala M., Kankasa C.,
Thea D.M., Kuhn L., Mullins J.I., Aldrovandi G.M.;
"Restriction of HIV-1 genotypes in breast milk does not account for
the population transmission genetic bottleneck that occurs following
transmission.";
PLoS ONE 5:E10213-E10213(2010).
[2] {ECO:0000313|EMBL:ADH82016.1}
NUCLEOTIDE SEQUENCE.
STRAIN=34M.BML.240 {ECO:0000313|EMBL:ADH82016.1};
Heath L.M., Conway S., Jones L., Semrau K., Nakamura K., Walter J.,
Decker D., Hong J., Heil M., Sinkala M., Kankasa C., Thea D.M.,
Kuhn L., Mullins J.I., Aldrovandi G.M.;
Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
-!- SUBUNIT: The mature envelope protein (Env) consists of a
homotrimer of non-covalently associated gp120-gp41 heterodimers.
The resulting complex protrudes from the virus surface as a spike.
{ECO:0000256|RuleBase:RU363095}.
-!- SUBCELLULAR LOCATION: Host cell membrane
{ECO:0000256|SAAS:SAAS01060237}; Peripheral membrane protein
{ECO:0000256|SAAS:SAAS01060237}. Host cell membrane
{ECO:0000256|SAAS:SAAS01060091}; Single-pass type I membrane
protein {ECO:0000256|SAAS:SAAS01060091}. Host endosome membrane
{ECO:0000256|SAAS:SAAS01060316}; Single-pass type I membrane
protein {ECO:0000256|SAAS:SAAS01060316}. Virion membrane
{ECO:0000256|SAAS:SAAS00796993}; Single-pass type I membrane
protein {ECO:0000256|SAAS:SAAS00796993}.
-!- DOMAIN: The 17 amino acids long immunosuppressive region is
present in many retroviral envelope proteins. Synthetic peptides
derived from this relatively conserved sequence inhibit immune
function in vitro and in vivo. {ECO:0000256|RuleBase:RU363095}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|RuleBase:RU363095}.
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EMBL; HM036934; ADH82016.1; -; Genomic_RNA.
ProteinModelPortal; D7R5J3; -.
GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
GO; GO:0090527; P:actin filament reorganization; IEA:UniProtKB-UniRule.
GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-UniRule.
GO; GO:0030683; P:evasion or tolerance by virus of host immune response; IEA:UniProtKB-UniRule.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule.
GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
GO; GO:1903905; P:positive regulation of establishment of T cell polarity; IEA:UniProtKB-UniRule.
GO; GO:1903908; P:positive regulation of plasma membrane raft polarization; IEA:UniProtKB-UniRule.
GO; GO:1903911; P:positive regulation of receptor clustering; IEA:UniProtKB-UniRule.
GO; GO:0019082; P:viral protein processing; IEA:UniProtKB-UniRule.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
CDD; cd09909; HIV-1-like_HR1-HR2; 1.
Gene3D; 2.170.40.20; -; 2.
HAMAP; MF_04083; HIV_ENV; 1.
InterPro; IPR036377; Gp120_core_sf.
InterPro; IPR037527; Gp160.
InterPro; IPR000328; GP41-like.
InterPro; IPR000777; HIV1_Gp120.
Pfam; PF00516; GP120; 2.
Pfam; PF00517; GP41; 1.
SUPFAM; SSF56502; SSF56502; 2.
3: Inferred from homology;
Apoptosis {ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS01060203};
Cleavage on pair of basic residues {ECO:0000256|RuleBase:RU363095};
Disulfide bond {ECO:0000256|SAAS:SAAS01050261};
Fusion of virus membrane with host membrane
{ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS01050351};
Host cell membrane {ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS01060118};
Host endosome {ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS01060155};
Host membrane {ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS01060118};
Host-virus interaction {ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS00797747};
Membrane {ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS00797734, ECO:0000256|SAAS:SAAS01060118};
Transmembrane {ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS00797734};
Transmembrane helix {ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS00797734};
Viral attachment to host cell {ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS00797747};
Viral envelope protein {ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS00797156, ECO:0000313|EMBL:ADH82016.1};
Viral penetration into host cytoplasm {ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS01050351};
Virion {ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00797156,
ECO:0000256|SAAS:SAAS00797747, ECO:0000313|EMBL:ADH82016.1};
Virus entry into host cell {ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS00797747, ECO:0000256|SAAS:SAAS01050351}.
TRANSMEM 13 35 Helical. {ECO:0000256|RuleBase:RU363095}.
TRANSMEM 503 528 Helical. {ECO:0000256|RuleBase:RU363095}.
TRANSMEM 669 696 Helical. {ECO:0000256|RuleBase:RU363095}.
DOMAIN 33 138 GP120. {ECO:0000259|Pfam:PF00516}.
DOMAIN 151 502 GP120. {ECO:0000259|Pfam:PF00516}.
DOMAIN 521 712 GP41. {ECO:0000259|Pfam:PF00517}.
SEQUENCE 841 AA; 95261 MW; 79A824A5AFCDE467 CRC64;
MRVRGILRNW QQWWMWGILG FWMVLICNVT GKLWVTVYYG VPVWKEAKTT LFCASDAKGY
EKEVHNVWAT HACVPTDPNP QELVLENVTE NFNMWKNDMV DQMHEDVISL WDQSLKPCIK
LTPLCVTLNC VDATSVNDIS NGKGTYNISK DGEIKNCSFN ITTELKDRKK NVYALFYRLD
IVPIDGNKSR VYTLINCNTS AIAKACPKVS FDPIPIHYCA PAGYAILKCN NKTFNGTGPC
QNVSTVQCTH GIKPVVSTQL LLNGSLAEEE IIIRSENLTD NTKTIIAHLN ESIKIECVRP
NNNIRESIRI GPGQAFYATG GIIGDIRQAY CNISEGAWNI TLQGIKEKLE KYFPNKTIQF
APALGGDLEI VTHSFNCRGE FFYCNTSELF NTSALFNRTS NSSITLPCRI KQFINMWQEV
GRAMYAPPIA GAINCTSNIT GLLLTRDGGN DPNSTEEIFR PGGGNMKDNW RSELYKYKVV
EIKPLGIAPT EAKRRVVERE KRAVGIGAVI FGFLGAAGST MGAASIALTA QARQVLSGIV
RQQNNLLRAI EAQQHMLQLT VWGIKQLQAR VLAIERYLKD QQLLGLWGCS GKFICTTNVP
WNSTWSDREK DDIWNNMTWM QWDKEISNYT DTIYKLLEES QYQQDKNEKD LLALDSWKNL
WNWFDISNWL WYIKIFIMIV GGLIGLRIIF AVLSIVNRVR QGYSPLSFQT LTPNPRGLDR
LGGIEEEGGE QDRDRSIRLV NGFLALAWDD LRSLCLFSYH RLRDFILIAA RAAELLGRSS
LRGLQRGWEA LKYLGSLVQY WGLELKKSAI SLFDALAIAV AERTDRVINL IQRIWRAIRN
E


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