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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)]

 Q0ED31_9HIV1            Unreviewed;       857 AA.
Q0ED31;
17-OCT-2006, integrated into UniProtKB/TrEMBL.
17-OCT-2006, sequence version 1.
18-JUL-2018, entry version 116.
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:BAF31376.1};
Human immunodeficiency virus 1.
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
NCBI_TaxID=11676 {ECO:0000313|EMBL:BAF31376.1, ECO:0000313|Proteomes:UP000180781};
NCBI_TaxID=9606; Homo sapiens (Human).
[1] {ECO:0000313|EMBL:BAF31376.1, ECO:0000313|Proteomes:UP000180781, ECO:0000313|Proteomes:UP000181403}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=93TH057 {ECO:0000313|EMBL:BAF31376.1};
Sakamoto Y., Takekawa N., Tatsumi M.;
"Construction and characterization of HIV-1 CRF01_AE infectious
molecular clones.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000213|PDB:3NGB}
X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 43-122; 201-303 AND 325-486,
GLYCOSYLATION AT ASN-87; ASN-236; ASN-243; ASN-264; ASN-278; ASN-291;
ASN-297; ASN-335; ASN-386; ASN-392 AND ASN-442, AND DISULFIDE BONDS.
PubMed=20616231; DOI=10.1126/science.1192819;
Zhou T., Georgiev I., Wu X., Yang Z.Y., Dai K., Finzi A., Kwon Y.D.,
Scheid J.F., Shi W., Xu L., Yang Y., Zhu J., Nussenzweig M.C.,
Sodroski J., Shapiro L., Nabel G.J., Mascola J.R., Kwong P.D.;
"Structural basis for broad and potent neutralization of HIV-1 by
antibody VRC01.";
Science 329:811-817(2010).
[3] {ECO:0000213|PDB:3SE8, ECO:0000213|PDB:3SE9}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 43-486, GLYCOSYLATION AT
ASN-87; ASN-160 AND ASN-188, AND DISULFIDE BONDS.
PubMed=21835983; DOI=10.1126/science.1207532;
NISC Comparative Sequencing Program;
Wu X., Zhou T., Zhu J., Zhang B., Georgiev I., Wang C., Chen X.,
Longo N.S., Louder M., McKee K., O'Dell S., Perfetto S., Schmidt S.D.,
Shi W., Wu L., Yang Y., Yang Z.Y., Yang Z., Zhang Z., Bonsignori M.,
Crump J.A., Kapiga S.H., Sam N.E., Haynes B.F., Simek M., Burton D.R.,
Koff W.C., Doria-Rose N.A., Connors M., Mullikin J.C., Nabel G.J.,
Roederer M., Shapiro L., Kwong P.D., Mascola J.R.;
"Focused evolution of HIV-1 neutralizing antibodies revealed by
structures and deep sequencing.";
Science 333:1593-1602(2011).
[4] {ECO:0000213|PDB:4DKO, ECO:0000213|PDB:4DKP, ECO:0000213|PDB:4DKQ}
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 43-486, GLYCOSYLATION AT
ASN-160 AND ASN-188, AND DISULFIDE BONDS.
PubMed=22497421; DOI=10.1021/jm300265j;
LaLonde J.M., Kwon Y.D., Jones D.M., Sun A.W., Courter J.R., Soeta T.,
Kobayashi T., Princiotto A.M., Wu X., Schon A., Freire E., Kwong P.D.,
Mascola J.R., Sodroski J., Madani N., Smith A.B.;
"Structure-based design, synthesis, and characterization of dual
hotspot small-molecule HIV-1 entry inhibitors.";
J. Med. Chem. 55:4382-4396(2012).
[5] {ECO:0000213|PDB:3TGT}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 43-486, GLYCOSYLATION AT
ASN-160 AND ASN-188, AND DISULFIDE BONDS.
PubMed=22451932; DOI=10.1073/pnas.1112391109;
Kwon Y.D., Finzi A., Wu X., Dogo-Isonagie C., Lee L.K., Moore L.R.,
Schmidt S.D., Stuckey J., Yang Y., Zhou T., Zhu J., Vicic D.A.,
Debnath A.K., Shapiro L., Bewley C.A., Mascola J.R., Sodroski J.G.,
Kwong P.D.;
"Unliganded HIV-1 gp120 core structures assume the CD4-bound
conformation with regulation by quaternary interactions and variable
loops.";
Proc. Natl. Acad. Sci. U.S.A. 109:5663-5668(2012).
[6] {ECO:0000213|PDB:4I54}
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 43-486, GLYCOSYLATION AT
ASN-160 AND ASN-188, AND DISULFIDE BONDS.
PubMed=23667716; DOI=10.1021/ml300407y;
Lalonde J.M., Le-Khac M., Jones D.M., Courter J.R., Park J., Schon A.,
Princiotto A.M., Wu X., Mascola J.R., Freire E., Sodroski J.,
Madani N., Hendrickson W.A., Smith A.B.;
"Structure-Based Design and Synthesis of an HIV-1 Entry Inhibitor
Exploiting X-Ray and Thermodynamic Characterization.";
ACS Med. Chem. Lett. 4:338-343(2013).
[7] {ECO:0000213|PDB:4JPV, ECO:0000213|PDB:4JPW}
X-RAY CRYSTALLOGRAPHY (2.83 ANGSTROMS) OF 43-486, GLYCOSYLATION AT
ASN-160 AND ASN-188, AND DISULFIDE BONDS.
PubMed=23540694; DOI=10.1016/j.cell.2013.03.018;
Klein F., Diskin R., Scheid J.F., Gaebler C., Mouquet H.,
Georgiev I.S., Pancera M., Zhou T., Incesu R.B., Fu B.Z.,
Gnanapragasam P.N., Oliveira T.Y., Seaman M.S., Kwong P.D.,
Bjorkman P.J., Nussenzweig M.C.;
"Somatic mutations of the immunoglobulin framework are generally
required for broad and potent HIV-1 neutralization.";
Cell 153:126-138(2013).
[8] {ECO:0000213|PDB:4LSP, ECO:0000213|PDB:4LSQ, ECO:0000213|PDB:4LSR}
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 43-486, GLYCOSYLATION AT
ASN-87; ASN-160 AND ASN-188, AND DISULFIDE BONDS.
PubMed=23911655; DOI=10.1016/j.immuni.2013.04.012;
NISC Comparative Sequencing Program;
Zhou T., Zhu J., Wu X., Moquin S., Zhang B., Acharya P.,
Georgiev I.S., Altae-Tran H.R., Chuang G.Y., Joyce M.G., Kwon Y.D.,
Longo N.S., Louder M.K., Luongo T., McKee K., Schramm C.A.,
Skinner J., Yang Y., Yang Z., Zhang Z., Zheng A., Bonsignori M.,
Haynes B.F., Scheid J.F., Nussenzweig M.C., Simek M., Burton D.R.,
Koff W.C., Mullikin J.C., Connors M., Shapiro L., Nabel G.J.,
Mascola J.R., Kwong P.D.;
"Multidonor analysis reveals structural elements, genetic
determinants, and maturation pathway for HIV-1 neutralization by
VRC01-class antibodies.";
Immunity 39:245-258(2013).
[9] {ECO:0000213|PDB:4JKP}
X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF 43-486, GLYCOSYLATION AT
ASN-160 AND ASN-188, AND DISULFIDE BONDS.
PubMed=23712429; DOI=10.1084/jem.20130221;
Diskin R., Klein F., Horwitz J.A., Halper-Stromberg A., Sather D.N.,
Marcovecchio P.M., Lee T., West A.P., Gao H., Seaman M.S.,
Stamatatos L., Nussenzweig M.C., Bjorkman P.J.;
"Restricting HIV-1 pathways for escape using rationally designed anti-
HIV-1 antibodies.";
J. Exp. Med. 210:1235-1249(2013).
[10] {ECO:0000213|PDB:4JDT}
X-RAY CRYSTALLOGRAPHY (3.26 ANGSTROMS) OF 43-486, GLYCOSYLATION AT
ASN-188, AND DISULFIDE BONDS.
PubMed=23524883; DOI=10.1073/pnas.1303682110;
Scharf L., West A.P., Gao H., Lee T., Scheid J.F., Nussenzweig M.C.,
Bjorkman P.J., Diskin R.;
"Structural basis for HIV-1 gp120 recognition by a germ-line version
of a broadly neutralizing antibody.";
Proc. Natl. Acad. Sci. U.S.A. 110:6049-6054(2013).
[11] {ECO:0000213|PDB:4JB9}
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 43-486, GLYCOSYLATION AT
ASN-160 AND ASN-188, AND DISULFIDE BONDS.
PubMed=23661761; DOI=10.1126/science.1233989;
Georgiev I.S., Doria-Rose N.A., Zhou T., Kwon Y.D., Staupe R.P.,
Moquin S., Chuang G.Y., Louder M.K., Schmidt S.D., Altae-Tran H.R.,
Bailer R.T., McKee K., Nason M., O'Dell S., Ofek G., Pancera M.,
Srivatsan S., Shapiro L., Connors M., Migueles S.A., Morris L.,
Nishimura Y., Martin M.A., Mascola J.R., Kwong P.D.;
"Delineating antibody recognition in polyclonal sera from patterns of
HIV-1 isolate neutralization.";
Science 340:751-756(2013).
[12] {ECO:0000213|PDB:4P9H}
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 43-122; 201-303 AND 325-486
IN COMPLEX WITH MANNOSE, GLYCOSYLATION AT ASN-236; ASN-243; ASN-264;
ASN-278; ASN-297; ASN-356 AND ASN-386, AND DISULFIDE BONDS.
PubMed=24767986; DOI=10.1016/j.celrep.2014.04.001;
Scharf L., Scheid J.F., Lee J.H., West A.P., Chen C., Gao H.,
Gnanapragasam P.N., Mares R., Seaman M.S., Ward A.B.,
Nussenzweig M.C., Bjorkman P.J.;
"Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1
envelope spike.";
Cell Rep. 7:785-795(2014).
[13] {ECO:0000213|PDB:4OLU, ECO:0000213|PDB:4OLV, ECO:0000213|PDB:4OLW}
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 43-122; 201-303 AND 325-486,
GLYCOSYLATION AT ASN-236; ASN-243; ASN-264; ASN-278; ASN-291; ASN-297;
ASN-335; ASN-386; ASN-392 AND ASN-442, AND DISULFIDE BONDS.
PubMed=25142607; DOI=10.1128/JVI.02213-14;
Rudicell R.S., Kwon Y.D., Ko S.Y., Pegu A., Louder M.K.,
Georgiev I.S., Wu X., Zhu J., Boyington J.C., Chen X., Shi W.,
Yang Z.Y., Doria-Rose N.A., McKee K., O'Dell S., Schmidt S.D.,
Chuang G.Y., Druz A., Soto C., Yang Y., Zhang B., Zhou T., Todd J.P.,
Lloyd K.E., Eudailey J., Roberts K.E., Donald B.R., Bailer R.T.,
Ledgerwood J., Mullikin J.C., Shapiro L., Koup R.A., Graham B.S.,
Nason M.C., Connors M., Haynes B.F., Rao S.S., Roederer M.,
Kwong P.D., Mascola J.R., Nabel G.J.;
"Enhanced potency of a broadly neutralizing HIV-1 antibody in vitro
improves protection against lentiviral infection in vivo.";
J. Virol. 88:12669-12682(2014).
[14] {ECO:0000213|PDB:4H8W}
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 43-486, GLYCOSYLATION AT
ASN-188, AND DISULFIDE BONDS.
PubMed=25165110; DOI=10.1128/JVI.02194-14;
Acharya P., Tolbert W.D., Gohain N., Wu X., Yu L., Liu T., Huang W.,
Huang C.C., Kwon Y.D., Louder R.K., Luongo T.S., McLellan J.S.,
Pancera M., Yang Y., Zhang B., Flinko R., Foulke J.S., Sajadi M.M.,
Kamin-Lewis R., Robinson J.E., Martin L., Kwong P.D., Guan Y.,
DeVico A.L., Lewis G.K., Pazgier M.;
"Structural definition of an antibody-dependent cellular cytotoxicity
response implicated in reduced risk for HIV-1 infection.";
J. Virol. 88:12895-12906(2014).
[15] {ECO:0000213|PDB:4XNZ, ECO:0000213|PDB:4XVT}
X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 43-486, GLYCOSYLATION AT
ASN-236; ASN-243; ASN-264; ASN-278; ASN-386 AND ASN-392, AND DISULFIDE
BONDS.
PubMed=25865483; DOI=10.1016/j.cell.2015.03.004;
NISC Comparative Sequencing Program;
Wu X., Zhang Z., Schramm C.A., Joyce M.G., Kwon Y.D., Zhou T.,
Sheng Z., Zhang B., O'Dell S., McKee K., Georgiev I.S., Chuang G.Y.,
Longo N.S., Lynch R.M., Saunders K.O., Soto C., Srivatsan S., Yang Y.,
Bailer R.T., Louder M.K., Mullikin J.C., Connors M., Kwong P.D.,
Mascola J.R., Shapiro L., Benjamin B., Blakesley R., Bouffard G.,
Brooks S., Coleman H., Dekhtyar M., Gregory M., Guan X., Gupta J.,
Han J., Hargrove A., Ho S.L., Legaspi R., Maduro Q., Masiello C.,
Maskeri B., McDowell J., Montemayor C., Park M., Riebow N.,
Schandler K., Schmidt B., Sison C., Stantripop M., Thomas J.,
Thomas P., Vemulapalli M., Young A.;
"Maturation and Diversity of the VRC01-Antibody Lineage over 15 Years
of Chronic HIV-1 Infection.";
Cell 161:470-485(2015).
[16] {ECO:0000213|PDB:4YDJ, ECO:0000213|PDB:4YDK, ECO:0000213|PDB:4YDL}
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 43-122; 201-303 AND 325-486,
GLYCOSYLATION AT ASN-236; ASN-243; ASN-264; ASN-278; ASN-291; ASN-297;
ASN-335; ASN-386; ASN-392 AND ASN-442, AND DISULFIDE BONDS.
PubMed=26004070; DOI=10.1016/j.cell.2015.05.007;
NISC Comparative Sequencing Program;
Zhou T., Lynch R.M., Chen L., Acharya P., Wu X., Doria-Rose N.A.,
Joyce M.G., Lingwood D., Soto C., Bailer R.T., Ernandes M.J., Kong R.,
Longo N.S., Louder M.K., McKee K., O'Dell S., Schmidt S.D., Tran L.,
Yang Z., Druz A., Luongo T.S., Moquin S., Srivatsan S., Yang Y.,
Zhang B., Zheng A., Pancera M., Kirys T., Georgiev I.S., Gindin T.,
Peng H.P., Yang A.S., Mullikin J.C., Gray M.D., Stamatatos L.,
Burton D.R., Koff W.C., Cohen M.S., Haynes B.F., Casazza J.P.,
Connors M., Corti D., Lanzavecchia A., Sattentau Q.J., Weiss R.A.,
West A.P.Jr., Bjorkman P.J., Scheid J.F., Nussenzweig M.C.,
Shapiro L., Mascola J.R., Kwong P.D.;
"Structural Repertoire of HIV-1-Neutralizing Antibodies Targeting the
CD4 Supersite in 14 Donors.";
Cell 161:1280-1292(2015).
[17] {ECO:0000213|PDB:4RFN, ECO:0000213|PDB:4RFO}
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 43-486, AND DISULFIDE BONDS.
PubMed=26085162; DOI=10.1128/JVI.01232-15;
Gohain N., Tolbert W.D., Acharya P., Yu L., Liu T., Zhao P.,
Orlandi C., Visciano M.L., Kamin-Lewis R., Sajadi M.M., Martin L.,
Robinson J.E., Kwong P.D., DeVico A.L., Ray K., Lewis G.K.,
Pazgier M.;
"Cocrystal Structures of Antibody N60-i3 and Antibody JR4 in Complex
with gp120 Define More Cluster A Epitopes Involved in Effective
Antibody-Dependent Effector Function against HIV-1.";
J. Virol. 89:8840-8854(2015).
-!- 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; AB253424; BAF31367.1; -; Genomic_DNA.
EMBL; AB253425; BAF31376.1; -; Genomic_DNA.
PDB; 3NGB; X-ray; 2.68 A; A/D/G/I=43-122, A/D/G/I=201-303, A/D/G/I=325-486.
PDB; 3SE8; X-ray; 1.90 A; G=43-486.
PDB; 3SE9; X-ray; 2.00 A; G=43-486.
PDB; 3TGT; X-ray; 1.90 A; A=43-486.
PDB; 4DKO; X-ray; 1.98 A; A/C=43-486.
PDB; 4DKP; X-ray; 1.80 A; A/C=43-486.
PDB; 4DKQ; X-ray; 1.89 A; A=43-486.
PDB; 4DKR; X-ray; 1.80 A; A/C=43-486.
PDB; 4H8W; X-ray; 1.85 A; G=43-486.
PDB; 4I54; X-ray; 2.50 A; A/B=43-486.
PDB; 4JB9; X-ray; 2.60 A; G=43-486.
PDB; 4JDT; X-ray; 3.26 A; G=43-486.
PDB; 4JKP; X-ray; 2.82 A; G=43-486.
PDB; 4JPV; X-ray; 2.83 A; G=43-486.
PDB; 4JPW; X-ray; 2.90 A; G=43-486.
PDB; 4LSP; X-ray; 2.15 A; G=43-486.
PDB; 4LSQ; X-ray; 2.25 A; G=43-486.
PDB; 4LSR; X-ray; 2.28 A; G=43-486.
PDB; 4LSU; X-ray; 2.30 A; G=43-486.
PDB; 4OLU; X-ray; 2.20 A; G=43-122, G=201-303, G=325-486.
PDB; 4OLV; X-ray; 2.50 A; G=43-122, G=201-303, G=325-486.
PDB; 4OLW; X-ray; 2.71 A; G=43-122, G=201-303, G=325-486.
PDB; 4OLX; X-ray; 2.20 A; G=43-122, G=201-303, G=325-486.
PDB; 4OLY; X-ray; 2.35 A; G=43-122, G=201-303, G=325-486.
PDB; 4OLZ; X-ray; 2.10 A; G=43-122, G=201-303, G=325-486.
PDB; 4OM0; X-ray; 2.29 A; G=43-122, G=201-303, G=325-486.
PDB; 4OM1; X-ray; 2.13 A; G=43-122, G=201-303, G=325-486.
PDB; 4P9H; X-ray; 3.00 A; G=43-122.
PDB; 4RFN; X-ray; 3.21 A; A/G=43-486.
PDB; 4RFO; X-ray; 3.20 A; G=43-486.
PDB; 4XNZ; X-ray; 3.39 A; A/D/G=43-122, A/D/G=201-303, A/D/G=325-486.
PDB; 4XVT; X-ray; 1.69 A; G=43-486.
PDB; 4YDJ; X-ray; 2.31 A; G/I=43-122, G/I=201-303, G/I=325-486.
PDB; 4YDK; X-ray; 2.05 A; G=43-122, G=201-303, G=325-486.
PDB; 4YDL; X-ray; 1.80 A; A/G=43-122, A/G=201-303, A/G=325-486.
PDB; 4YFL; X-ray; 3.39 A; E/G=43-122, E/G=201-303, E/G=325-486.
PDBsum; 3NGB; -.
PDBsum; 3SE8; -.
PDBsum; 3SE9; -.
PDBsum; 3TGT; -.
PDBsum; 4DKO; -.
PDBsum; 4DKP; -.
PDBsum; 4DKQ; -.
PDBsum; 4DKR; -.
PDBsum; 4H8W; -.
PDBsum; 4I54; -.
PDBsum; 4JB9; -.
PDBsum; 4JDT; -.
PDBsum; 4JKP; -.
PDBsum; 4JPV; -.
PDBsum; 4JPW; -.
PDBsum; 4LSP; -.
PDBsum; 4LSQ; -.
PDBsum; 4LSR; -.
PDBsum; 4LSU; -.
PDBsum; 4OLU; -.
PDBsum; 4OLV; -.
PDBsum; 4OLW; -.
PDBsum; 4OLX; -.
PDBsum; 4OLY; -.
PDBsum; 4OLZ; -.
PDBsum; 4OM0; -.
PDBsum; 4OM1; -.
PDBsum; 4P9H; -.
PDBsum; 4RFN; -.
PDBsum; 4RFO; -.
PDBsum; 4XNZ; -.
PDBsum; 4XVT; -.
PDBsum; 4YDJ; -.
PDBsum; 4YDK; -.
PDBsum; 4YDL; -.
PDBsum; 4YFL; -.
Proteomes; UP000180781; Genome.
Proteomes; UP000181403; Genome.
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.
1: Evidence at protein level;
3D-structure {ECO:0000213|PDB:3NGB, ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9, ECO:0000213|PDB:3TGT};
Apoptosis {ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS01060203};
Cleavage on pair of basic residues {ECO:0000256|RuleBase:RU363095};
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000180781,
ECO:0000313|Proteomes:UP000181403};
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};
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};
Virus entry into host cell {ECO:0000256|RuleBase:RU363095,
ECO:0000256|SAAS:SAAS00797747, ECO:0000256|SAAS:SAAS01050351}.
TRANSMEM 20 41 Helical. {ECO:0000256|RuleBase:RU363095}.
TRANSMEM 506 529 Helical. {ECO:0000256|RuleBase:RU363095}.
TRANSMEM 672 699 Helical. {ECO:0000256|RuleBase:RU363095}.
DOMAIN 33 140 GP120. {ECO:0000259|Pfam:PF00516}.
DOMAIN 141 505 GP120. {ECO:0000259|Pfam:PF00516}.
DOMAIN 524 715 GP41. {ECO:0000259|Pfam:PF00517}.
REGION 209 211 Mannose binding. {ECO:0000213|PDB:4JKP}.
COILED 85 105 {ECO:0000256|SAM:Coils}.
BINDING 61 61 Mannose. {ECO:0000213|PDB:4P9H}.
CARBOHYD 87 87 N-linked (GlcNAc...) asparagine.
{ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:4LSP}.
CARBOHYD 236 236 N-linked (GlcNAc...) asparagine.
{ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
CARBOHYD 243 243 N-linked (GlcNAc...) asparagine.
{ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
CARBOHYD 264 264 C-linked (GlcNAc) asparagine.
{ECO:0000213|PDB:4RFO}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
CARBOHYD 278 278 N-linked (GlcNAc...) asparagine.
{ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
CARBOHYD 291 291 N-linked (GlcNAc...) asparagine.
{ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
CARBOHYD 297 297 N-linked (GlcNAc...) asparagine.
{ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
CARBOHYD 335 335 N-linked (GlcNAc...) asparagine.
{ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
CARBOHYD 356 356 N-linked (GlcNAc...) asparagine.
{ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:4DKO,
ECO:0000213|PDB:4DKP}.
CARBOHYD 386 386 N-linked (GlcNAc...) asparagine.
{ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
CARBOHYD 392 392 N-linked (GlcNAc...) asparagine.
{ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
CARBOHYD 405 405 N-linked (GlcNAc...) asparagine.
{ECO:0000213|PDB:4LSP,
ECO:0000213|PDB:4YFL}.
CARBOHYD 442 442 N-linked (GlcNAc...) asparagine.
{ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
CARBOHYD 455 455 N-linked (GlcNAc...) asparagine.
{ECO:0000213|PDB:4XVT}.
DISULFID 53 73 {ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
DISULFID 118 207 {ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
DISULFID 220 249 {ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
DISULFID 230 241 {ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
DISULFID 298 332 {ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
DISULFID 332 412 {ECO:0000213|PDB:4LSR}.
DISULFID 332 385 {ECO:0000213|PDB:4LSR}.
DISULFID 378 439 {ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
DISULFID 385 412 {ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
DISULFID 395 404 {ECO:0000213|PDB:3NGB,
ECO:0000213|PDB:3SE8,
ECO:0000213|PDB:3SE9}.
SEQUENCE 857 AA; 97310 MW; AA83C4FF189CCD0E CRC64;
MRVKETQMNW PNLWKWGTLI LGLVIICSAS DNLWVTVYYG VPVWKDADTT LFCASDAKAH
ETEVHNVWAT HACVPTDPNP QEIHLENVTE NFNMWKNNMV EQMQEDVISL WDQSLQPCVK
LTPLCVTLHC TTAKLTNVTN ITNVPNIGNI TDEVRNCSFN MTTEIRDKKQ KVHALFYKLD
IVQIEDKNDS SKYRLINCNT SVIKQACPKI SFDPIPIHYC TPAGYVILKC NDKNFNGTGP
CKNVSSVQCT HGIKPVVSTQ LLLNGSLAEE EIIIRSENLT NNAKTIIVHL NKSVEINCTR
PSNNMRTSMR IGPGQVFYRT GSITGDIRKA YCEINGTKWN KVLKQVTEKL KEHFNNKTII
FQPPSGGDLE ITMHHFNCRG EFFYCNTTQL FNNTCIGNET MKGCNGTITL PCKIKQIINM
WQGTGQAMYA PPIDGKINCV SNITGILLTR DGGANNTSNE TFRPGGGNIK DNWRSELYKY
KVVQIEPLGI APTRAKRRVV EREKRAVGIG AMIFGFLGAA GSTMGAASIT LTVQARQLLS
GIVQQQSNLL RAIEAQQHLL QLTVWGIKQL QARVLAVERY LKDQKFLGLW GCSGKIICTT
AVPWNSTWSN KSFEEIWNNM TWIEWEREIS NYTNQIYEIL TESQNQQDRN EKDLLELDKW
ASLWNWFDIT NWLWYIKIFI MIVGGLIGLR IIFAVLSIVN RVRQGYSPLS FQTPIHHQRE
PDRPERIEEG GGEQGRDRSV RLVSGFLSLA WDDLRSLCLF SYHRLRDFIL IATRTVELLG
HSSLKGLRRG WEGLKYLGNL LLYWGQELKI SAISLLNTTA IAVAGWTDRV IEVAQGAWRA
ILHIPRRIRQ GLERTLL


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