ID ENV_HV1H2 Reviewed; 856 AA. AC P04578; O09779; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 02-SEP-2026, entry version 215. DE RecName: Full=Envelope glycoprotein gp160 {ECO:0000255|HAMAP-Rule:MF_04083}; DE AltName: Full=Env polyprotein {ECO:0000255|HAMAP-Rule:MF_04083}; DE Contains: DE RecName: Full=Surface protein gp120 {ECO:0000255|HAMAP-Rule:MF_04083}; DE Short=SU {ECO:0000255|HAMAP-Rule:MF_04083}; DE AltName: Full=Glycoprotein 120 {ECO:0000255|HAMAP-Rule:MF_04083}; DE Short=gp120 {ECO:0000255|HAMAP-Rule:MF_04083}; DE Contains: DE RecName: Full=Transmembrane protein gp41 {ECO:0000255|HAMAP-Rule:MF_04083}; DE Short=TM {ECO:0000255|HAMAP-Rule:MF_04083}; DE AltName: Full=Glycoprotein 41 {ECO:0000255|HAMAP-Rule:MF_04083}; DE Short=gp41 {ECO:0000255|HAMAP-Rule:MF_04083}; DE Flags: Precursor; GN Name=env {ECO:0000255|HAMAP-Rule:MF_04083}; OS Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) OS (HIV-1). OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus; OC Lentivirus humimdef1; Human immunodeficiency virus type 1. OX NCBI_TaxID=11706; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=3040055; DOI=10.1089/aid.1987.3.57; RA Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S., Gallo R.C., RA Wong-Staal F.; RT "Complete nucleotide sequences of functional clones of the AIDS virus."; RL AIDS Res. Hum. Retroviruses 3:57-69(1987). RN [2] RP SEQUENCE REVISION. RA Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S., Gallo R.C., RA Wong-Staal F.; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP FUNCTION (ENVELOPE GLYCOPROTEIN GP160). RX PubMed=2450679; DOI=10.1016/0092-8674(88)90487-4; RA McCune J.M., Rabin L.B., Feinberg M.B., Lieberman M., Kosek J.C., RA Reyes G.R., Weissman I.L.; RT "Endoproteolytic cleavage of gp160 is required for the activation of human RT immunodeficiency virus."; RL Cell 53:55-67(1988). RN [4] RP FUNCTION (TRANSMEMBRANE PROTEIN GP41). RX PubMed=2243396; DOI=10.1128/jvi.64.12.6314-6318.1990; RA Helseth E., Olshevsky U., Gabuzda D., Ardman B., Haseltine W., Sodroski J.; RT "Changes in the transmembrane region of the human immunodeficiency virus RT type 1 gp41 envelope glycoprotein affect membrane fusion."; RL J. Virol. 64:6314-6318(1990). RN [5] RP FUNCTION (ENVELOPE GLYCOPROTEIN GP160). RX PubMed=1360148; DOI=10.1038/360358a0; RA Hallenberger S., Bosch V., Angliker H., Shaw E., Klenk H.D., Garten W.; RT "Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein RT gp160."; RL Nature 360:358-361(1992). RN [6] RP IMMUNOSUPPRESSIVE REGION. RX PubMed=7986401; DOI=10.1097/00002030-199408000-00005; RA Denner J., Norley S., Kurth R.; RT "The immunosuppressive peptide of HIV-1: functional domains and immune RT response in AIDS patients."; RL AIDS 8:1063-1072(1994). RN [7] RP PALMITOYLATION AT CYS-764 AND CYS-837, AND MUTAGENESIS OF CYS-764 AND RP CYS-837. RX PubMed=7568235; DOI=10.1073/pnas.92.21.9871; RA Yang C., Spies C.P., Compans R.W.; RT "The human and simian immunodeficiency virus envelope glycoprotein RT transmembrane subunits are palmitoylated."; RL Proc. Natl. Acad. Sci. U.S.A. 92:9871-9875(1995). RN [8] RP INTERACTION OF SURFACE PROTEIN GP120 WITH GALACTOSYL CERAMIDE AND RP SULFO-GALACTOSYL CERAMIDE. RX PubMed=7494242; DOI=10.1128/jvi.69.12.7383-7390.1995; RA Harouse J.M., Collman R.G., Gonzalez-Scarano F.; RT "Human immunodeficiency virus type 1 infection of SK-N-MC cells: domains of RT gp120 involved in entry into a CD4-negative, galactosyl ceramide/3' sulfo- RT galactosyl ceramide-positive cell line."; RL J. Virol. 69:7383-7390(1995). RN [9] RP DOMAIN YXXL MOTIF. RX PubMed=10233963; DOI=10.1128/jvi.73.6.5010-5017.1999; RA Deschambeault J., Lalonde J.P., Cervantes-Acosta G., Lodge R., Cohen E.A., RA Lemay G.; RT "Polarized human immunodeficiency virus budding in lymphocytes involves a RT tyrosine-based signal and favors cell-to-cell viral transmission."; RL J. Virol. 73:5010-5017(1999). RN [10] RP FUNCTION (SURFACE PROTEIN GP120). RX PubMed=11257134; DOI=10.1084/jem.193.6.671; RA Bashirova A.A., Geijtenbeek T.B.H., van Duijnhoven G.C.F., van Vliet S.J., RA Eilering J.B.G., Martin M.P., Wu L., Martin T.D., Viebig N., Knolle P.A., RA Kewalramani V.N., van Kooyk Y., Carrington M.; RT "A dendritic cell-specific intercellular adhesion molecule 3-grabbing RT nonintegrin (DC-SIGN)-related protein is highly expressed on human liver RT sinusoidal endothelial cells and promotes HIV-1 infection."; RL J. Exp. Med. 193:671-678(2001). RN [11] RP REVIEW. RX PubMed=12974773; DOI=10.1034/j.1600-0463.2003.11107803.x; RA Geijtenbeek T.B., van Kooyk Y.; RT "Pathogens target DC-SIGN to influence their fate DC-SIGN functions as a RT pathogen receptor with broad specificity."; RL APMIS 111:698-714(2003). RN [12] RP DISULFIDE BOND. RX PubMed=12218052; DOI=10.1074/jbc.m205467200; RA Barbouche R., Miquelis R., Jones I.M., Fenouillet E.; RT "Protein-disulfide isomerase-mediated reduction of two disulfide bonds of RT HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for RT fusion."; RL J. Biol. Chem. 278:3131-3136(2003). RN [13] RP INTERACTION OF SURFACE PROTEIN GP120 WITH HOST CD209/DC-SIGN AND RP CLEC4M/DC-SIGNR. RX PubMed=12502850; DOI=10.1128/jvi.77.2.1337-1346.2003; RA Lin G., Simmons G., Poehlmann S., Baribaud F., Ni H., Leslie G.J., RA Haggarty B.S., Bates P., Weissman D., Hoxie J.A., Doms R.W.; RT "Differential N-linked glycosylation of human immunodeficiency virus and RT Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and RT DC-SIGNR."; RL J. Virol. 77:1337-1346(2003). RN [14] RP STOICHIOMETRY (ENVELOPE GLYCOPROTEIN GP160). RX PubMed=16160141; DOI=10.1128/jvi.79.19.12132-12147.2005; RA Yang X., Kurteva S., Ren X., Lee S., Sodroski J.; RT "Stoichiometry of envelope glycoprotein trimers in the entry of human RT immunodeficiency virus type 1."; RL J. Virol. 79:12132-12147(2005). RN [15] RP REVIEW. RX PubMed=12873764; DOI=10.1016/s0005-2736(03)00161-5; RA Gallo S.A., Finnegan C.M., Viard M., Raviv Y., Dimitrov A., Rawat S.S., RA Puri A., Durell S., Blumenthal R.; RT "The HIV Env-mediated fusion reaction."; RL Biochim. Biophys. Acta 1614:36-50(2003). RN [16] RP REVIEW. RX PubMed=15719026; DOI=10.1038/sj.cdd.4401584; RA Perfettini J.-L., Castedo M., Roumier T., Andreau K., Nardacci R., RA Piacentini M., Kroemer G.; RT "Mechanisms of apoptosis induction by the HIV-1 envelope."; RL Cell Death Differ. 12:916-923(2005). RN [17] RP REVIEW. RX PubMed=15725757; DOI=10.1089/aid.2005.21.171; RA Hartley O., Klasse P.J., Sattentau Q.J., Moore J.P.; RT "V3: HIV's switch-hitter."; RL AIDS Res. Hum. Retroviruses 21:171-189(2005). RN [18] RP REVIEW. RX PubMed=16114975; DOI=10.2165/00003495-200565130-00002; RA Reeves J.D., Piefer A.J.; RT "Emerging drug targets for antiretroviral therapy."; RL Drugs 65:1747-1766(2005). RN [19] RP REVIEW. RX PubMed=16437164; DOI=10.1038/sj.emboj.7600947; RA Lusso P.; RT "HIV and the chemokine system: 10 years later."; RL EMBO J. 25:447-456(2006). RN [20] RP DI-LEUCINE INTERNALIZATION MOTIF. RX PubMed=17108326; DOI=10.1091/mbc.e06-06-0535; RA Byland R., Vance P.J., Hoxie J.A., Marsh M.; RT "A conserved dileucine motif mediates clathrin and AP-2-dependent RT endocytosis of the HIV-1 envelope protein."; RL Mol. Biol. Cell 18:414-425(2007). RN [21] RP MEMBRANE-PROXIMAL EXTERNAL REGION. RX PubMed=18322034; DOI=10.1128/mmbr.00020-07; RA Montero M., van Houten N.E., Wang X., Scott J.K.; RT "The membrane-proximal external region of the human immunodeficiency virus RT type 1 envelope: dominant site of antibody neutralization and target for RT vaccine design."; RL Microbiol. Mol. Biol. Rev. 72:54-84(2008). RN [22] RP INTERACTION OF SURFACE PROTEIN GP120 WITH HEPARAN SULFATE. RC STRAIN=HXBC2; RX PubMed=18378683; DOI=10.1074/jbc.m800066200; RA Crublet E., Andrieu J.P., Vives R.R., Lortat-Jacob H.; RT "The HIV-1 envelope glycoprotein gp120 features four heparan sulfate RT binding domains, including the co-receptor binding site."; RL J. Biol. Chem. 283:15193-15200(2008). RN [23] RP FUNCTION. RX PubMed=19410541; DOI=10.1016/j.cell.2009.02.046; RA Miyauchi K., Kim Y., Latinovic O., Morozov V., Melikyan G.B.; RT "HIV enters cells via endocytosis and dynamin-dependent fusion with RT endosomes."; RL Cell 137:433-444(2009). RN [24] RP IMMUNOSUPPRESSIVE REGION. RX PubMed=23383108; DOI=10.1371/journal.pone.0055199; RA Denner J., Eschricht M., Lauck M., Semaan M., Schlaermann P., Ryu H., RA Akyuez L.; RT "Modulation of cytokine release and gene expression by the RT immunosuppressive domain of gp41 of HIV-1."; RL PLoS ONE 8:E55199-E55199(2013). RN [25] RP GLYCOSYLATION AT ASN-88; ASN-156; ASN-160; ASN-197; ASN-234; ASN-262; RP ASN-276; ASN-295; ASN-332; ASN-339; ASN-386; ASN-392; ASN-448; ASN-611 AND RP ASN-637. RC STRAIN=BG505; RX PubMed=26972002; DOI=10.1016/j.celrep.2016.02.058; RA Behrens A.J., Vasiljevic S., Pritchard L.K., Harvey D.J., Andev R.S., RA Krumm S.A., Struwe W.B., Cupo A., Kumar A., Zitzmann N., Seabright G.E., RA Kramer H.B., Spencer D.I., Royle L., Lee J.H., Klasse P.J., Burton D.R., RA Wilson I.A., Ward A.B., Sanders R.W., Moore J.P., Doores K.J., Crispin M.; RT "Composition and antigenic effects of individual glycan sites of a trimeric RT HIV-1 envelope glycoprotein."; RL Cell Rep. 14:2695-2706(2016). RN [26] RP GLYCOSYLATION. RX PubMed=28667249; DOI=10.1038/s41598-017-04532-9; RA Yang M., Huang J., Simon R., Wang L.X., MacKerell A.D. Jr.; RT "Conformational heterogeneity of the HIV envelope glycan shield."; RL Sci. Rep. 7:4435-4435(2017). RN [27] RP FUNCTION (ENVELOPE GLYCOPROTEIN GP160). RX PubMed=31091448; DOI=10.1016/j.celrep.2019.04.063; RA Braun E., Hotter D., Koepke L., Zech F., Gross R., Sparrer K.M.J., RA Mueller J.A., Pfaller C.K., Heusinger E., Wombacher R., Sutter K., RA Dittmer U., Winkler M., Simmons G., Jakobsen M.R., Conzelmann K.K., RA Poehlmann S., Muench J., Fackler O.T., Kirchhoff F., Sauter D.; RT "Guanylate-binding proteins 2 and 5 exert broad antiviral activity by RT inhibiting furin-mediated processing of viral envelope proteins."; RL Cell Rep. 27:2092-2104(2019). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 628-661 AND 546-581. RX PubMed=9108481; DOI=10.1016/s0092-8674(00)80205-6; RA Chan D.C., Fass D., Berger J.M., Kim P.S.; RT "Core structure of gp41 from the HIV envelope glycoprotein."; RL Cell 89:263-273(1997). RN [29] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 83-127; 195-297; 330-396 AND RP 410-492, AND GLYCOSYLATION AT ASN-197; ASN-262; ASN-276; ASN-289; ASN-295; RP ASN-332; ASN-339; ASN-386; ASN-392 AND ASN-448. RX PubMed=9641677; DOI=10.1038/31405; RA Kwong P.D., Wyatt R., Robinson J., Sweet R.W., Sodroski J., RA Hendrickson W.A.; RT "Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 RT receptor and a neutralizing human antibody."; RL Nature 393:648-659(1998). RN [30] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 546-579 AND 628-655. RX PubMed=10677212; DOI=10.1021/bi9921687; RA Shu W., Liu J., Ji H., Radigen L., Jiang S., Lu M.; RT "Helical interactions in the HIV-1 gp41 core reveal structural basis for RT the inhibitory activity of gp41 peptides."; RL Biochemistry 39:1634-1642(2000). RN [31] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 546-579 AND 628-655. RX PubMed=10636883; DOI=10.1074/jbc.275.3.1839; RA Shu W., Ji H., Lu M.; RT "Interactions between HIV-1 gp41 core and detergents and their implications RT for membrane fusion."; RL J. Biol. Chem. 275:1839-1845(2000). RN [32] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 83-127; 195-297 AND 330-492, AND RP GLYCOSYLATION AT ASN-197; ASN-234; ASN-262; ASN-276; ASN-289; ASN-295; RP ASN-339; ASN-386; ASN-392; ASN-448 AND ASN-463. RX PubMed=11188697; DOI=10.1016/s0969-2126(00)00547-5; RA Kwong P.D., Wyatt R., Majeed S., Robinson J., Sweet R.W., Sodroski J., RA Hendrickson W.A.; RT "Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted RT and primary isolates."; RL Structure 8:1329-1339(2000). RN [33] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 546-579 AND 628-655. RX PubMed=12044159; DOI=10.1021/bi025648y; RA Wang S., York J., Shu W., Stoller M.O., Nunberg J.H., Lu M.; RT "Interhelical interactions in the gp41 core: implications for activation of RT HIV-1 membrane fusion."; RL Biochemistry 41:7283-7292(2002). RN [34] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 565-581. RX PubMed=12417739; DOI=10.1073/pnas.232566599; RA Sia S.K., Carr P.A., Cochran A.G., Malashkevich V.N., Kim P.S.; RT "Short constrained peptides that inhibit HIV-1 entry."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14664-14669(2002). RN [35] RP STRUCTURE BY NMR OF 659-671. RX PubMed=12860131; DOI=10.1016/s0022-2836(03)00611-9; RA Barbato G., Bianchi E., Ingallinella P., Hurni W.H., Miller M.D., RA Ciliberto G., Cortese R., Bazzo R., Shiver J.W., Pessi A.; RT "Structural analysis of the epitope of the anti-HIV antibody 2F5 sheds RT light into its mechanism of neutralization and HIV fusion."; RL J. Mol. Biol. 330:1101-1115(2003). RN [36] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 195-492, AND GLYCOSYLATION AT RP ASN-197; ASN-234; ASN-262; ASN-276; ASN-289; ASN-295; ASN-392; ASN-448 AND RP ASN-463. RX PubMed=14981267; DOI=10.1073/pnas.0308527100; RA Huang C.C., Venturi M., Majeed S., Moore M.J., Phogat S., Zhang M.Y., RA Dimitrov D.S., Hendrickson W.A., Robinson J., Sodroski J., Wyatt R., RA Choe H., Farzan M., Kwong P.D.; RT "Structural basis of tyrosine sulfation and VH-gene usage in antibodies RT that recognize the HIV type 1 coreceptor-binding site on gp120."; RL Proc. Natl. Acad. Sci. U.S.A. 101:2706-2711(2004). RN [37] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 83-492, AND GLYCOSYLATION AT RP ASN-356. RX PubMed=17301785; DOI=10.1038/nature05580; RA Zhou T., Xu L., Dey B., Hessell A.J., Van Ryk D., Xiang S.H., Yang X., RA Zhang M.Y., Zwick M.B., Arthos J., Burton D.R., Dimitrov D.S., Sodroski J., RA Wyatt R., Nabel G.J., Kwong P.D.; RT "Structural definition of a conserved neutralization epitope on HIV-1 RT gp120."; RL Nature 445:732-737(2007). RN [38] RP STRUCTURE BY NMR OF 662-683. RX PubMed=18191596; DOI=10.1016/j.immuni.2007.11.018; RA Sun Z.Y., Oh K.J., Kim M., Yu J., Brusic V., Song L., Qiao Z., Wang J.H., RA Wagner G., Reinherz E.L.; RT "HIV-1 broadly neutralizing antibody extracts its epitope from a kinked RT gp41 ectodomain region on the viral membrane."; RL Immunity 28:52-63(2008). RN [39] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 660-670. RX PubMed=18824005; DOI=10.1016/j.jmb.2008.09.024; RA Julien J.P., Bryson S., Nieva J.L., Pai E.F.; RT "Structural details of HIV-1 recognition by the broadly neutralizing RT monoclonal antibody 2F5: epitope conformation, antigen-recognition loop RT mobility, and anion-binding site."; RL J. Mol. Biol. 384:377-392(2008). RN [40] RP STRUCTURE BY ELECTRON MICROSCOPY (20.00 ANGSTROMS) OF 90-124; 198-297; RP 330-396 AND 410-492. RX PubMed=18668044; DOI=10.1038/nature07159; RA Liu J., Bartesaghi A., Borgnia M.J., Sapiro G., Subramaniam S.; RT "Molecular architecture of native HIV-1 gp120 trimers."; RL Nature 455:109-113(2008). RN [41] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 83-492, AND GLYCOSYLATION AT RP ASN-88 AND ASN-356. RX PubMed=19965434; DOI=10.1126/science.1175868; RA Chen L., Kwon Y.D., Zhou T., Wu X., O'Dell S., Cavacini L., Hessell A.J., RA Pancera M., Tang M., Xu L., Yang Z.Y., Zhang M.Y., Arthos J., Burton D.R., RA Dimitrov D.S., Nabel G.J., Posner M.R., Sodroski J., Wyatt R., RA Mascola J.R., Kwong P.D.; RT "Structural basis of immune evasion at the site of CD4 attachment on HIV-1 RT gp120."; RL Science 326:1123-1127(2009). RN [42] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 543-582; 590-639; 625-662 AND RP 654-688. RX PubMed=21124990; DOI=10.1371/journal.ppat.1001195; RA Sabin C., Corti D., Buzon V., Seaman M.S., Lutje Hulsik D., Hinz A., RA Vanzetta F., Agatic G., Silacci C., Mainetti L., Scarlatti G., Sallusto F., RA Weiss R., Lanzavecchia A., Weissenhorn W.; RT "Crystal structure and size-dependent neutralization properties of HK20, a RT human monoclonal antibody binding to the highly conserved heptad repeat 1 RT of gp41."; RL PLoS Pathog. 6:E1001195-E1001195(2010). RN [43] RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 254-297; 330-401; 412-419 AND RP 445-477, AND GLYCOSYLATION AT ASN-332. RX PubMed=21998254; DOI=10.1126/science.1213256; RA Pejchal R., Doores K.J., Walker L.M., Khayat R., Huang P.S., Wang S.K., RA Stanfield R.L., Julien J.P., Ramos A., Crispin M., Depetris R., RA Katpally U., Marozsan A., Cupo A., Maloveste S., Liu Y., McBride R., RA Ito Y., Sanders R.W., Ogohara C., Paulson J.C., Feizi T., Scanlan C.N., RA Wong C.H., Moore J.P., Olson W.C., Ward A.B., Poignard P., Schief W.R., RA Burton D.R., Wilson I.A.; RT "A potent and broad neutralizing antibody recognizes and penetrates the HIV RT glycan shield."; RL Science 334:1097-1103(2011). RN [44] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 546-581. RX PubMed=22228771; DOI=10.1074/jbc.m111.317883; RA Yao X., Chong H., Zhang C., Waltersperger S., Wang M., Cui S., He Y.; RT "Broad antiviral activity and crystal structure of HIV-1 fusion inhibitor RT sifuvirtide."; RL J. Biol. Chem. 287:6788-6796(2012). RN [45] RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 254-399, AND GLYCOSYLATION AT RP ASN-262. RX PubMed=23539181; DOI=10.1126/science.1234150; RA Jardine J., Julien J.P., Menis S., Ota T., Kalyuzhniy O., McGuire A., RA Sok D., Huang P.S., MacPherson S., Jones M., Nieusma T., Mathison J., RA Baker D., Ward A.B., Burton D.R., Stamatatos L., Nemazee D., Wilson I.A., RA Schief W.R.; RT "Rational HIV immunogen design to target specific germline B cell RT receptors."; RL Science 340:711-716(2013). RN [46] RP STRUCTURE BY NMR OF 657-683. RX PubMed=24075869; DOI=10.1016/j.jmb.2013.09.030; RA Sun Z.Y., Cheng Y., Kim M., Song L., Choi J., Kudahl U.J., Brusic V., RA Chowdhury B., Yu L., Seaman M.S., Bellot G., Shih W.M., Wagner G., RA Reinherz E.L.; RT "Disruption of helix-capping residues 671 and 674 reveals a role in HIV-1 RT entry for a specialized hinge segment of the membrane proximal external RT region of gp41."; RL J. Mol. Biol. 426:1095-1108(2014). CC -!- FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host CC endoplasmic reticulum into predominantly trimers. In a second time, CC gp160 transits in the host Golgi, where glycosylation is completed. The CC precursor is then proteolytically cleaved in the trans-Golgi and CC thereby activated by cellular furin or furin-like proteases to produce CC gp120 and gp41. {ECO:0000255|HAMAP-Rule:MF_04083, CC ECO:0000269|PubMed:1360148, ECO:0000269|PubMed:2450679, CC ECO:0000269|PubMed:31091448}. CC -!- FUNCTION: [Surface protein gp120]: 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 CXCR4 and/or CCR5. Acts as a CC ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively CC found on dendritic cells (DCs), and on endothelial cells of liver CC sinusoids and lymph node sinuses. These interactions allow capture of CC viral particles at mucosal surfaces by these cells and subsequent CC transmission to permissive cells. HIV subverts the migration properties CC of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus CC transmission to permissive T-cells occurs either in trans (without DCs CC infection, through viral capture and transmission), or in cis CC (following DCs productive infection, through the usual CD4-gp120 CC interaction), thereby inducing a robust infection. In trans infection, CC bound virions remain infectious over days and it is proposed that they CC are not degraded, but protected in non-lysosomal acidic organelles CC within the DCs close to the cell membrane thus contributing to the CC viral infectious potential during DCs' migration from the periphery to CC the lymphoid tissues. On arrival at lymphoid tissues, intact virions CC recycle back to DCs' cell surface allowing virus transmission to CD4+ CC T-cells. {ECO:0000255|HAMAP-Rule:MF_04083, ECO:0000269|PubMed:11257134, CC ECO:0000269|PubMed:19410541}. CC -!- FUNCTION: [Transmembrane protein gp41]: Acts as a class I viral fusion CC 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 and is dynamin-dependent, however CC some lipid transfer might occur at the plasma membrane. The virus CC undergoes clathrin-dependent internalization long before endosomal CC fusion, thus minimizing the surface exposure of conserved viral CC epitopes during fusion and reducing the efficacy of inhibitors CC targeting these epitopes. Membranes fusion leads to delivery of the CC nucleocapsid into the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04083, CC ECO:0000269|PubMed:19410541, ECO:0000269|PubMed:2243396}. CC -!- SUBUNIT: [Surface protein gp120]: The mature envelope protein (Env) CC consists of a homotrimer of non-covalently associated gp120-gp41 CC heterodimers. The resulting complex protrudes from the virus surface as CC a spike. There seems to be as few as 10 spikes on the average virion. CC Interacts with host CD4, CCR5 and CXCR4. Gp120 also interacts with the CC C-type lectins CD209/DC-SIGN and CLEC4M/DC-SIGNR (collectively referred CC to as DC-SIGN(R)). Gp120 and gp41 interact with GalCer. Gp120 interacts CC with host ITGA4/ITGB7 complex; on CD4+ T-cells, this interaction CC results in rapid activation of integrin ITGAL/LFA-1, which facilitates CC efficient cell-to-cell spreading of HIV-1. Gp120 interacts with cell- CC associated heparan sulfate; this interaction increases virus CC infectivity on permissive cells and may be involved in infection of CC CD4- cells. {ECO:0000255|HAMAP-Rule:MF_04083, CC ECO:0000269|PubMed:12502850, ECO:0000269|PubMed:18378683, CC ECO:0000269|PubMed:7494242}. CC -!- SUBUNIT: [Transmembrane protein gp41]: The mature envelope protein CC (Env) consists of a homotrimer of non-covalently associated gp120-gp41 CC heterodimers. The resulting complex protrudes from the virus surface as CC a spike. There seems to be as few as 10 spikes on the average virion. CC {ECO:0000255|HAMAP-Rule:MF_04083, ECO:0000269|PubMed:12502850, CC ECO:0000269|PubMed:18378683, ECO:0000269|PubMed:7494242}. CC -!- INTERACTION: CC P04578; P04608: tat; NbExp=4; IntAct=EBI-6163496, EBI-6164389; CC P04578; P27824: CANX; Xeno; NbExp=3; IntAct=EBI-6163496, EBI-355947; CC P04578; P01730: CD4; Xeno; NbExp=2; IntAct=EBI-6163496, EBI-353826; CC P04578; Q9ULD8: KCNH3; Xeno; NbExp=3; IntAct=EBI-6163496, EBI-8079227; CC PRO_0000038427; P01730: CD4; Xeno; NbExp=3; IntAct=EBI-6179761, EBI-353826; CC PRO_0000038428; PRO_0000038428 [P04578]: env; NbExp=2; IntAct=EBI-6179711, EBI-6179711; CC PRO_0000038428; P08962: CD63; Xeno; NbExp=4; IntAct=EBI-6179711, EBI-762053; CC -!- SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane CC {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein CC {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane CC {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein CC {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane CC {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein CC {ECO:0000255|HAMAP-Rule:MF_04083}. Note=The surface protein is not CC anchored to the viral envelope, but associates with the extravirion CC surface through its binding to TM. It is probably concentrated at the CC site of budding and incorporated into the virions possibly by contacts CC between the cytoplasmic tail of Env and the N-terminus of Gag. CC {ECO:0000255|HAMAP-Rule:MF_04083}. CC -!- SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane CC {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein CC {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane CC {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein CC {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane CC {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein CC {ECO:0000255|HAMAP-Rule:MF_04083}. Note=It is probably concentrated at CC the site of budding and incorporated into the virions possibly by CC contacts between the cytoplasmic tail of Env and the N-terminus of Gag. CC {ECO:0000255|HAMAP-Rule:MF_04083}. CC -!- DOMAIN: Some of the most genetically diverse regions of the viral CC genome are present in Env. They are called variable regions 1 through 5 CC (V1 through V5). Coreceptor usage of gp120 is determined mainly by the CC primary structure of the third variable region (V3) in the outer domain CC of gp120. The sequence of V3 determines which coreceptor, CCR5 and/or CC CXCR4 (corresponding to R5/macrophage, X4/T cell and R5X4/T cell and CC macrophage tropism), is used to trigger the fusion potential of the Env CC complex, and hence which cells the virus can infect. Binding to CCR5 CC involves a region adjacent in addition to V3. {ECO:0000255|HAMAP- CC Rule:MF_04083, ECO:0000269|PubMed:10233963}. CC -!- DOMAIN: The membrane proximal external region (MPER) present in gp41 is CC a tryptophan-rich region recognized by the antibodies 2F5, Z13, and CC 4E10. MPER seems to play a role in fusion. {ECO:0000255|HAMAP- CC Rule:MF_04083, ECO:0000269|PubMed:10233963}. 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:0000255|HAMAP-Rule:MF_04083, ECO:0000269|PubMed:23383108}. CC -!- DOMAIN: The YXXL motif is involved in determining the exact site of CC viral release at the surface of infected mononuclear cells and promotes CC endocytosis. YXXL and di-leucine endocytosis motifs interact directly CC or indirectly with the clathrin adapter complexes, opperate CC independently, and their activities are not additive. CC {ECO:0000255|HAMAP-Rule:MF_04083, ECO:0000269|PubMed:10233963}. CC -!- DOMAIN: The CD4-binding region is targeted by the antibody b12. CC {ECO:0000255|HAMAP-Rule:MF_04083, ECO:0000269|PubMed:10233963}. CC -!- PTM: Palmitoylation of the transmembrane protein and of Env polyprotein CC (prior to its proteolytic cleavage) is essential for their association CC with host cell membrane lipid rafts. Palmitoylation is therefore CC required for envelope trafficking to classical lipid rafts, but not for CC viral replication. {ECO:0000255|HAMAP-Rule:MF_04083, CC ECO:0000269|PubMed:7568235}. CC -!- PTM: Highly glycosylated by host. The high number of glycan on the CC protein is reffered to as 'glycan shield' because it contributes to CC hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP- CC Rule:MF_04083, ECO:0000269|PubMed:26972002, CC ECO:0000269|PubMed:28667249}. CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. CC Envelope glycoproteins are synthesized as an inactive precursor that is CC heavily N-glycosylated and processed likely by host cell furin in the CC Golgi to yield the mature SU and TM proteins. The cleavage site between CC SU and TM requires the minimal sequence [KR]-X-[KR]-R. About 2 of the 9 CC disulfide bonds of gp41 are reduced by P4HB/PDI, following binding to CC CD4 receptor. {ECO:0000255|HAMAP-Rule:MF_04083, CC ECO:0000269|PubMed:12218052, ECO:0000269|PubMed:2450679, CC ECO:0000269|PubMed:31091448}. CC -!- MISCELLANEOUS: Inhibitors targeting HIV-1 viral envelope proteins are CC used as antiretroviral drugs. Attachment of virions to the cell surface CC via non-specific interactions and CD4 binding can be blocked by CC inhibitors that include cyanovirin-N, cyclotriazadisulfonamide analogs, CC PRO 2000, TNX 355 and PRO 542. In addition, BMS 806 can block CD4- CC induced conformational changes. Env interactions with the coreceptor CC molecules can be targeted by CCR5 antagonists including SCH-D, CC maraviroc (UK 427857) and aplaviroc (GW 873140), and the CXCR4 CC antagonist AMD 070. Fusion of viral and cellular membranes can be CC inhibited by peptides such as enfuvirtide and tifuvirtide (T 1249). CC Resistance to inhibitors associated with mutations in Env are observed. CC Most of the time, single mutations confer only a modest reduction in CC drug susceptibility. Combination of several mutations is usually CC required to develop a high-level drug resistance. {ECO:0000255|HAMAP- CC Rule:MF_04083}. CC -!- MISCELLANEOUS: HIV-1 lineages are divided in three main groups, M (for CC Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast CC majority of strains found worldwide belong to the group M. Group O CC seems to be endemic to and largely confined to Cameroon and neighboring CC countries in West Central Africa, where these viruses represent a small CC minority of HIV-1 strains. The group N is represented by a limited CC number of isolates from Cameroonian persons. The group M is further CC subdivided in 9 clades or subtypes (A to D, F to H, J and K). CC {ECO:0000255|HAMAP-Rule:MF_04083}. CC -!- SIMILARITY: Belongs to the HIV-1 env protein family. CC {ECO:0000255|HAMAP-Rule:MF_04083}. CC -!- WEB RESOURCE: Name=hivdb; Note=HIV drug resistance database; CC URL="https://hivdb.stanford.edu"; CC -!- WEB RESOURCE: Name=HIV drug resistance mutations; CC URL="https://www.iasusa.org/hiv-drug-resistance/hiv-drug-resistance-mutations/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; K03455; AAB50262.1; -; Genomic_RNA. DR EMBL; AF038399; AAB99976.1; -; Genomic_DNA. DR EMBL; AF033819; AAC82596.1; -; Genomic_RNA. DR RefSeq; NP_057856.1; NC_001802.1. DR PDB; 1AIK; X-ray; 2.00 A; C=627-661, N=546-581. DR PDB; 1DF4; X-ray; 1.45 A; A=546-655. DR PDB; 1DF5; X-ray; 2.70 A; A=546-655. DR PDB; 1DLB; X-ray; 2.00 A; A=546-655. DR PDB; 1FAV; X-ray; 3.00 A; C=636-665. DR PDB; 1G9M; X-ray; 2.20 A; G=83-492. DR PDB; 1GC1; X-ray; 2.50 A; G=83-127, G=195-297, G=330-492. DR PDB; 1GZL; X-ray; 1.80 A; A/B=566-581, C/D=628-639. DR PDB; 1K33; X-ray; 1.75 A; A=546-655. DR PDB; 1K34; X-ray; 1.88 A; A=546-655. DR PDB; 1MZI; NMR; -; A=659-671. DR PDB; 1RZJ; X-ray; 2.20 A; G=195-492. DR PDB; 2CMR; X-ray; 2.00 A; A=543-662. DR PDB; 2ME1; NMR; -; A=657-683. DR PDB; 2MG1; NMR; -; A=683-704. DR PDB; 2MG2; NMR; -; A=671-693. DR PDB; 2MG3; NMR; -; A=671-693. DR PDB; 2NY7; X-ray; 2.30 A; G=83-492. DR PDB; 2PV6; NMR; -; A=662-683. DR PDB; 2XRA; X-ray; 2.30 A; A=543-582, A=625-662. DR PDB; 3D0V; X-ray; 2.05 A; C=660-670. DR PDB; 3DNL; EM; 20.00 A; A/D/G=90-124, B/E/H=198-297, B/E/H=330-396, C/F/I=410-492. DR PDB; 3DNN; EM; 20.00 A; A/D/G=90-124, B/E/H=198-297, B/E/H=330-396, C/F/I=410-492. DR PDB; 3DNO; EM; 20.00 A; A/D/G=90-124, B/E/H=198-297, B/E/H=330-396, C/F/I=410-492. DR PDB; 3DRO; X-ray; 3.90 A; P=659-671. DR PDB; 3IDX; X-ray; 2.50 A; G=83-492. DR PDB; 3IDY; X-ray; 3.20 A; A/G=83-492. DR PDB; 3J70; EM; -; D/P/U=31-500. DR PDB; 3MNZ; X-ray; 1.80 A; P=653-671. DR PDB; 3TYG; X-ray; 3.25 A; A=275-314, A=340-401. DR PDB; 3VIE; X-ray; 1.80 A; A/C/E=546-581. DR PDB; 4JPJ; X-ray; 2.50 A; A/B/C/D=254-399. DR PDB; 4JPK; X-ray; 2.40 A; A=254-399. DR PDB; 4YDV; X-ray; 2.70 A; P/Q=596-606. DR PDB; 4ZTO; X-ray; 2.30 A; P/Q=430-444. DR PDB; 5BN0; X-ray; 2.80 A; A/C/D=627-661, B/E/N=546-581. DR PDB; 5C0R; X-ray; 3.19 A; A=546-577. DR PDB; 5C0S; X-ray; 4.30 A; A=546-577. DR PDB; 5CIL; X-ray; 1.81 A; P=671-683. DR PDB; 5CIN; X-ray; 1.70 A; P=671-683. DR PDB; 5CMU; X-ray; 2.11 A; A/B/C=546-582. DR PDB; 5CMZ; X-ray; 2.57 A; A/C=546-590. DR PDB; 5CN0; X-ray; 1.90 A; A=546-582. DR PDB; 5DD0; X-ray; 2.49 A; P=660-670. DR PDB; 5GHW; X-ray; 2.40 A; P=666-690. DR PDB; 5H0N; X-ray; 2.80 A; A/C/E/G/I/K=536-581. DR PDB; 5HFL; X-ray; 2.29 A; A/B/C/D/E/F=546-653. DR PDB; 5HM1; X-ray; 2.96 A; D/E/F=582-596. DR PDB; 5IVX; X-ray; 2.10 A; P=311-320. DR PDB; 5KA5; X-ray; 1.80 A; A=543-582, A=625-661. DR PDB; 5KA6; X-ray; 1.85 A; A/B/C=543-582, A/B/C=625-661. DR PDB; 5NVP; NMR; -; A=514-528, A=655-671. DR PDB; 5NWU; NMR; -; A=514-528, A=655-671. DR PDB; 5NWW; NMR; -; A=655-671. DR PDB; 5TKJ; X-ray; 2.12 A; C/F/I/L=512-519. DR PDB; 5TKK; X-ray; 1.55 A; A=512-519. DR PDB; 5WDF; X-ray; 3.10 A; P/Q=668-683. DR PDB; 5X08; X-ray; 1.49 A; P=671-683. DR PDB; 5YB2; X-ray; 3.80 A; A/B/C/D/E/F/M=538-581. DR PDB; 5YB3; X-ray; 2.04 A; D/E/F=546-581. DR PDB; 5YB4; X-ray; 2.50 A; D/E/F=546-581. DR PDB; 5YC0; X-ray; 2.00 A; A/B/C/D/E/F=538-581. DR PDB; 5Z0W; X-ray; 1.90 A; E=546-581. DR PDB; 5ZCX; X-ray; 2.30 A; A/B/C=528-566, P/Q/W=638-673. DR PDB; 6B9K; NMR; -; A=311-320. DR PDB; 6BXP; X-ray; 1.45 A; C=2-11. DR PDB; 6BXQ; X-ray; 1.58 A; A=2-11. DR PDB; 6DE7; X-ray; 4.12 A; B=512-664. DR PDB; 6DLN; NMR; -; A/B/C=665-703. DR PDB; 6J5E; X-ray; 2.33 A; G/I/K=538-581. DR PDB; 6JQK; X-ray; 1.50 A; C=623-661, N=546-581. DR PDB; 6KTS; X-ray; 1.65 A; A/C/D=627-661, B/E/N=546-581. DR PDB; 6MQC; X-ray; 1.99 A; C/D=512-519. DR PDB; 6MQE; X-ray; 2.46 A; C/D=512-519. DR PDB; 6MQM; X-ray; 3.48 A; C/F/I/L=512-518. DR PDB; 6MQR; X-ray; 2.45 A; A=512-519. DR PDB; 6MQS; X-ray; 3.00 A; E/F=512-519. DR PDB; 6N16; X-ray; 2.30 A; E/F/G/I=512-519. DR PDB; 6NCP; X-ray; 2.76 A; E=512-520. DR PDB; 6NPR; X-ray; 2.37 A; P/R=311-320. DR PDB; 6O3G; X-ray; 3.65 A; G/I/Q/S=671-683. DR PDB; 6O3J; X-ray; 3.42 A; G/I=671-683. DR PDB; 6O3L; X-ray; 1.98 A; D/E=671-683. DR PDB; 6O42; X-ray; 2.60 A; G/I=671-683. DR PDB; 6P60; X-ray; 2.50 A; E/F/I/L=512-519. DR PDB; 6P7H; X-ray; 1.78 A; C=512-519. DR PDB; 6P8D; X-ray; 2.10 A; C/F=512-519. DR PDB; 6PDR; X-ray; 1.55 A; A=512-519. DR PDB; 6PDS; X-ray; 1.89 A; C/G=512-519. DR PDB; 6PDU; X-ray; 1.95 A; C=512-519. DR PDB; 6PEC; X-ray; 1.75 A; A=512-519. DR PDB; 6PEF; X-ray; 2.00 A; C/F=512-519. DR PDB; 6PSA; X-ray; 1.30 A; A=566-581. DR PDB; 6RYF; X-ray; 1.72 A; G=308-320. DR PDB; 6SNC; X-ray; 3.20 A; C/P=671-689. DR PDB; 6SND; X-ray; 3.10 A; C/P=671-689. DR PDB; 6SNE; X-ray; 3.90 A; J/N/O/P=649-711. DR PDB; 6UBI; X-ray; 1.90 A; C/F=512-519. DR PDB; 6UCE; X-ray; 1.38 A; C=512-519. DR PDB; 6UCF; X-ray; 1.29 A; A=512-519. DR PDB; 6UJU; NMR; -; A/B/C=677-788. DR PDB; 6UJV; NMR; -; A/B/C=660-788. DR PDB; 6WWC; X-ray; 2.56 A; C/F=512-519. DR PDB; 7AEJ; X-ray; 3.80 A; A/B/C=512-594, A/B/C=629-718. DR PDB; 7EKB; X-ray; 1.45 A; P=671-683. DR PDB; 7EKK; X-ray; 1.70 A; P=671-683. DR PDB; 7FF1; X-ray; 1.69 A; A/C/D=627-661, B/E/N=546-581. DR PDB; 7LOH; NMR; -; A/B/C=677-856. DR PDB; 7LOI; NMR; -; A/B/C=660-856. DR PDB; 7N05; X-ray; 1.70 A; E=596-610. DR PDB; 7N08; X-ray; 2.00 A; E/F/G=596-610. DR PDB; 7R73; X-ray; 1.76 A; G=44-64. DR PDB; 7R74; X-ray; 2.76 A; A/C=44-492. DR PDB; 7RDW; X-ray; 3.55 A; C/D/M/N=44-495. DR PDB; 8B6Y; NMR; -; A=671-690. DR PDB; 8F3A; X-ray; 1.20 A; A/B/C=540-581. DR PDB; 8F3B; X-ray; 2.00 A; A/B/C=540-586. DR PDB; 8FYM; X-ray; 2.45 A; C/F/J/P=667-683. DR PDB; 8FZ2; X-ray; 3.50 A; P=657-679. DR PDB; 8G8A; X-ray; 2.44 A; C/P=652-671. DR PDB; 8G8C; X-ray; 2.08 A; C/P=651-671. DR PDB; 8G8D; X-ray; 2.02 A; C/P=653-683. DR PDB; 8IPG; X-ray; 1.64 A; A/B/C=538-581. DR PDB; 8TQ7; X-ray; 2.80 A; E/P=311-320. DR PDB; 8TQ8; X-ray; 2.69 A; E/P=311-320. DR PDB; 8TQ9; X-ray; 2.90 A; P=311-320. DR PDB; 8W2Y; X-ray; 1.63 A; A=542-591. DR PDB; 8W32; X-ray; 1.72 A; A=542-591. DR PDB; 8W37; X-ray; 2.07 A; A=542-591. DR PDB; 9ARN; X-ray; 1.41 A; A=542-591. DR PDB; 9ARP; X-ray; 2.04 A; A/B=542-591. DR AlphaFoldDB; P04578; -. DR BMRB; P04578; -. DR MDposit; P04578; -. DR MDRepo; P04578; -. DR SMR; P04578; -. DR BioGRID; 1205544; 160. DR DIP; DIP-58525N; -. DR IntAct; P04578; 141. DR MINT; P04578; -. DR BindingDB; P04578; -. DR ChEMBL; CHEMBL3520; -. DR TCDB; 1.G.16.1.3; the human immunodeficiency virus type 1 (hiv-1) fusion peptide (hiv-fp) family. DR GlyCosmos; P04578; 29 sites, No reported glycans. DR iPTMnet; P04578; -. DR SwissPalm; P04578; -. DR ABCD; P04578; 109 sequenced antibodies. DR GeneID; 155971; -. DR KEGG; vg:155971; -. DR Reactome; R-HSA-1462054; Alpha-defensins. DR Reactome; R-HSA-162588; Budding and maturation of HIV virion. DR Reactome; R-HSA-171286; Synthesis and processing of ENV and VPU. DR Reactome; R-HSA-173107; Binding and entry of HIV virion. DR Reactome; R-HSA-175474; Assembly Of The HIV Virion. DR Reactome; R-HSA-5621480; Dectin-2 family. DR EvolutionaryTrace; P04578; -. DR PRO; PR:P04578; -. DR Proteomes; UP000002241; Segment. DR Proteomes; UP000105453; Segment. 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:0016020; C:membrane; IEA:UniProtKB-UniRule. 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:UniProtKB-UniRule. DR GO; GO:0007015; P:actin filament organization; IDA:UniProtKB. DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-UniRule. DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-UniRule. DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule. DR GO; GO:1903905; P:positive regulation of establishment of T cell polarity; IDA:UniProtKB. DR GO; GO:1903908; P:positive regulation of plasma membrane raft polarization; IDA:UniProtKB. DR GO; GO:1903911; P:positive regulation of receptor clustering; IDA:UniProtKB. DR GO; GO:0046718; P:symbiont entry into host cell; EXP:DisProt. DR GO; GO:0042783; P:symbiont-mediated evasion of host immune response; EXP:DisProt. DR GO; GO:0019082; P:viral protein processing; IEA:UniProtKB-UniRule. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule. DR CDD; cd09909; HIV-1-like_HR1-HR2; 1. DR DisProt; DP00976; -. DR FunFam; 1.10.287.210:FF:000001; Envelope glycoprotein gp160; 1. DR FunFam; 1.20.5.490:FF:000001; Envelope glycoprotein gp160; 1. DR FunFam; 2.170.40.20:FF:000001; Envelope glycoprotein gp160; 1. DR FunFam; 2.170.40.20:FF:000003; Envelope glycoprotein gp160; 1. DR Gene3D; 1.10.287.210; -; 1. DR Gene3D; 2.170.40.20; Human immunodeficiency virus 1, Gp160, envelope glycoprotein; 2. DR Gene3D; 1.20.5.490; Single helix bin; 1. DR HAMAP; MF_04083; HIV_ENV; 1. DR InterPro; IPR036377; Gp120_core_sf. DR InterPro; IPR037527; Gp160. 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. DR PDBsum; 1AIK; -. DR PDBsum; 1DF4; -. DR PDBsum; 1DF5; -. DR PDBsum; 1DLB; -. DR PDBsum; 1FAV; -. DR PDBsum; 1G9M; -. DR PDBsum; 1GC1; -. DR PDBsum; 1GZL; -. DR PDBsum; 1K33; -. DR PDBsum; 1K34; -. DR PDBsum; 1MZI; -. DR PDBsum; 1RZJ; -. DR PDBsum; 2CMR; -. DR PDBsum; 2ME1; -. DR PDBsum; 2MG1; -. DR PDBsum; 2MG2; -. DR PDBsum; 2MG3; -. DR PDBsum; 2NY7; -. DR PDBsum; 2PV6; -. DR PDBsum; 2XRA; -. DR PDBsum; 3D0V; -. DR PDBsum; 3DNL; -. DR PDBsum; 3DNN; -. DR PDBsum; 3DNO; -. DR PDBsum; 3DRO; -. DR PDBsum; 3IDX; -. DR PDBsum; 3IDY; -. DR PDBsum; 3J70; -. DR PDBsum; 3MNZ; -. DR PDBsum; 3TYG; -. DR PDBsum; 3VIE; -. DR PDBsum; 4JPJ; -. DR PDBsum; 4JPK; -. DR PDBsum; 4YDV; -. DR PDBsum; 4ZTO; -. DR PDBsum; 5BN0; -. DR PDBsum; 5C0R; -. DR PDBsum; 5C0S; -. DR PDBsum; 5CIL; -. DR PDBsum; 5CIN; -. DR PDBsum; 5CMU; -. DR PDBsum; 5CMZ; -. DR PDBsum; 5CN0; -. DR PDBsum; 5DD0; -. DR PDBsum; 5GHW; -. DR PDBsum; 5H0N; -. DR PDBsum; 5HFL; -. DR PDBsum; 5HM1; -. DR PDBsum; 5IVX; -. DR PDBsum; 5KA5; -. DR PDBsum; 5KA6; -. DR PDBsum; 5NVP; -. DR PDBsum; 5NWU; -. DR PDBsum; 5NWW; -. DR PDBsum; 5TKJ; -. DR PDBsum; 5TKK; -. DR PDBsum; 5WDF; -. DR PDBsum; 5X08; -. DR PDBsum; 5YB2; -. DR PDBsum; 5YB3; -. DR PDBsum; 5YB4; -. DR PDBsum; 5YC0; -. DR PDBsum; 5Z0W; -. DR PDBsum; 5ZCX; -. DR PDBsum; 6B9K; -. DR PDBsum; 6BXP; -. DR PDBsum; 6BXQ; -. DR PDBsum; 6DE7; -. DR PDBsum; 6DLN; -. DR PDBsum; 6J5E; -. DR PDBsum; 6JQK; -. DR PDBsum; 6KTS; -. DR PDBsum; 6MQC; -. DR PDBsum; 6MQE; -. DR PDBsum; 6MQM; -. DR PDBsum; 6MQR; -. DR PDBsum; 6MQS; -. DR PDBsum; 6N16; -. DR PDBsum; 6NCP; -. DR PDBsum; 6NPR; -. DR PDBsum; 6O3G; -. DR PDBsum; 6O3J; -. DR PDBsum; 6O3L; -. DR PDBsum; 6O42; -. DR PDBsum; 6P60; -. DR PDBsum; 6P7H; -. DR PDBsum; 6P8D; -. DR PDBsum; 6PDR; -. DR PDBsum; 6PDS; -. DR PDBsum; 6PDU; -. DR PDBsum; 6PEC; -. DR PDBsum; 6PEF; -. DR PDBsum; 6PSA; -. DR PDBsum; 6RYF; -. DR PDBsum; 6SNC; -. DR PDBsum; 6SND; -. DR PDBsum; 6SNE; -. DR PDBsum; 6UBI; -. DR PDBsum; 6UCE; -. DR PDBsum; 6UCF; -. DR PDBsum; 6UJU; -. DR PDBsum; 6UJV; -. DR PDBsum; 6WWC; -. DR PDBsum; 7AEJ; -. DR PDBsum; 7EKB; -. DR PDBsum; 7EKK; -. DR PDBsum; 7FF1; -. DR PDBsum; 7LOH; -. DR PDBsum; 7LOI; -. DR PDBsum; 7N05; -. DR PDBsum; 7N08; -. DR PDBsum; 7R73; -. DR PDBsum; 7R74; -. DR PDBsum; 7RDW; -. DR PDBsum; 8B6Y; -. DR PDBsum; 8F3A; -. DR PDBsum; 8F3B; -. DR PDBsum; 8FYM; -. DR PDBsum; 8FZ2; -. DR PDBsum; 8G8A; -. DR PDBsum; 8G8C; -. DR PDBsum; 8G8D; -. DR PDBsum; 8IPG; -. DR PDBsum; 8TQ7; -. DR PDBsum; 8TQ8; -. DR PDBsum; 8TQ9; -. DR PDBsum; 8W2Y; -. DR PDBsum; 8W32; -. DR PDBsum; 8W37; -. DR PDBsum; 9ARN; -. DR PDBsum; 9ARP; -. PE 1: Evidence at protein level; KW 3D-structure; AIDS; Apoptosis; KW Clathrin-mediated endocytosis of virus by host; KW Cleavage on pair of basic residues; Coiled coil; Disulfide bond; KW Fusion of virus membrane with host endosomal membrane; KW Fusion of virus membrane with host membrane; Glycoprotein; KW Host cell membrane; Host endosome; Host membrane; Host-virus interaction; KW Lipoprotein; Membrane; Palmitate; Reference proteome; Signal; KW Transmembrane; Transmembrane helix; Viral attachment to host cell; KW Viral envelope protein; Viral immunoevasion; KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host; KW Virus entry into host cell. FT SIGNAL 1..32 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT CHAIN 33..856 FT /note="Envelope glycoprotein gp160" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT /id="PRO_0000239240" FT CHAIN 33..511 FT /note="Surface protein gp120" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT /id="PRO_0000038427" FT CHAIN 512..856 FT /note="Transmembrane protein gp41" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT /id="PRO_0000038428" FT TOPO_DOM 33..684 FT /note="Extracellular" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT TRANSMEM 685..705 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT TOPO_DOM 706..856 FT /note="Cytoplasmic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT REGION 131..156 FT /note="V1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT REGION 157..196 FT /note="V2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT REGION 296..330 FT /note="V3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT REGION 364..374 FT /note="CD4-binding loop" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT REGION 385..418 FT /note="V4" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT REGION 461..471 FT /note="V5" FT REGION 463..471 FT /note="V5" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT REGION 512..532 FT /note="Fusion peptide" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT REGION 574..592 FT /note="Immunosuppression" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:23383108" FT REGION 662..683 FT /note="MPER; binding to GalCer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT REGION 718..742 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 633..667 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT MOTIF 712..715 FT /note="YXXL motif; contains endocytosis signal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT MOTIF 855..856 FT /note="Di-leucine internalization motif" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT SITE 511..512 FT /note="Cleavage; by host furin" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT LIPID 764 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:7568235" FT LIPID 837 FT /note="S-palmitoyl cysteine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:7568235" FT CARBOHYD 88 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:19965434, ECO:0000269|PubMed:26972002" FT CARBOHYD 136 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT CARBOHYD 141 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT CARBOHYD 156 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:26972002" FT CARBOHYD 160 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:26972002" FT CARBOHYD 186 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT CARBOHYD 197 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:11188697, ECO:0000269|PubMed:14981267, FT ECO:0000269|PubMed:26972002, ECO:0000269|PubMed:9641677" FT CARBOHYD 230 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT CARBOHYD 234 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:11188697, ECO:0000269|PubMed:14981267, FT ECO:0000269|PubMed:26972002" FT CARBOHYD 241 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT CARBOHYD 262 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:11188697, ECO:0000269|PubMed:14981267, FT ECO:0000269|PubMed:23539181, ECO:0000269|PubMed:26972002, FT ECO:0000269|PubMed:9641677" FT CARBOHYD 276 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:11188697, ECO:0000269|PubMed:14981267, FT ECO:0000269|PubMed:26972002, ECO:0000269|PubMed:9641677" FT CARBOHYD 289 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:11188697, ECO:0000269|PubMed:14981267, FT ECO:0000269|PubMed:9641677" FT CARBOHYD 295 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:11188697, ECO:0000269|PubMed:14981267, FT ECO:0000269|PubMed:26972002, ECO:0000269|PubMed:9641677" FT CARBOHYD 301 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT CARBOHYD 332 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:21998254, ECO:0000269|PubMed:26972002, FT ECO:0000269|PubMed:9641677" FT CARBOHYD 339 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:11188697, ECO:0000269|PubMed:26972002, FT ECO:0000269|PubMed:9641677" FT CARBOHYD 356 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:17301785, ECO:0000269|PubMed:19965434, FT ECO:0007744|PDB:2NY7, ECO:0007744|PDB:3IDX, FT ECO:0007744|PDB:3IDY" FT CARBOHYD 386 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:11188697, ECO:0000269|PubMed:26972002, FT ECO:0000269|PubMed:9641677" FT CARBOHYD 392 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:11188697, ECO:0000269|PubMed:14981267, FT ECO:0000269|PubMed:26972002, ECO:0000269|PubMed:9641677" FT CARBOHYD 397 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT CARBOHYD 406 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT CARBOHYD 448 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:11188697, ECO:0000269|PubMed:14981267, FT ECO:0000269|PubMed:26972002, ECO:0000269|PubMed:9641677" FT CARBOHYD 463 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:11188697, ECO:0000269|PubMed:14981267" FT CARBOHYD 611 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:26972002" FT CARBOHYD 616 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT CARBOHYD 624 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT CARBOHYD 637 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083, FT ECO:0000269|PubMed:26972002" FT CARBOHYD 674 FT /note="N-linked (GlcNAc...) asparagine; by host" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT DISULFID 54..74 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT DISULFID 119..205 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT DISULFID 126..196 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT DISULFID 131..157 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT DISULFID 218..247 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT DISULFID 228..239 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT DISULFID 296..331 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT DISULFID 378..445 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT DISULFID 385..418 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT DISULFID 598..604 FT /evidence="ECO:0000255|HAMAP-Rule:MF_04083" FT MUTAGEN 764 FT /note="C->S: Complete loss of palmitoylation, decreased FT association with host cell membrane lipid rafts, decreased FT incorporation onto virions and severe reduction of FT infectivity; when associated with S-837." FT /evidence="ECO:0000269|PubMed:7568235" FT MUTAGEN 837 FT /note="C->S: Complete loss of palmitoylation, decreased FT association with host cell membrane lipid rafts, decreased FT incorporation onto virions and severe reduction of FT infectivity; when associated with S-764." FT /evidence="ECO:0000269|PubMed:7568235" FT STRAND 53..56 FT /evidence="ECO:0007829|PDB:7R73" FT STRAND 84..93 FT /evidence="ECO:0007829|PDB:1G9M" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:3IDX" FT HELIX 99..113 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 119..123 FT /evidence="ECO:0007829|PDB:1G9M" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:1GC1" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:1G9M" FT HELIX 212..214 FT /evidence="ECO:0007829|PDB:1RZJ" FT STRAND 215..218 FT /evidence="ECO:0007829|PDB:7R74" FT STRAND 223..228 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 235..247 FT /evidence="ECO:0007829|PDB:1G9M" FT HELIX 248..250 FT /evidence="ECO:0007829|PDB:1RZJ" FT STRAND 256..258 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:1G9M" FT HELIX 264..266 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 267..269 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 271..273 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 277..279 FT /evidence="ECO:0007829|PDB:1GC1" FT STRAND 280..282 FT /evidence="ECO:0007829|PDB:3TYG" FT STRAND 284..297 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 303..305 FT /evidence="ECO:0007829|PDB:3TYG" FT TURN 312..314 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 330..334 FT /evidence="ECO:0007829|PDB:1G9M" FT HELIX 335..352 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 359..361 FT /evidence="ECO:0007829|PDB:1G9M" FT HELIX 369..372 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 374..378 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 381..385 FT /evidence="ECO:0007829|PDB:1G9M" FT HELIX 388..390 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 393..395 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 413..417 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 420..425 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 427..430 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 432..434 FT /evidence="ECO:0007829|PDB:1G9M" FT HELIX 436..438 FT /evidence="ECO:0007829|PDB:1G9M" FT TURN 440..442 FT /evidence="ECO:0007829|PDB:3IDX" FT STRAND 444..456 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 466..470 FT /evidence="ECO:0007829|PDB:1G9M" FT HELIX 475..483 FT /evidence="ECO:0007829|PDB:1G9M" FT STRAND 486..490 FT /evidence="ECO:0007829|PDB:1G9M" FT HELIX 514..516 FT /evidence="ECO:0007829|PDB:5TKK" FT HELIX 525..528 FT /evidence="ECO:0007829|PDB:5NVP" FT HELIX 540..580 FT /evidence="ECO:0007829|PDB:8F3A" FT HELIX 583..594 FT /evidence="ECO:0007829|PDB:5HM1" FT STRAND 597..601 FT /evidence="ECO:0007829|PDB:7N05" FT HELIX 604..606 FT /evidence="ECO:0007829|PDB:7N05" FT HELIX 626..628 FT /evidence="ECO:0007829|PDB:6JQK" FT HELIX 629..650 FT /evidence="ECO:0007829|PDB:1DF4" FT HELIX 657..667 FT /evidence="ECO:0007829|PDB:3MNZ" FT TURN 668..670 FT /evidence="ECO:0007829|PDB:5NVP" FT HELIX 672..674 FT /evidence="ECO:0007829|PDB:7EKB" FT HELIX 675..683 FT /evidence="ECO:0007829|PDB:7EKB" FT HELIX 690..693 FT /evidence="ECO:0007829|PDB:2MG3" FT HELIX 698..709 FT /evidence="ECO:0007829|PDB:7LOH" FT STRAND 712..714 FT /evidence="ECO:0007829|PDB:6UJU" FT HELIX 742..745 FT /evidence="ECO:0007829|PDB:6UJU" FT HELIX 748..763 FT /evidence="ECO:0007829|PDB:6UJU" FT STRAND 766..769 FT /evidence="ECO:0007829|PDB:6UJU" FT HELIX 771..786 FT /evidence="ECO:0007829|PDB:6UJU" FT HELIX 791..820 FT /evidence="ECO:0007829|PDB:7LOH" FT STRAND 822..824 FT /evidence="ECO:0007829|PDB:7LOH" FT HELIX 826..841 FT /evidence="ECO:0007829|PDB:7LOH" FT HELIX 847..854 FT /evidence="ECO:0007829|PDB:7LOH" SQ SEQUENCE 856 AA; 97213 MW; 6FAB16AF85107FE0 CRC64; MRVKEKYQHL WRWGWRWGTM LLGMLMICSA TEKLWVTVYY GVPVWKEATT TLFCASDAKA YDTEVHNVWA THACVPTDPN PQEVVLVNVT ENFNMWKNDM VEQMHEDIIS LWDQSLKPCV KLTPLCVSLK CTDLKNDTNT NSSSGRMIME KGEIKNCSFN ISTSIRGKVQ KEYAFFYKLD IIPIDNDTTS YKLTSCNTSV ITQACPKVSF EPIPIHYCAP AGFAILKCNN KTFNGTGPCT NVSTVQCTHG IRPVVSTQLL LNGSLAEEEV VIRSVNFTDN AKTIIVQLNT SVEINCTRPN NNTRKRIRIQ RGPGRAFVTI GKIGNMRQAH CNISRAKWNN TLKQIASKLR EQFGNNKTII FKQSSGGDPE IVTHSFNCGG EFFYCNSTQL FNSTWFNSTW STEGSNNTEG SDTITLPCRI KQIINMWQKV GKAMYAPPIS GQIRCSSNIT GLLLTRDGGN SNNESEIFRP GGGDMRDNWR SELYKYKVVK IEPLGVAPTK AKRRVVQREK RAVGIGALFL GFLGAAGSTM GAASMTLTVQ ARQLLSGIVQ QQNNLLRAIE AQQHLLQLTV WGIKQLQARI LAVERYLKDQ QLLGIWGCSG KLICTTAVPW NASWSNKSLE QIWNHTTWME WDREINNYTS LIHSLIEESQ NQQEKNEQEL LELDKWASLW NWFNITNWLW YIKLFIMIVG GLVGLRIVFA VLSIVNRVRQ GYSPLSFQTH LPTPRGPDRP EGIEEEGGER DRDRSIRLVN GSLALIWDDL RSLCLFSYHR LRDLLLIVTR IVELLGRRGW EALKYWWNLL QYWSQELKNS AVSLLNATAI AVAEGTDRVI EVVQGACRAI RHIPRRIRQG LERILL //