ID Q993A8_9HIV1 Unreviewed; 588 AA. AC Q993A8; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=Envelope glycoprotein gp160 {ECO:0000256|ARBA:ARBA00015406}; DE AltName: Full=Env polyprotein {ECO:0000256|ARBA:ARBA00029888}; DE Flags: Fragment; GN Name=env {ECO:0000313|EMBL:AAK20295.1}; OS Human immunodeficiency virus 1. OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus. OX NCBI_TaxID=11676 {ECO:0000313|EMBL:AAK20295.1}; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:AAK20295.1} RP NUCLEOTIDE SEQUENCE. RA Yang J.-Y., Tu C.-Y., Leu W.-M.; RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAK20295.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=11522189; DOI=10.1089/088922201316912808; RA D'Costa S., Slobod K.S., Webster R.G., White S.W., Hurwitz J.L.; RT "Structural features of HIV envelope defined by antibody escape mutant RT analysis."; RL AIDS Res. Hum. Retroviruses 17:1205-1209(2001). RN [3] {ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3} RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 26-435, GLYCOSYLATION AT ASN-31 RP AND ASN-298, AND DISULFIDE BONDS. 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). 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 --------------------------------------------------------------------------- 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; AF321147; AAK20295.1; -; Genomic_DNA. DR PIR; A53591; A53591. DR PDB; 2NY1; X-ray; 1.99 A; A=26-435. DR PDB; 2NY3; X-ray; 2.00 A; A=26-435. DR PDBsum; 2NY1; -. DR PDBsum; 2NY3; -. DR SMR; Q993A8; -. DR GlyCosmos; Q993A8; 14 sites, No reported glycans. DR EvolutionaryTrace; Q993A8; -. 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 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 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3}; KW Apoptosis {ECO:0000256|ARBA:ARBA00022703}; KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511}; KW Host endosome {ECO:0000256|ARBA:ARBA00023046}; KW Host membrane {ECO:0000256|ARBA:ARBA00022870}; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Viral envelope protein {ECO:0000313|EMBL:AAK20295.1}; KW Virion {ECO:0000313|EMBL:AAK20295.1}. FT TRANSMEM 455..476 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..454 FT /note="Human immunodeficiency virus 1 envelope glycoprotein FT Gp120" FT /evidence="ECO:0000259|Pfam:PF00516" FT DOMAIN 473..587 FT /note="Retroviral envelope protein GP41-like" FT /evidence="ECO:0000259|Pfam:PF00517" FT CARBOHYD 31 FT /note="N-acetyl-D-glucosamine 1" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 31 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 140 FT /note="N-acetyl-D-glucosamine 2" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 140 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 173 FT /note="N-acetyl-D-glucosamine 3" FT /evidence="ECO:0007829|PDB:2NY3" FT CARBOHYD 173 FT /note="N-acetyl-D-glucosamine 4" FT /evidence="ECO:0007829|PDB:2NY1" FT CARBOHYD 173 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 175 FT /note="N-acetyl-D-glucosamine 3" FT /evidence="ECO:0007829|PDB:2NY3" FT CARBOHYD 177 FT /note="N-acetyl-D-glucosamine 5" FT /evidence="ECO:0007829|PDB:2NY1" FT CARBOHYD 177 FT /note="N-acetyl-D-glucosamine 6" FT /evidence="ECO:0007829|PDB:2NY3" FT CARBOHYD 177 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 179 FT /note="N-acetyl-D-glucosamine 6" FT /evidence="ECO:0007829|PDB:2NY3" FT CARBOHYD 181 FT /note="N-acetyl-D-glucosamine 3" FT /evidence="ECO:0007829|PDB:2NY3" FT CARBOHYD 181 FT /note="N-acetyl-D-glucosamine 4" FT /evidence="ECO:0007829|PDB:2NY1" FT CARBOHYD 184 FT /note="N-acetyl-D-glucosamine 7" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 184 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 205 FT /note="N-acetyl-D-glucosamine 8" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 205 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 213 FT /note="N-acetyl-D-glucosamine 9" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 219 FT /note="N-acetyl-D-glucosamine 10" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 219 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 232 FT /note="N-acetyl-D-glucosamine 9" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 232 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 234 FT /note="N-acetyl-D-glucosamine 11" FT /evidence="ECO:0007829|PDB:2NY3" FT CARBOHYD 236 FT /note="N-acetyl-D-glucosamine 12" FT /evidence="ECO:0007829|PDB:2NY1" FT CARBOHYD 238 FT /note="N-acetyl-D-glucosamine 12" FT /evidence="ECO:0007829|PDB:2NY1" FT CARBOHYD 238 FT /note="N-acetyl-D-glucosamine 13" FT /evidence="ECO:0007829|PDB:2NY3" FT CARBOHYD 238 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 282 FT /note="N-acetyl-D-glucosamine 14" FT /evidence="ECO:0007829|PDB:2NY3" FT CARBOHYD 282 FT /note="N-acetyl-D-glucosamine 15" FT /evidence="ECO:0007829|PDB:2NY1" FT CARBOHYD 282 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 286 FT /note="N-acetyl-D-glucosamine 14" FT /evidence="ECO:0007829|PDB:2NY3" FT CARBOHYD 329 FT /note="N-acetyl-D-glucosamine 16" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 329 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 335 FT /note="N-acetyl-D-glucosamine 17" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 335 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 390 FT /note="N-acetyl-D-glucosamine 8" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 391 FT /note="N-acetyl-D-glucosamine 11" FT /evidence="ECO:0007829|PDB:2NY3" FT CARBOHYD 391 FT /note="N-acetyl-D-glucosamine 18" FT /evidence="ECO:0007829|PDB:2NY1" FT CARBOHYD 391 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT CARBOHYD 405 FT /note="N-acetyl-D-glucosamine 19" FT /evidence="ECO:0007829|PDB:2NY1" FT CARBOHYD 406 FT /note="N-acetyl-D-glucosamine 19" FT /evidence="ECO:0007829|PDB:2NY1" FT CARBOHYD 406 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007829|PDB:2NY1" FT DISULFID 62..148 FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT DISULFID 69..139 FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT DISULFID 161..190 FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT DISULFID 171..182 FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT DISULFID 239..274 FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT DISULFID 321..388 FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT DISULFID 328..361 FT /evidence="ECO:0007829|PDB:2NY1, ECO:0007829|PDB:2NY3" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAK20295.1" FT NON_TER 588 FT /evidence="ECO:0000313|EMBL:AAK20295.1" SQ SEQUENCE 588 AA; 65643 MW; 47475A5780240AE8 CRC64; AKAYDTEVHN VWATHACVPT DPNPQEVVLV NVTENFNMWK NDMVEQMHED IISLWDQSLK PCVKLTPLCV SLKCTDLKND TNTNSSSGRM IMEKGEIKNC SFNISTSIRG KVQKEYAFFY KLDIIPIDND TTSYTLTSCN TSVITQACPK VSFEPIPIHY CAPAGFAILK CNNKTFNGTG PCTNVSTVQC THGIRPVVST QLLLNGSLAE EEVVIRSVNF TDNAKTIIVQ LNTSVEINCT RPNNNTRKKI RIQRGPGRAF VTIGKIGNMR QAHCNISRAK WNATLKQIAS KLREQFGNNK TIIFKQSSGG DPEIVTHSFN CGGEFFYCNS TQLFNSTWFN STWSTEGSNN TEGSDTITLP CRIKQIINMW QEVGKAMYAP PISGQIRCSS NITGLLLTRD GGNSNNESEI FRPGGGDMRD NWRSELYKYK VVKIEPLGVA PTKAKRRVVQ REKRAVGIGA LFLGFLGAAG STMGAASMTL TVQARQLLSG IVQQQNNLLR AIEAQQHLLQ LTVWGIKQLQ ARILAVERYL KDQQLLGIWG CSGKLICTTA VPWNASWSNK SLEQIWNNMT WMEWDREINN YTSLIHSL //