ID Q1HSF8_9HIV1 Unreviewed; 846 AA. AC Q1HSF8; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 10-MAY-2017, entry version 84. DE RecName: Full=Envelope glycoprotein gp160 {ECO:0000256|RuleBase:RU363095}; DE Contains: DE RecName: Full=Surface protein gp120 {ECO:0000256|RuleBase:RU363095}; DE Short=SU {ECO:0000256|RuleBase:RU363095}; DE AltName: Full=Glycoprotein 120 {ECO:0000256|RuleBase:RU363095}; DE Short=gp120 {ECO:0000256|RuleBase:RU363095}; DE Contains: DE RecName: Full=Transmembrane protein gp41 {ECO:0000256|RuleBase:RU363095}; DE Short=TM {ECO:0000256|RuleBase:RU363095}; GN Name=env {ECO:0000313|EMBL:ABE03508.1}; OS Human immunodeficiency virus 1. OC Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae; OC Lentivirus; Primate lentivirus group. OX NCBI_TaxID=11676 {ECO:0000313|EMBL:ABE03508.1}; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:ABE03508.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C61v1e3 {ECO:0000313|EMBL:ABE03508.1}; RX PubMed=16641269; DOI=10.1128/JVI.80.10.4758-4770.2006; RA Bailey J.R., Lassen K.G., Yang H.C., Quinn T.C., Ray S.C., RA Blankson J.N., Siliciano R.F.; RT "Neutralizing antibodies do not mediate suppression of human RT immunodeficiency virus type 1 in elite suppressors or selection of RT plasma virus variants in patients on highly active antiretroviral RT therapy."; RL J. Virol. 80:4758-4770(2006). RN [2] {ECO:0000213|PDB:5IQ9} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 645-673. RX PubMed=27053554; DOI=10.1128/JVI.03246-15; RA Kwon Y.D., Georgiev I.S., Ofek G., Zhang B., Asokan M., Bailer R.T., RA Bao A., Caruso W., Chen X., Choe M., Druz A., Ko S.Y., Louder M.K., RA McKee K., O'Dell S., Pegu A., Rudicell R., Shi W., Wang K., Yang Y., RA Alger M., Bender M.F., Carlton K., Cooper J.W., Blinn J., Eudailey J., RA Lloyd K., Parks R., Alam S.M., Haynes B.F., Padte N.N., Yu J., RA Ho D.D., Huang J., Connors M., Schwartz R.M., Mascola J.R., RA Kwong P.D.; RT "Optimization of the Solubility of HIV-1-Neutralizing Antibody 10E8 RT through Somatic Variation and Structure-Based Design."; RL J. Virol. 0:0-0(2016). CC -!- SUBUNIT: The mature envelope protein (Env) consists of a CC homotrimer of non-covalently associated gp120-gp41 heterodimers. CC The resulting complex protrudes from the virus surface as a spike. CC {ECO:0000256|RuleBase:RU363095}. CC -!- SUBCELLULAR LOCATION: Host cell membrane CC {ECO:0000256|SAAS:SAAS00797479}; Single-pass type I membrane CC protein {ECO:0000256|SAAS:SAAS00797479}. CC -!- SUBCELLULAR LOCATION: Host endosome membrane CC {ECO:0000256|SAAS:SAAS00797669}; Single-pass type I membrane CC protein {ECO:0000256|SAAS:SAAS00797669}. CC -!- SUBCELLULAR LOCATION: Virion membrane CC {ECO:0000256|SAAS:SAAS00796993}; Single-pass type I membrane CC protein {ECO:0000256|SAAS:SAAS00796993}. CC -!- DOMAIN: The 17 amino acids long immunosuppressive region is CC present in many retroviral envelope proteins. Synthetic peptides CC derived from this relatively conserved sequence inhibit immune CC function in vitro and in vivo. {ECO:0000256|RuleBase:RU363095}. 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; DQ410516; ABE03508.1; -; Genomic_RNA. DR PDB; 5IQ9; X-ray; 2.40 A; C/P=645-673. DR PDBsum; 5IQ9; -. DR ProteinModelPortal; Q1HSF8; -. 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0039663; P:membrane fusion involved in viral entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule. DR CDD; cd09909; HIV-1-like_HR1-HR2; 1. DR InterPro; IPR000328; GP41-like. DR InterPro; IPR000777; HIV1_GP160. DR Pfam; PF00516; GP120; 1. DR Pfam; PF00517; GP41; 1. DR SUPFAM; SSF56502; SSF56502; 2. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:5IQ9}; KW Apoptosis {ECO:0000256|RuleBase:RU363095, KW ECO:0000256|SAAS:SAAS00797441}; KW Cleavage on pair of basic residues {ECO:0000256|RuleBase:RU363095}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00487956}; KW Fusion of virus membrane with host membrane KW {ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00487637}; KW Host cell membrane {ECO:0000256|RuleBase:RU363095, KW ECO:0000256|SAAS:SAAS00797298}; KW Host endosome {ECO:0000256|RuleBase:RU363095, KW ECO:0000256|SAAS:SAAS00797530}; KW Host membrane {ECO:0000256|RuleBase:RU363095, KW ECO:0000256|SAAS:SAAS00797793}; KW Host-virus interaction {ECO:0000256|RuleBase:RU363095, KW ECO:0000256|SAAS:SAAS00797036}; KW Membrane {ECO:0000256|RuleBase:RU363095, KW ECO:0000256|SAAS:SAAS00797370}; KW Transmembrane {ECO:0000256|RuleBase:RU363095, KW ECO:0000256|SAAS:SAAS00797262}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363095, KW ECO:0000256|SAAS:SAAS00797734}; KW Viral attachment to host cell {ECO:0000256|RuleBase:RU363095, KW ECO:0000256|SAAS:SAAS00797747}; KW Viral envelope protein {ECO:0000256|RuleBase:RU363095, KW ECO:0000256|SAAS:SAAS00797156, ECO:0000313|EMBL:ABE03508.1}; KW Viral penetration into host cytoplasm {ECO:0000256|RuleBase:RU363095, KW ECO:0000256|SAAS:SAAS00132213}; KW Virion {ECO:0000256|RuleBase:RU363095, ECO:0000256|SAAS:SAAS00796948}; KW Virus entry into host cell {ECO:0000256|RuleBase:RU363095, KW ECO:0000256|SAAS:SAAS00797206}. FT TRANSMEM 668 695 Helical. {ECO:0000256|RuleBase:RU363095}. FT DOMAIN 33 501 GP120. {ECO:0000259|Pfam:PF00516}. FT DOMAIN 520 709 GP41. {ECO:0000259|Pfam:PF00517}. SQ SEQUENCE 846 AA; 95846 MW; E40EFAB2B740C443 CRC64; MTVMGIRKNY QHCGGWGALF LGVLLICSAA EQLWVTVYYG VPVWKEANTT LFCASDAKGY ETEKHNVWAT HACVPTDPSP QELVLANVTE NFNMWKNNMV EQMHEDIISL WDQSLKPCVK LTPLCVTLTC KNVTNTNGTK TNNSSEKTMR EEMKNCSFNI TTNIRDRIQK QYALFYKLDI VQIDENDNTS YRLISCNTSI ITQACPKVSF EPIPIHYCAP AGFAILKCNN ETFNGTGPCK NVSTVQCTHG IRPVVSTQLL LNGSLAKGEV IIRSANFSDN AKTIIVQLNE SVIINCTRPN NNTRKSIPIG PGRAFYATGD IIGDIRQAHC NVSRKQWNNT LKWVTAKLRE QFNKTIVFKN SSGGDPEIVM HSFNCGGEFF YCNTTPLFNN DTNNETEDNN NTITLQCRIK QIINMWQEVG KAMYAPPISG NISCSSNITG LLLTRDGGHN VSDMTETFRP GGGDMKDNWR SELYKYKVVR IEPLGIAPTK AKRRVVQREK RAVGLGAVFI GFLGAAGSTM GAASMTLTVQ ARQLLSGIVQ QQNNLLRAIE AQQHLLQLTV WGIKQLQARI LAVERYLKDQ QLLGIWGCSG KLICPTTVPW NNSWSNKSMK VIWENMTWMQ WEREIENYTG VIYSLIEESQ NQQERNEQEL LELDKWASLW NWFDITNWLW YIRLFIMIVG GLVGLRIIFV VLSIVNRVRQ GYSPLSFQIR PPAPRGPDRP EGIEEEGGER DRDTSGPLVN GFLEIIWVDL RSLCLFSYRH LRDLLLIAAR IVEILGRRGW EALKYWWNLL QYWSQELKNS AVSLLNAIAI AVAEGTDRIL EILQRAFRAI LHIPTRIRQG LERALL //