ID Q1HSF8_9HIV1 Unreviewed; 846 AA. AC Q1HSF8; DT 13-JUN-2006, integrated into UniProtKB/TrEMBL. DT 13-JUN-2006, sequence version 1. DT 15-JAN-2008, entry version 17. DE Envelope glycoprotein. GN Name=env; OS Human immunodeficiency virus 1. OC Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae; OC Lentivirus; Primate lentivirus group. OX NCBI_TaxID=11676; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C61v1e3; 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). CC -!- FUNCTION: Allows rapid transcytosis of the virus through CD4 CC negative cells such as simple epithelial monolayers of the CC intestinal, rectal and endocervical epithelial barriers. Both CC gp120 and gp41 specifically recognize glycosphingolipids CC galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide CC (GalS) present in the lipid rafts structures of epithelial cells. CC Binding to these alternative receptors allows the rapid CC transcytosis of the virus through the epithelial cells. This CC transcytotic vesicle-mediated transport of virions from the apical CC side to the basolateral side of the epithelial cells does not CC involve infection of the cells themselves (By similarity). CC -!- FUNCTION: The transmembrane protein gp41 (TM) acts as a class I CC viral fusion protein. Under the current model, the protein has at CC least 3 conformational states: pre-fusion native state, pre- CC hairpin intermediate state, and post-fusion hairpin state. During CC viral and target cell membrane fusion, the coiled coil regions CC (heptad repeats) assume a trimer-of-hairpins structure, CC positioning the fusion peptide in close proximity to the C- CC terminal region of the ectodomain. The formation of this structure CC appears to drive apposition and subsequent fusion of viral and CC target cell membranes. Membranes fusion leads to delivery of the CC nucleocapsid into the cytoplasm (By similarity). 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 SMR; Q1HSF8; 82-126, 195-482, 530-616. DR GO; GO:0019031; C:viral envelope; IEA:InterPro. DR InterPro; IPR000328; Env_GP41. DR InterPro; IPR000777; GP120. DR Gene3D; G3DSA:2.170.40.20; GP120; 1. DR Pfam; PF00516; GP120; 1. DR Pfam; PF00517; GP41; 1. PE 3: Inferred from homology; KW AIDS; Apoptosis; Coiled coil; Envelope protein; Fusion protein; KW Host-virus interaction; Membrane; Transmembrane; Virion. 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 //