ID J9XVC2_SIV Unreviewed; 887 AA. AC J9XVC2; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 09-JAN-2013, entry version 2. DE SubName: Full=Envelope glycoprotein; OS Simian immunodeficiency virus - sm. OC Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae; OC Lentivirus; Primate lentivirus group. OX NCBI_TaxID=11712; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=783; RA Dang Q., Whitted S., Goeken R.M., Masuda K., Brown C.R., RA Brenchley J.M., Keele B.F., Lafont B., Starost M.F., Iyengar R., RA Plishka R.J., Buckler-White A., Lifson J.D., Hirsch V.M.; RT "Immune activation plays a role in the development of neurological RT disease in SIV-infected macaques."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The envelope glyprotein gp160 precursor down-modulates CC cell surface CD4 antigen by interacting with it in the endoplasmic CC reticulum and blocking its transport to the cell surface (By CC similarity). CC -!- FUNCTION: The gp120-gp41 heterodimer allows rapid transcytosis of CC the virus through CD4 negative cells such as simple epithelial CC monolayers of the intestinal, rectal and endocervical epithelial CC barriers. Both gp120 and gp41 specifically recognize CC glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo- CC galactosyl-ceramide (GalS) present in the lipid rafts structures CC of epithelial cells. Binding to these alternative receptors allows CC the rapid transcytosis of the virus through the epithelial cells. CC This transcytotic vesicle-mediated transport of virions from the CC apical side to the basolateral side of the epithelial cells does CC not involve infection of the cells themselves (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; JQ686972; AFS33706.1; -; Genomic_RNA. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR Gene3D; 2.170.40.20; GP120; 2. DR InterPro; IPR000777; HIV1_GP160. DR InterPro; IPR000328; Retroviral_envelope_protein. DR Pfam; PF00516; GP120; 1. DR Pfam; PF00517; GP41; 1. DR SUPFAM; SSF56502; GP120; 1. PE 3: Inferred from homology; KW Apoptosis; Disulfide bond; KW Fusion of virus membrane with host membrane; Host cell membrane; KW Host endosome; Host membrane; Host-virus interaction; Membrane; KW Transmembrane; Transmembrane helix; Viral attachment to host cell; KW Viral envelope protein; Viral penetration into host cytoplasm; Virion; KW Virus entry into host cell. SQ SEQUENCE 887 AA; 102186 MW; 1B26ACDC118B61CF CRC64; MGCLGNQLLI ALLLVSVLEI WCVQYVTVFY GVPAWKNATI PLFCATRNRD TWGTTQCLPD NDDYSELAVN ITEAFDAWDN TVTEQAIEDV WNLFETSIKP CVKLTPLCIA MRCNKTETDR WGLTGEAGTA TTTKSTTSPT TTTVTPKVIN EGDSCIKNDS CAGLEQEPMI GCKFNMTGLK RDKKTEYNET WYARDLICEQ SANESESKCY MQHCNTSVIQ ESCDKHYWDA IRFRYCAPPG YALLRCNDSN YSGFAPNCSK VVVSSCTRMM ETQTSTWFGF NGTRAENRTY IYWHGNSNRT IISLNKFYNL TMKCRRPGNK TVLPVTIMSG LVFHSQPINE RPKQAWCRFG GNWSEAIQEV KETLVKHPRY TGTNETRKIN LTAPAGGDPE VTFMWTNCRG EFLYCKMNWF LNWVEDRDQN GSRWKQQKNS EQQKRNYVPC HIRQIINTWH KVGKNVYLPP REGDLTCNST VTSLIAEIDW INNNETNITM SAEVAQLYRL ELGDYKLVEI TPIGLAPTNV RRYTTTGASR NKXGVFVLGF LGFLATAGSA MGAASLTLSA QSRTLLAGIV QQQQQLLDVV KRQQELLRLT VWGTKNLQTR VTAIEKYLKD QAQLNSWGCA FRQVCHTTVQ WPNNSLVPNW NNMTWQEWER QVDFLEANIT QLLEEAQIQQ EKNMYELQKL NSWDIFGNWF DLTSWLRYIQ YGVLIVLGVV GLRIVIYVVQ MLARLRQGYR PVFSPPPVYV QQIPIHKDQE PPTKEGEEGE GGDRGGSKSW PWQIEYIHFL IRQLIRLLTW LFSSCRDWLL RIYQTLQPVL QRLSRTLQRV REVIRIERAY LQYGWSYFQE AAQAWWRFAR ETLASAWRDI WETLGRVGRG ILAIPRRVRQ GLELTLL //