ID B4ZYU4_HBV Unreviewed; 400 AA. AC B4ZYU4; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 58. DE RecName: Full=Large envelope protein {ECO:0000256|HAMAP-Rule:MF_04075}; DE AltName: Full=L glycoprotein {ECO:0000256|HAMAP-Rule:MF_04075}; DE AltName: Full=L-HBsAg {ECO:0000256|HAMAP-Rule:MF_04075}; DE Short=LHB {ECO:0000256|HAMAP-Rule:MF_04075}; DE AltName: Full=Large S protein {ECO:0000256|HAMAP-Rule:MF_04075}; DE AltName: Full=Large surface protein {ECO:0000256|HAMAP-Rule:MF_04075}; DE AltName: Full=Major surface antigen {ECO:0000256|HAMAP-Rule:MF_04075}; GN Name=S {ECO:0000256|HAMAP-Rule:MF_04075, ECO:0000313|EMBL:ACG68641.1}; OS Hepatitis B virus (HBV). OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC Blubervirales; Hepadnaviridae; Orthohepadnavirus. OX NCBI_TaxID=10407 {ECO:0000313|EMBL:ACG68641.1, ECO:0000313|Proteomes:UP000103653}; OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee). RN [1] {ECO:0000313|EMBL:ACG68641.1, ECO:0000313|Proteomes:UP000103653} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=114 {ECO:0000313|EMBL:ACG68641.1}; RA Sun X.-F., Zhang Y.-X., Hou J.-L., Wang Z.-H.; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The large envelope protein exists in two topological CC conformations, one which is termed 'external' or Le-HBsAg and the other CC 'internal' or Li-HBsAg. In its external conformation the protein CC attaches the virus to cell receptors and thereby initiating infection. CC This interaction determines the species specificity and liver tropism. CC This attachment induces virion internalization predominantly through CC caveolin-mediated endocytosis. The large envelope protein also assures CC fusion between virion membrane and endosomal membrane. In its internal CC conformation the protein plays a role in virion morphogenesis and CC mediates the contact with the nucleocapsid like a matrix protein. CC {ECO:0000256|HAMAP-Rule:MF_04075}. CC -!- FUNCTION: The middle envelope protein plays an important role in the CC budding of the virion. It is involved in the induction of budding in a CC nucleocapsid independent way. In this process the majority of envelope CC proteins bud to form subviral lipoprotein particles of 22 nm of CC diameter that do not contain a nucleocapsid. {ECO:0000256|HAMAP- CC Rule:MF_04075}. CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000256|HAMAP- CC Rule:MF_04075}. CC -!- DOMAIN: The large envelope protein is synthesized with the pre-S region CC at the cytosolic side of the endoplasmic reticulum and, hence will be CC within the virion after budding. Therefore the pre-S region is not N- CC glycosylated. Later a post-translational translocation of N-terminal CC pre-S and TM1 domains occur in about 50% of proteins at the virion CC surface. These molecules change their topology by an unknown mechanism, CC resulting in exposure of pre-S region at virion surface. For isoform M CC in contrast, the pre-S2 region is translocated cotranslationally to the CC endoplasmic reticulum lumen and is N-glycosylated. {ECO:0000256|HAMAP- CC Rule:MF_04075}. CC -!- PTM: Isoform M is N-terminally acetylated by host at a ratio of 90%, CC and N-glycosylated by host at the pre-S2 region. {ECO:0000256|HAMAP- CC Rule:MF_04075}. CC -!- PTM: Myristoylated. {ECO:0000256|HAMAP-Rule:MF_04075}. CC -!- SIMILARITY: Belongs to the orthohepadnavirus major surface antigen CC family. {ECO:0000256|HAMAP-Rule:MF_04075}. 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; EU787435; ACG68641.1; -; Genomic_DNA. DR Proteomes; UP000103653; Genome. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-UniRule. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0075513; P:caveolin-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW. DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule. DR HAMAP; MF_04075; HBV_HBSAG; 1. DR InterPro; IPR000349; HBV_HBSAG. DR Pfam; PF00695; vMSA; 1. PE 3: Inferred from homology; KW Acetylation {ECO:0000256|HAMAP-Rule:MF_04075}; KW Caveolin-mediated endocytosis of virus by host {ECO:0000256|HAMAP- KW Rule:MF_04075}; KW Fusion of virus membrane with host endosomal membrane {ECO:0000256|HAMAP- KW Rule:MF_04075}; KW Fusion of virus membrane with host membrane {ECO:0000256|HAMAP- KW Rule:MF_04075}; Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04075}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04075}; KW Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04075}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_04075, ECO:0000256|SAM:Phobius}; KW Myristate {ECO:0000256|HAMAP-Rule:MF_04075}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_04075, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04075, KW ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|HAMAP-Rule:MF_04075}; KW Viral penetration into host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04075}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04075}; KW Virus endocytosis by host {ECO:0000256|HAMAP-Rule:MF_04075}; KW Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04075}. FT INIT_MET 1 FT /note="Removed; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04075" FT CHAIN 2..400 FT /note="Large envelope protein" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04075" FT /id="PRO_5023427804" FT TOPO_DOM 2..253 FT /note="Intravirion; in internal conformation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04075" FT TOPO_DOM 2..181 FT /note="Virion surface; in external conformation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04075" FT TRANSMEM 182..200 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TOPO_DOM 203..253 FT /note="Intravirion; in external conformation" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04075" FT TRANSMEM 254..272 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TOPO_DOM 275..348 FT /note="Virion surface" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04075" FT TRANSMEM 344..373 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TOPO_DOM 370..375 FT /note="Intravirion" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04075" FT TRANSMEM 379..399 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TOPO_DOM 399..400 FT /note="Virion surface" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04075" FT REGION 1..55 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2..174 FT /note="Pre-S" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04075" FT REGION 2..119 FT /note="Pre-S1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04075" FT REGION 87..119 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 120..174 FT /note="Pre-S2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04075" FT COMPBIAS 93..119 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT LIPID 2 FT /note="N-myristoyl glycine; by host" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04075" SQ SEQUENCE 400 AA; 43729 MW; 5D49ED7A8C87B4DA CRC64; MGGWSSKPRQ GMGTNLSVPN PLGFFPDHQL DPAFGANSNN PDWDFNPNKD HWPEANQVGV GAFGPGFTPP HGGLLGWSPQ AQGILTAVPA APPPASTNRQ SGRQPTPISP PLRDSHPQAT QWNSTTFLQT LQDPRVRGLY FPAGGSSSGT VNPVPTTVSP ISSIFSRIGD PAPNMENITS GFLGPLLVLQ AGFFLLTRIL TIPQSLDSWW TSLNFLGGTT VCLGQNSQSP TSNHSPTSCP PTCPGYRWMC LRRFIIFLFI LLLCLIFLLV LLDYQGMLPV CPLIPGSPTT STGPCRTCTT PAQGTSMYPS CCCTKPLDGN CTCIPIPSSW AFGKFLWEWA SARFSWLSLL VPFVQWFVGL SPTVWLSVIW MMWYWGPSLY SILSPFLPLL PIFFCLWVYI //