ID D5LBD8_HBV Unreviewed; 400 AA. AC D5LBD8; DT 15-JUN-2010, integrated into UniProtKB/TrEMBL. DT 15-JUN-2010, sequence version 1. DT 16-JAN-2019, entry version 36. 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:ADF05703.1}; GN ORFNames=HBVgp2 {ECO:0000313|EMBL:ADF05703.1}; OS Hepatitis B virus (HBV). OC Viruses; Retro-transcribing viruses; Hepadnaviridae; OC Orthohepadnavirus. OX NCBI_TaxID=10407 {ECO:0000313|EMBL:ADF05703.1, ECO:0000313|Proteomes:UP000112467}; OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee). OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] {ECO:0000313|EMBL:ADF05703.1, ECO:0000313|Proteomes:UP000112467, ECO:0000313|Proteomes:UP000164999} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A2-10 {ECO:0000313|EMBL:ADF05759.1}, and A2-2 RC {ECO:0000313|EMBL:ADF05703.1}; RX PubMed=20089644; DOI=10.1128/JVI.02164-09; RA Wang H.Y., Chien M.H., Huang H.P., Chang H.C., Wu C.C., Chen P.J., RA Chang M.H., Chen D.S.; RT "Distinct hepatitis B virus dynamics in the immunotolerant and early RT immunoclearance phases."; RL J. Virol. 84:3454-3463(2010). RN [2] {ECO:0000313|EMBL:ADF05703.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=A2-10 {ECO:0000313|EMBL:ADF05759.1}, and A2-2 RC {ECO:0000313|EMBL:ADF05703.1}; RA Wang H.-Y., Chien M.-H., Huang H.-P., Chang H.-C., Wu C.-C., RA Chen P.-J., Chang M.-H., Chen D.-S.; RL Submitted (FEB-2010) 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 CC other 'internal' or Li-HBsAg. In its external conformation the CC protein attaches the virus to cell receptors and thereby CC initiating infection. This interaction determines the species CC specificity and liver tropism. This attachment induces virion CC internalization predominantly through caveolin-mediated CC endocytosis. The large envelope protein also assures fusion CC 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, ECO:0000256|SAAS:SAAS00968829}. CC -!- FUNCTION: The middle envelope protein plays an important role in CC the budding of the virion. It is involved in the induction of CC budding in a nucleocapsid independent way. In this process the CC majority of envelope proteins bud to form subviral lipoprotein CC particles of 22 nm of diameter that do not contain a nucleocapsid. CC {ECO:0000256|HAMAP-Rule:MF_04075, ECO:0000256|SAAS:SAAS00968840}. CC -!- SUBUNIT: Li-HBsAg interacts with capsid protein and with HDV Large CC delta antigen. Isoform M associates with host chaperone CANX CC through its pre-S2 N glycan. This association may be essential for CC M proper secretion. {ECO:0000256|HAMAP-Rule:MF_04075, CC ECO:0000256|SAAS:SAAS00968834}. CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000256|HAMAP- CC Rule:MF_04075, ECO:0000256|SAAS:SAAS00968828}. CC -!- DOMAIN: The large envelope protein is synthesized with the pre-S CC region at the cytosolic side of the endoplasmic reticulum and, CC hence will be within the virion after budding. Therefore the pre-S CC region is not N-glycosylated. Later a post-translational CC translocation of N-terminal pre-S and TM1 domains occur in about CC 50% of proteins at the virion surface. These molecules change CC their topology by an unknown mechanism, resulting in exposure of CC pre-S region at virion surface. For isoform M in contrast, the CC pre-S2 region is translocated cotranslationally to the endoplasmic CC 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 CC 90%, and N-glycosylated by host at the pre-S2 region. CC {ECO:0000256|HAMAP-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 ECO:0000256|SAAS:SAAS00968839}. 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; GU815561; ADF05703.1; -; Genomic_DNA. DR EMBL; GU815569; ADF05759.1; -; Genomic_DNA. DR OrthoDB; 10974at10239; -. DR Proteomes; UP000112467; Genome. DR Proteomes; UP000164999; Genome. DR GO; GO:0016021; C:integral component of 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, ECO:0000256|SAAS:SAAS00968835}; KW Complete proteome {ECO:0000313|Proteomes:UP000112467, KW ECO:0000313|Proteomes:UP000164999}; KW Fusion of virus membrane with host endosomal membrane KW {ECO:0000256|HAMAP-Rule:MF_04075, ECO:0000256|SAAS:SAAS00968831}; KW Fusion of virus membrane with host membrane {ECO:0000256|HAMAP- KW Rule:MF_04075, ECO:0000256|SAAS:SAAS00968838}; KW Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04075}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04075, KW ECO:0000256|SAAS:SAAS00968843}; KW Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04075}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_04075, KW ECO:0000256|SAAS:SAAS00968830, ECO:0000256|SAM:Phobius}; KW Myristate {ECO:0000256|HAMAP-Rule:MF_04075}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_04075, KW ECO:0000256|SAAS:SAAS00968837, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04075, KW ECO:0000256|SAAS:SAAS00968833, ECO:0000256|SAM:Phobius}; KW Viral attachment to host cell {ECO:0000256|HAMAP-Rule:MF_04075, KW ECO:0000256|SAAS:SAAS00968842}; KW Viral penetration into host cytoplasm {ECO:0000256|HAMAP- KW Rule:MF_04075, ECO:0000256|SAAS:SAAS00968841}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04075, KW ECO:0000256|SAAS:SAAS00968826}; KW Virus endocytosis by host {ECO:0000256|HAMAP-Rule:MF_04075, KW ECO:0000256|SAAS:SAAS00968827}; KW Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04075, KW ECO:0000256|SAAS:SAAS00968836}. FT INIT_MET 1 1 Removed; by host. {ECO:0000256|HAMAP- FT Rule:MF_04075}. FT TOPO_DOM 2 253 Intravirion; in internal conformation. FT {ECO:0000256|HAMAP-Rule:MF_04075}. FT TOPO_DOM 2 181 Virion surface; in external conformation. FT {ECO:0000256|HAMAP-Rule:MF_04075}. FT TOPO_DOM 203 253 Intravirion; in external conformation. FT {ECO:0000256|HAMAP-Rule:MF_04075}. FT TRANSMEM 254 272 Helical. {ECO:0000256|SAM:Phobius}. FT TOPO_DOM 275 348 Virion surface. {ECO:0000256|HAMAP-Rule: FT MF_04075}. FT TRANSMEM 344 373 Helical. {ECO:0000256|SAM:Phobius}. FT TOPO_DOM 370 375 Intravirion. {ECO:0000256|HAMAP-Rule: FT MF_04075}. FT TRANSMEM 379 399 Helical. {ECO:0000256|SAM:Phobius}. FT TOPO_DOM 399 400 Virion surface. {ECO:0000256|HAMAP-Rule: FT MF_04075}. FT REGION 2 174 Pre-S. {ECO:0000256|HAMAP-Rule:MF_04075}. FT REGION 2 119 Pre-S1. {ECO:0000256|HAMAP-Rule: FT MF_04075}. FT REGION 120 174 Pre-S2. {ECO:0000256|HAMAP-Rule: FT MF_04075}. FT LIPID 2 2 N-myristoyl glycine; by host. FT {ECO:0000256|HAMAP-Rule:MF_04075}. SQ SEQUENCE 400 AA; 43715 MW; 51B5C03A3692694D CRC64; MGGWSSKPRK GMGTNLSVPN PLGFFPDHQL DPAFKANSEN PDWDLNPHKD NWPDANKVGV GAFGPGFTPP HGGLLGWSPQ AQGLLTTVPA APPPASTNRQ SGRQPTPLSP PLRDTHPQAM QWNSTTFHQT LQDPRVRALY FPAGGSSSGT VSPAQNTVSA ISSILSKTGD PVPNMENIAS GLLGPLLVLQ AGFFLLTKIL TIPQSLDSWW TSLNFLGGTP VCLGQNSQSQ ISSHSPTCCP PICPGYRWMC LRRFIIFLCI LLLCLIFLLV LLDYQGMLPV CPLIPGSSTT STGPCKTCTT PAQGTSMFPS CCCTKPTDGN CTCIPIPSSW AFAKYLWEWA SVRFSWLSLL VPFVQWFVGL SPIVWLSVIW MMWFWGPSLY NILSPFIPLL PIFFCLWVYI //