ID Q6TMG7_9HEPA Unreviewed; 330 AA. AC Q6TMG7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 12-AUG-2020, entry version 59. DE RecName: Full=Large envelope protein {ECO:0000256|RuleBase:RU003356}; OS Duck hepatitis B virus. OC Viruses; Hepadnaviridae; Avihepadnavirus. OX NCBI_TaxID=12639 {ECO:0000313|EMBL:AAQ93080.1, ECO:0000313|Proteomes:UP000158610}; RN [1] {ECO:0000313|EMBL:AAQ93080.1, ECO:0000313|Proteomes:UP000158610} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GD1 {ECO:0000313|EMBL:AAQ93080.1}; RX PubMed=16015703; RA He J.Y., Zhu Y.T., Yang R.Y., Feng L.L., Guo X.B., Zhang F.X., Chen H.S.; RT "Mutations outside the YMDD motif in the P protein can also cause DHBV RT resistant to Lamivudine."; RL World J. Gastroenterol. 11:4261-4267(2005). 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 The large envelope protein probably also assumes fusion between virion CC and host membranes. In its internal conformation the protein plays a CC role in virion morphogenesis and mediates the contact with the CC nucleocapsid like a matrix protein. {ECO:0000256|ARBA:ARBA00003608}. CC -!- FUNCTION: Truncated S protein may be involved in translocation of pre-S CC domain through the virion membrane. {ECO:0000256|ARBA:ARBA00002006}. CC -!- SUBUNIT: Large internal envelope protein interacts with capsid protein. CC {ECO:0000256|ARBA:ARBA00011793}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}. Virion CC membrane {ECO:0000256|ARBA:ARBA00004182}. CC -!- SIMILARITY: Belongs to the avihepadnavirus major surface antigen CC family. {ECO:0000256|ARBA:ARBA00009335}. 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; AY392760; AAQ93080.1; -; Genomic_DNA. DR Proteomes; UP000158610; Genome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016032; P:viral process; IEA:InterPro. DR InterPro; IPR000349; HBV_HBSAG. DR Pfam; PF00695; vMSA; 2. PE 3: Inferred from homology; KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Virion {ECO:0000256|ARBA:ARBA00022844}. FT TRANSMEM 168..189 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 239..259 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 298..328 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT REGION 63..125 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 88..108 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 330 AA; 36482 MW; 385F6E9AABD5AA98 CRC64; MGQSPAKSMD VRRIEGGELL LQQLAGRMIP KGTVTWSGKF PTIDHVLDHV QTMEEINTLQ NQGAWPEGAG RRAGLTNPAP QEIPQPKWTP EEDQKAREAF RRYQEERPPE TTTIPPTSPT QWKLQPGDDP LLGNKSLLET HPIYQNPEPA AVPVIKTPPL KKKMSGTFGG ILAGLIGLLV SFFLLIKILE ILRRLDWWWI SLSSPKGKMQ CAFQDTGAQT SPHYVGSCPW GCPGFLWTYL RLFIIFLLIL LVAAGLLYLT DNGSTILGKL QWASVSALFS SISSLLPSDQ KSLVALMFGL LLIWMTSSSA TQTLVTLTQL ATLSALFYKS //