HBSAG_DHBV3
ID HBSAG_DHBV3 Reviewed; 328 AA.
AC P0C684;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Large envelope protein;
DE AltName: Full=L glycoprotein;
DE AltName: Full=L-HBsAg;
DE Short=LHB;
DE AltName: Full=Large S protein;
DE AltName: Full=Large surface protein;
DE AltName: Full=Major surface antigen;
GN Name=S;
OS Duck hepatitis B virus (strain Germany/DHBV-3) (DHBV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Avihepadnavirus.
OX NCBI_TaxID=489542;
OH NCBI_TaxID=8835; Anas (ducks).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3981148; DOI=10.1002/jmv.1890150402;
RA Sprengel R., Kuhn C., Will H., Schaller H.;
RT "Comparative sequence analysis of duck and human hepatitis B virus
RT genomes.";
RL J. Med. Virol. 15:323-333(1985).
RN [2]
RP ALTERNATIVE INITIATION.
RX PubMed=8212596; DOI=10.1006/viro.1993.1567;
RA Fernholz D., Wildner G., Will H.;
RT "Minor envelope proteins of duck hepatitis B virus are initiated at
RT internal pre-S AUG codons but are not essential for infectivity.";
RL Virology 197:64-73(1993).
RN [3]
RP TRANSMEMBRANE TOPOLOGY.
RX PubMed=9371604; DOI=10.1128/jvi.71.12.9434-9441.1997;
RA Swameye I., Schaller H.;
RT "Dual topology of the large envelope protein of duck hepatitis B virus:
RT determinants preventing pre-S translocation and glycosylation.";
RL J. Virol. 71:9434-9441(1997).
RN [4]
RP TOPOLOGICAL CONFORMATION.
RX PubMed=17045625; DOI=10.1016/j.virol.2006.09.006;
RA Franke C., Matschl U., Bruns M.;
RT "Enzymatic treatment of duck hepatitis B virus: topology of the surface
RT proteins for virions and noninfectious subviral particles.";
RL Virology 359:126-136(2007).
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 (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Truncated S protein may be involved in translocation of pre-S
CC domain through the virion membrane. {ECO:0000250}.
CC -!- SUBUNIT: Large internal envelope protein interacts with capsid protein.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=L; Synonyms=Large envelope protein, LHB, L-HBsAg;
CC IsoId=P0C684-1; Sequence=Displayed;
CC Name=S; Synonyms=Small envelope protein, SHB, S-HBsAg;
CC IsoId=P0C684-2; Sequence=VSP_031897;
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.
CC -!- PTM: Myristoylation contributes importantly to DHBV infectivity. It is
CC most likely required for an early step of the life cycle involving the
CC entry or uncoating of virus particles.
CC -!- PTM: Phosphorylated on pre-S domain for about 50% of L proteins, the L
CC chains with internal pre-S region (Li-HBsAg).
CC -!- SIMILARITY: Belongs to the avihepadnavirus major surface antigen
CC family. {ECO:0000305}.
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DR EMBL; DQ195079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PRIDE; P0C684; -.
DR Proteomes; UP000007204; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0039663; P:membrane fusion involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR000349; HBV_HBSAG.
DR Pfam; PF00695; vMSA; 2.
PE 1: Evidence at protein level;
KW Alternative initiation; Fusion of virus membrane with host membrane;
KW Glycoprotein; Host-virus interaction; Lipoprotein; Membrane; Myristate;
KW Phosphoprotein; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral penetration into host cytoplasm;
KW Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..328
FT /note="Large envelope protein"
FT /id="PRO_0000322376"
FT TOPO_DOM 2..236
FT /note="Intravirion; in internal conformation"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2..163
FT /note="Virion surface; in external conformation"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical; Name=TM1; Note=In external conformation"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..236
FT /note="Intravirion; in external conformation"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical; Name=TM2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..282
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical; Name=TM3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..328
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 2..161
FT /note="Pre-S"
FT /evidence="ECO:0000250"
FT REGION 77..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE ?238..?239
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..161
FT /note="Missing (in isoform S)"
FT /evidence="ECO:0000305"
FT /id="VSP_031897"
SQ SEQUENCE 328 AA; 36218 MW; B26768D718127EE9 CRC64;
MGQHPAKSMD VRRIEGGELL LNQLAGRMIP KGTLTWSGKF PTIDHVLDHV QTMEEINTLQ
QQGAWPAGAG RRVGLSNPAP QEIPQPQWTP EEDQKAREAF RRYQEERPPE TTTIPPTSPT
QWKLQPGDDP LLGNQSLLET HPLYQTEPAV PVIKTPPLKK KMSGTFGGIL AGLIGLLVSF
FLLIKILEIL RRLDWWWISL SSPKGKMQCA FQDTGAQISP HYAGSCPWGC PGFLWTYLRL
FIIFLLILLV AAGLLYLTDN GSTILGKLQW ASVSALFSSI SSLLPSDPKS LVALTFGLSL
IWMTSSSATQ TLVTLTQLAT LSALFYKS
