HBSAG_HHBV
ID HBSAG_HHBV Reviewed; 335 AA.
AC P13847; Q67853;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 85.
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;
DE Contains:
DE RecName: Full=Truncated S protein;
DE Short=St;
GN Name=S;
OS Heron hepatitis B virus (HHBV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Avihepadnavirus.
OX NCBI_TaxID=28300;
OH NCBI_TaxID=8899; Ardeidae (herons).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3418788; DOI=10.1128/jvi.62.10.3832-3839.1988;
RA Sprengel R., Kaleta E.F., Will H.;
RT "Isolation and characterization of a hepatitis B virus endemic in herons.";
RL J. Virol. 62:3832-3839(1988).
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=P13847-1; Sequence=Displayed;
CC Name=S; Synonyms=Small envelope protein, SHB, S-HBsAg;
CC IsoId=P13847-2; Sequence=VSP_031891;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA45740.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M22056; AAA45739.1; -; Genomic_DNA.
DR EMBL; M22056; AAA45740.1; ALT_INIT; Genomic_DNA.
DR PIR; B30082; SAVLHH.
DR RefSeq; NP_040999.1; NC_001486.1. [P13847-1]
DR RefSeq; NP_041000.1; NC_001486.1. [P13847-2]
DR GeneID; 2703546; -.
DR GeneID; 2703548; -.
DR KEGG; vg:2703548; -.
DR Proteomes; UP000008679; 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 3: Inferred from homology;
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..335
FT /note="Large envelope protein"
FT /id="PRO_0000038085"
FT CHAIN 167..?243
FT /note="Truncated S protein"
FT /id="PRO_0000322200"
FT TOPO_DOM 2..241
FT /note="Cytoplasmic; in internal conformation"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2..167
FT /note="Extracellular; in external conformation"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical; Name=TM1; Note=In internal conformation"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..241
FT /note="Cytoplasmic; in external conformation"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical; Name=TM2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..295
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical; Name=TM3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..335
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 2..166
FT /note="Pre-S"
FT /evidence="ECO:0000250"
FT REGION 68..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE ?243..?244
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 265
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..166
FT /note="Missing (in isoform S)"
FT /evidence="ECO:0000305"
FT /id="VSP_031891"
SQ SEQUENCE 335 AA; 37219 MW; E90F7DA6A0623354 CRC64;
MGHTQAKSTT DRRVEGGELL LQHLAGRMIP PEFSGPITTA GKFPTIQHVM DHIDSVEELR
TLQAGGHWPE GTARRLGLDQ PRPTPPPITW TEEEDKKAKE FFKQYQENRP KPAETAPPPI
TELHAAEPPQ WKISPEDPLL KAKALIPVKE PEVPILKVPK LTNKKKMGAT FGGILAGLIG
LLVGFFLLTK ILEILRKLDW WWISLSSPKE KMLCAFQNTG AQTSPHYVGS CPWGCPGFLW
TYLRLFIIFL LLLLVAAGLL FLTENKSTIF EKLQWESVSA LSSSIYSLLP SEPKSLVALT
FGLFLIWTTS SSVTQVLVTL TQLATLSALF FKNSG
