HBSAG_DHBVQ
ID HBSAG_DHBVQ Reviewed; 330 AA.
AC Q66405; Q66404; Q89748;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 74.
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 Duck hepatitis B virus (isolate Shanghai/DHBVQCA34) (DHBV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Avihepadnavirus.
OX NCBI_TaxID=644639;
OH NCBI_TaxID=8835; Anas (ducks).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ISOFORM S.
RA Tong S., Mattes F., Blum H.E., Fernholz D., Schneider R., Will H.;
RT "Complete nucleotide sequence of a chinese Hepatitis B virus.";
RL Submitted (JUN-1991) 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 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=Q66405-1; Sequence=Displayed;
CC Name=S; Synonyms=Small envelope protein, SHB, S-HBsAg;
CC IsoId=Q66405-2; Sequence=VSP_039691;
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 ---------------------------------------------------------------------------
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; X60213; CAA42770.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X60213; CAA42771.1; -; Genomic_DNA.
DR EMBL; X60213; CAA42772.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_039823.1; NC_001344.1.
DR RefSeq; NP_039824.1; NC_001344.1.
DR RefSeq; NP_039826.1; NC_001344.1.
DR GeneID; 2546411; -.
DR GeneID; 2546412; -.
DR GeneID; 2546415; -.
DR KEGG; vg:2546411; -.
DR KEGG; vg:2546412; -.
DR KEGG; vg:2546415; -.
DR Proteomes; UP000009098; 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; Reference proteome; 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..330
FT /note="Large envelope protein"
FT /id="PRO_0000397681"
FT CHAIN 164..?240
FT /note="Truncated S protein"
FT /id="PRO_0000397682"
FT TOPO_DOM 2..238
FT /note="Cytoplasmic; in internal conformation"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2..165
FT /note="Extracellular; in external conformation"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..238
FT /note="Cytoplasmic; in external conformation"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 2..163
FT /note="Pre-S"
FT /evidence="ECO:0000250"
FT REGION 68..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..186
FT /note="TM1"
FT /evidence="ECO:0000250"
FT REGION 239..259
FT /note="TM2"
FT /evidence="ECO:0000250"
FT REGION 293..313
FT /note="TM3"
FT /evidence="ECO:0000250"
FT COMPBIAS 91..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE ?240..?241
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 262
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..163
FT /note="Missing (in isoform S)"
FT /evidence="ECO:0000305"
FT /id="VSP_039691"
SQ SEQUENCE 330 AA; 36959 MW; 7CE142013BB8D9F4 CRC64;
MGQQPAKSMD VRRIEGGELL LNQLAGRMIP KGTVTWSGKF PTIDHLLDHV QTMEEVNTLQ
QQGAWPAGAG RRLGLTNPTP HETPQPQWTP EEDQKAREAF RRYQEERPPE TTTIAPTSPT
PWKLQPGDDP LLENKSLLET HPLYQNPEPA VPVIKTPPLK KKKMPGTFGG ILAGLIGLLV
SFFLLIKILE ILRRLDWWWI SLSSPKGKMQ CAFQDTGAQI SQHYVGSCPW GCPGFLWTYL
RLFIIFLLIL LVAAGLLYLT DNMSIILEKL QWESVSVLFS SISSLLPSDQ KSLVALMFGL
LLIWMTSSSA TQTLVTLTQL ATLSVLFYKN
