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Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen)

 HBSAG_DHBV3             Reviewed;         328 AA.
P0C684;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 1.
16-JAN-2019, entry version 37.
RecName: Full=Large envelope protein;
AltName: Full=L glycoprotein;
AltName: Full=L-HBsAg;
Short=LHB;
AltName: Full=Large S protein;
AltName: Full=Large surface protein;
AltName: Full=Major surface antigen;
Name=S;
Duck hepatitis B virus (strain Germany/DHBV-3) (DHBV).
Viruses; Retro-transcribing viruses; Hepadnaviridae; Avihepadnavirus.
NCBI_TaxID=489542;
NCBI_TaxID=8835; Anas (ducks).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3981148; DOI=10.1002/jmv.1890150402;
Sprengel R., Kuhn C., Will H., Schaller H.;
"Comparative sequence analysis of duck and human hepatitis B virus
genomes.";
J. Med. Virol. 15:323-333(1985).
[2]
ALTERNATIVE INITIATION.
PubMed=8212596; DOI=10.1006/viro.1993.1567;
Fernholz D., Wildner G., Will H.;
"Minor envelope proteins of duck hepatitis B virus are initiated at
internal pre-S AUG codons but are not essential for infectivity.";
Virology 197:64-73(1993).
[3]
TRANSMEMBRANE TOPOLOGY.
PubMed=9371604;
Swameye I., Schaller H.;
"Dual topology of the large envelope protein of duck hepatitis B
virus: determinants preventing pre-S translocation and
glycosylation.";
J. Virol. 71:9434-9441(1997).
[4]
TOPOLOGICAL CONFORMATION.
PubMed=17045625; DOI=10.1016/j.virol.2006.09.006;
Franke C., Matschl U., Bruns M.;
"Enzymatic treatment of duck hepatitis B virus: topology of the
surface proteins for virions and noninfectious subviral particles.";
Virology 359:126-136(2007).
-!- FUNCTION: The large envelope protein exists in two topological
conformations, one which is termed 'external' or Le-HBsAg and the
other 'internal' or Li-HBsAg. In its external conformation the
protein attaches the virus to cell receptors and thereby
initiating infection. This interaction determines the species
specificity and liver tropism. The large envelope protein probably
also assumes fusion between virion and host membranes. In its
internal conformation the protein plays a role in virion
morphogenesis and mediates the contact with the nucleocapsid like
a matrix protein (By similarity). {ECO:0000250}.
-!- FUNCTION: Truncated S protein may be involved in translocation of
pre-S domain through the virion membrane. {ECO:0000250}.
-!- SUBUNIT: Large internal envelope protein interacts with capsid
protein. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Virion membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=L; Synonyms=Large envelope protein, LHB, L-HBsAg;
IsoId=P0C684-1; Sequence=Displayed;
Name=S; Synonyms=Small envelope protein, SHB, S-HBsAg;
IsoId=P0C684-2; Sequence=VSP_031897;
-!- DOMAIN: The large envelope protein is synthesized with the pre-S
region at the cytosolic side of the endoplasmic reticulum and,
hence will be within the virion after budding. Therefore the pre-S
region is not N-glycosylated. Later a post-translational
translocation of N-terminal pre-S and TM1 domains occur in about
50% of proteins at the virion surface. These molecules change
their topology by an unknown mechanism, resulting in exposure of
pre-S region at virion surface.
-!- PTM: Myristoylation contributes importantly to DHBV infectivity.
It is most likely required for an early step of the life cycle
involving the entry or uncoating of virus particles.
-!- PTM: Phosphorylated on pre-S domain for about 50% of L proteins,
the L chains with internal pre-S region (Li-HBsAg).
-!- SIMILARITY: Belongs to the avihepadnavirus major surface antigen
family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; DQ195079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PRIDE; P0C684; -.
Proteomes; UP000007204; Genome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0039663; P:membrane fusion involved in viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR000349; HBV_HBSAG.
Pfam; PF00695; vMSA; 2.
1: Evidence at protein level;
Alternative initiation; Complete proteome;
Fusion of virus membrane with host membrane; Glycoprotein;
Host-virus interaction; Lipoprotein; Membrane; Myristate;
Phosphoprotein; Transmembrane; Transmembrane helix;
Viral attachment to host cell; Viral penetration into host cytoplasm;
Virion; Virus entry into host cell.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 328 Large envelope protein.
/FTId=PRO_0000322376.
TOPO_DOM 2 236 Intravirion; in internal conformation.
{ECO:0000255}.
TOPO_DOM 2 163 Virion surface; in external conformation.
{ECO:0000255}.
TRANSMEM 164 184 Helical; Name=TM1; Note=In external
conformation. {ECO:0000255}.
TOPO_DOM 185 236 Intravirion; in external conformation.
{ECO:0000255}.
TRANSMEM 237 257 Helical; Name=TM2. {ECO:0000255}.
TOPO_DOM 258 282 Virion surface. {ECO:0000255}.
TRANSMEM 283 303 Helical; Name=TM3. {ECO:0000255}.
TOPO_DOM 304 328 Intravirion. {ECO:0000255}.
REGION 2 161 Pre-S. {ECO:0000250}.
SITE ?238 ?239 Cleavage; by host. {ECO:0000255}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
CARBOHYD 260 260 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
VAR_SEQ 1 161 Missing (in isoform S). {ECO:0000305}.
/FTId=VSP_031897.
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


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Bibliography :