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

 HBSAG_HBVE1             Reviewed;         399 AA.
Q69603;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 2.
16-JAN-2019, entry version 71.
RecName: Full=Large envelope protein {ECO:0000255|HAMAP-Rule:MF_04075};
AltName: Full=L glycoprotein {ECO:0000255|HAMAP-Rule:MF_04075};
AltName: Full=L-HBsAg {ECO:0000255|HAMAP-Rule:MF_04075};
Short=LHB {ECO:0000255|HAMAP-Rule:MF_04075};
AltName: Full=Large S protein {ECO:0000255|HAMAP-Rule:MF_04075};
AltName: Full=Large surface protein {ECO:0000255|HAMAP-Rule:MF_04075};
AltName: Full=Major surface antigen {ECO:0000255|HAMAP-Rule:MF_04075};
Name=S {ECO:0000255|HAMAP-Rule:MF_04075};
Hepatitis B virus genotype E subtype ayw4 (isolate Kou) (HBV-E).
Viruses; Retro-transcribing viruses; Hepadnaviridae;
Orthohepadnavirus.
NCBI_TaxID=489495;
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8291231; DOI=10.1006/viro.1994.1060;
Norder H., Courouce A.M., Magnius L.O.;
"Complete genomes, phylogenetic relatedness, and structural proteins
of six strains of the hepatitis B virus, four of which represent two
new genotypes.";
Virology 198:489-503(1994).
[2]
REVIEW.
PubMed=8957666;
Bruss V., Gerhardt E., Vieluf K., Wunderlich G.;
"Functions of the large hepatitis B virus surface protein in viral
particle morphogenesis.";
Intervirology 39:23-31(1996).
[3]
REVIEW.
PubMed=9498079;
Block T.M., Lu X., Mehta A., Park J., Blumberg B.S., Dwek R.;
"Role of glycan processing in hepatitis B virus envelope protein
trafficking.";
Adv. Exp. Med. Biol. 435:207-216(1998).
[4]
REVIEW.
PubMed=15567498; DOI=10.1016/j.virusres.2004.08.016;
Bruss V.;
"Envelopment of the hepatitis B virus nucleocapsid.";
Virus Res. 106:199-209(2004).
[5]
REVIEW.
PubMed=16863502; DOI=10.1111/j.1349-7006.2006.00235.x;
Wang H.C., Huang W., Lai M.D., Su I.J.;
"Hepatitis B virus pre-S mutants, endoplasmic reticulum stress and
hepatocarcinogenesis.";
Cancer Sci. 97:683-688(2006).
-!- 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. This attachment induces virion
internalization predominantly through caveolin-mediated
endocytosis. The large envelope protein also assures fusion
between virion membrane and endosomal membrane. In its internal
conformation the protein plays a role in virion morphogenesis and
mediates the contact with the nucleocapsid like a matrix protein.
{ECO:0000255|HAMAP-Rule:MF_04075}.
-!- FUNCTION: The middle envelope protein plays an important role in
the budding of the virion. It is involved in the induction of
budding in a nucleocapsid independent way. In this process the
majority of envelope proteins bud to form subviral lipoprotein
particles of 22 nm of diameter that do not contain a nucleocapsid.
{ECO:0000255|HAMAP-Rule:MF_04075}.
-!- SUBUNIT: Li-HBsAg interacts with capsid protein and with HDV Large
delta antigen. Isoform M associates with host chaperone CANX
through its pre-S2 N glycan. This association may be essential for
M proper secretion. {ECO:0000255|HAMAP-Rule:MF_04075}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
Rule:MF_04075}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=3;
Name=L; Synonyms=Large envelope protein, LHB, L-HBsAg;
IsoId=Q69603-1; Sequence=Displayed;
Name=M; Synonyms=Middle envelope protein, MHB, M-HBsAg;
IsoId=Q69603-2; Sequence=VSP_031414;
Note=Contains a N-acetylmethionine at position 1. Contains a
N-linked (GlcNAc...) asparagine at position 4.
{ECO:0000250|UniProtKB:P03138};
Name=S; Synonyms=Small envelope protein, SHB, S-HBsAg;
IsoId=Q69603-3; Sequence=VSP_031413;
-!- 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. For isoform M in contrast, the
pre-S2 region is translocated cotranslationally to the endoplasmic
reticulum lumen and is N-glycosylated. {ECO:0000255|HAMAP-
Rule:MF_04075}.
-!- PTM: Isoform M is N-terminally acetylated by host at a ratio of
90%, and N-glycosylated by host at the pre-S2 region.
{ECO:0000250|UniProtKB:P03138, ECO:0000255|HAMAP-Rule:MF_04075}.
-!- PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04075}.
-!- BIOTECHNOLOGY: Systematic vaccination of individuals at risk of
exposure to the virus has been the main method of controlling the
morbidity and mortality associated with hepatitis B. The first
hepatitis B vaccine was manufactured by the purification and
inactivation of HBsAg obtained from the plasma of chronic
hepatitis B virus carriers. The vaccine is now produced by
recombinant DNA techniques and expression of the S isoform in
yeast cells. The pre-S region do not seem to induce strong enough
antigenic response.
-!- SIMILARITY: Belongs to the orthohepadnavirus major surface antigen
family. {ECO:0000255|HAMAP-Rule:MF_04075}.
-!- SEQUENCE CAUTION:
Sequence=CAA53355.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X75664; CAA53355.1; ALT_INIT; Genomic_DNA.
PIR; JQ1578; JQ1578.
PIR; JQ2079; JQ2079.
PIR; JQ2087; JQ2087.
PIR; JQ2088; JQ2088.
PIR; JQ2089; JQ2089.
PIR; JQ2091; JQ2091.
PIR; JQ2092; JQ2092.
ProteinModelPortal; Q69603; -.
Proteomes; UP000008538; Genome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0075513; P:caveolin-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW.
GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
HAMAP; MF_04075; HBV_HBSAG; 1.
InterPro; IPR000349; HBV_HBSAG.
Pfam; PF00695; vMSA; 1.
1: Evidence at protein level;
Acetylation; Alternative initiation; Alternative splicing;
Caveolin-mediated endocytosis of virus by host; Complete proteome;
Fusion of virus membrane with host endosomal membrane;
Fusion of virus membrane with host membrane; Glycoprotein;
Host-virus interaction; Lipoprotein; Membrane; Myristate;
Transmembrane; Transmembrane helix; Viral attachment to host cell;
Viral penetration into host cytoplasm; Virion;
Virus endocytosis by host; Virus entry into host cell.
INIT_MET 1 1 Removed; by host. {ECO:0000255|HAMAP-
Rule:MF_04075}.
CHAIN 2 399 Large envelope protein.
{ECO:0000255|HAMAP-Rule:MF_04075}.
/FTId=PRO_0000319089.
TOPO_DOM 2 252 Intravirion; in internal conformation.
{ECO:0000255|HAMAP-Rule:MF_04075}.
TOPO_DOM 2 180 Virion surface; in external conformation.
{ECO:0000255|HAMAP-Rule:MF_04075}.
TRANSMEM 181 201 Helical; Name=TM1; Note=In external
conformation. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TOPO_DOM 202 252 Intravirion; in external conformation.
{ECO:0000255|HAMAP-Rule:MF_04075}.
TRANSMEM 253 273 Helical; Name=TM2. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TOPO_DOM 274 347 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TRANSMEM 348 368 Helical. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TOPO_DOM 369 374 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TRANSMEM 375 397 Helical; Name=TM3. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TOPO_DOM 398 399 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04075}.
REGION 2 173 Pre-S. {ECO:0000255|HAMAP-Rule:MF_04075}.
REGION 2 118 Pre-S1. {ECO:0000255|HAMAP-
Rule:MF_04075}.
REGION 119 173 Pre-S2. {ECO:0000255|HAMAP-
Rule:MF_04075}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000255|HAMAP-Rule:MF_04075}.
CARBOHYD 319 319 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04075}.
VAR_SEQ 1 173 Missing (in isoform S). {ECO:0000305}.
/FTId=VSP_031413.
VAR_SEQ 1 118 Missing (in isoform M). {ECO:0000305}.
/FTId=VSP_031414.
SEQUENCE 399 AA; 43984 MW; 79B52A0B9A55DB73 CRC64;
MGLSWTVPLE WGKNISTTNP LGFFPDHQLD PAFRANTRNP DWDHNPNKDH WTEANKVGVG
AFGPGFTPPH GGLLGWSPQA QGMLKTLPAD PPPASTNRQS GRQPTPITPP LRDTHPQAMQ
WNSTTFHQAL QDPRVRGLYF PAGGSSSGTV NPVPTTASLI SSIFSRIGDP APNMESITSG
FLGPLLVLQA GFFLLTKILT IPQSLDSWWT SLNFLGGAPV CLGQNSQSPT SNHSPTSCPP
ICPGYRWMCL RRFIIFLFIL LLCLIFLLVL LDYQGMLPVC PLIPGSSTTS TGPCRTCMTL
AQGTSMFPSC CCSKPSDGNC TCIPIPSSWA FGKFLWEWAS ARFSWLSLLV PFVQWFAGLS
PTVWLSVIWM MWYWGPSLYD ILSPFIPLLP IFFCLWVYI


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