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

 HBSAG_HBVA3             Reviewed;         400 AA.
P03141;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
10-OCT-2018, entry version 75.
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 A2 subtype adw2 (strain Rutter 1979)
(HBV-A).
Viruses; Retro-transcribing viruses; Hepadnaviridae;
Orthohepadnavirus.
NCBI_TaxID=480116;
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Valenzuela P., Quiroga M., Zaldivar J., Gray P., Rutter W.J.;
"The nucleotide sequence of the hepatitis B viral genome and the
identification of the major viral genes.";
(In) Field B.N., Jaenisch R., Fox C.F. (eds.);
Animal virus genetics, pp.57-70, Academic Press, New York (1980).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 175-400.
PubMed=471053; DOI=10.1038/280815a0;
Valenzuela P., Gray P., Quiroga M., Zaldivar J., Goodman H.M.,
Rutter W.J.;
"Nucleotide sequence of the gene coding for the major protein of
hepatitis B virus surface antigen.";
Nature 280:815-819(1979).
[3]
ISOFORM S RECOMBINANT VACCINE.
PubMed=6150233; DOI=10.1016/S0140-6736(84)92740-5;
Jilg W., Lorbeer B., Schmidt M., Wilske B., Zoulek G., Deinhardt F.;
"Clinical evaluation of a recombinant hepatitis B vaccine.";
Lancet 2:1174-1175(1984).
[4]
CHARACTERIZATION.
STRAIN=Isolate clinical;
PubMed=6492255;
Heermann K.H., Goldmann U., Schwartz W., Seyffarth T., Baumgarten H.,
Gerlich W.H.;
"Large surface proteins of hepatitis B virus containing the pre-s
sequence.";
J. Virol. 52:396-402(1984).
[5]
FUNCTION.
PubMed=2041095;
Bruss V., Ganem D.;
"Mutational analysis of hepatitis B surface antigen particle assembly
and secretion.";
J. Virol. 65:3813-3820(1991).
[6]
TRANSMEMBRANE TOPOLOGY.
PubMed=8194518;
Bruss V., Lu X., Thomssen R., Gerlich W.H.;
"Post-translational alterations in transmembrane topology of the
hepatitis B virus large envelope protein.";
EMBO J. 13:2273-2279(1994).
[7]
FUNCTION OF ISOFORM M.
PubMed=9050863; DOI=10.1073/pnas.94.5.1822;
Mehta A., Lu X., Block T.M., Blumberg B.S., Dwek R.A.;
"Hepatitis B virus (HBV) envelope glycoproteins vary drastically in
their sensitivity to glycan processing: evidence that alteration of a
single N-linked glycosylation site can regulate HBV secretion.";
Proc. Natl. Acad. Sci. U.S.A. 94:1822-1827(1997).
[8]
FUNCTION OF GLYCOSYLATION.
PubMed=9122203; DOI=10.1073/pnas.94.6.2380;
Lu X., Mehta A., Dadmarz M., Dwek R., Blumberg B.S., Block T.M.;
"Aberrant trafficking of hepatitis B virus glycoproteins in cells in
which N-glycan processing is inhibited.";
Proc. Natl. Acad. Sci. U.S.A. 94:2380-2385(1997).
[9]
MYRISTOYLATION AT GLY-2.
PubMed=11350599; DOI=10.1034/j.1399-3011.2001.00848.x;
De Falco S., Ruvo M., Verdoliva A., Scarallo A., Raimondo D.,
Raucci A., Fassina G.;
"N-terminal myristylation of HBV preS1 domain enhances receptor
recognition.";
J. Pept. Res. 57:390-400(2001).
[10]
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).
[11]
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).
[12]
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).
[13]
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=P03141-1; Sequence=Displayed;
Name=M; Synonyms=Middle envelope protein, MHB, M-HBsAg;
IsoId=P03141-2; Sequence=VSP_030415;
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=P03141-3; Sequence=VSP_030414;
-!- 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,
ECO:0000269|PubMed:11350599}.
-!- 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}.
-!- WEB RESOURCE: Name=HepSEQ; Note=Hepatitis virus B database;
URL="http://www.hpa-bioinformatics.org.uk/HepSEQ/main.php";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X02763; CAA26539.1; -; Genomic_DNA.
EMBL; J02205; AAA45524.1; -; Genomic_RNA.
PIR; A03706; SAVLVD.
OrthoDB; VOG090000AH; -.
Proteomes; UP000008766; 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 2 400 Large envelope protein.
{ECO:0000255|HAMAP-Rule:MF_04075}.
/FTId=PRO_0000038087.
TOPO_DOM 2 253 Intravirion; in internal conformation.
{ECO:0000255|HAMAP-Rule:MF_04075}.
TOPO_DOM 2 181 Virion surface; in external conformation.
{ECO:0000255|HAMAP-Rule:MF_04075}.
TRANSMEM 182 202 Helical; Name=TM1; Note=In external
conformation. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TOPO_DOM 203 253 Intravirion; in external conformation.
{ECO:0000255|HAMAP-Rule:MF_04075}.
TRANSMEM 254 274 Helical; Name=TM2. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TOPO_DOM 275 348 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TRANSMEM 349 369 Helical. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TOPO_DOM 370 375 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TRANSMEM 376 398 Helical; Name=TM3. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TOPO_DOM 399 400 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04075}.
REGION 2 174 Pre-S. {ECO:0000255|HAMAP-Rule:MF_04075}.
REGION 2 119 Pre-S1. {ECO:0000255|HAMAP-
Rule:MF_04075}.
REGION 120 174 Pre-S2. {ECO:0000255|HAMAP-
Rule:MF_04075}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000255|HAMAP-Rule:MF_04075}.
CARBOHYD 320 320 N-linked (GlcNAc...) asparagine; by host;
partial. {ECO:0000255|HAMAP-
Rule:MF_04075}.
VAR_SEQ 1 174 Missing (in isoform S). {ECO:0000305}.
/FTId=VSP_030414.
VAR_SEQ 1 119 Missing (in isoform M). {ECO:0000305}.
/FTId=VSP_030415.
SEQUENCE 400 AA; 43705 MW; 57356B6293872BC5 CRC64;
MGGWSSKPRK GMGTNLSVPN PLGFFPDHQL DPAFGANSNN PDWDFNPVKD DWPAANQVGV
GAFGPRLTPP HGGILGWSPQ AQGILTTVST IPPPASTNRQ SGRQPTPISP PLRDSHPQAM
QWNSTAFHQT LQDPRVRGLY LPAGGSSSGT VNPAPNIASH ISSISARTGD PVTNMENITS
GFLGPLLVLQ AGFFLLTRIL TIPQSLDSWW TSLNFLGGSP VCLGQNSQSP TSNHSPTSCP
PICPGYRWMC LRRFIIFLFI LLLCLIFLLV LLDYQGMLPV CPLIPGSTTT STGPCKTCTT
PAQGNSMFPS CCCTKPTDGN CTCIPIPSSW AFAKYLWEWA SVRFSWLSLL VPFVQWFVGL
SPTVWLSAIW MMWYWGPSLY SIVSPFIPLL PIFFCLWVYI


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