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

 HBSAG_HBVD3             Reviewed;         389 AA.
P03138;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
07-NOV-2018, entry version 98.
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 D subtype ayw (isolate
France/Tiollais/1979) (HBV-D).
Viruses; Retro-transcribing viruses; Hepadnaviridae;
Orthohepadnavirus.
NCBI_TaxID=490133;
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=399327; DOI=10.1038/281646a0;
Galibert F., Mandart E., Fitoussi F., Tiollais P., Charnay P.;
"Nucleotide sequence of the hepatitis B virus genome (subtype ayw)
cloned in E. coli.";
Nature 281:646-650(1979).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Latvia;
PubMed=3996597; DOI=10.1016/0014-5793(85)80771-7;
Bichko V., Pushko P., Dreilina D., Pumpen P., Gren E.Y.;
"Subtype ayw variant of hepatitis B virus. DNA primary structure
analysis.";
FEBS Lett. 185:208-212(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Latvia;
PubMed=6373205;
Kozlovskaia T.M., Pumpen P.P., Borisova G.P., Dishler A.V.,
Bychko V.V.;
"Synthesis of the full amino acid sequence of the surface antigen of
the hepatitis B virus in Escherichia coli.";
Dokl. Akad. Nauk SSSR 274:1250-1253(1984).
[4]
MYRISTOYLATION AT GLY-2.
PubMed=3573147;
Persing D.H., Varmus H.E., Ganem D.;
"The preS1 protein of hepatitis B virus is acylated at its amino
terminus with myristic acid.";
J. Virol. 61:1672-1677(1987).
[5]
TRANSMEMBRANE TOPOLOGY.
PubMed=7835336;
Prange R., Streeck R.E.;
"Novel transmembrane topology of the hepatitis B virus envelope
proteins.";
EMBO J. 14:247-256(1995).
[6]
MUTAGENESIS OF GLY-2.
PubMed=7491754; DOI=10.1006/viro.1995.0002;
Gripon P., Le Seyec J., Rumin S., Guguen-Guillouzo C.;
"Myristylation of the hepatitis B virus large surface protein is
essential for viral infectivity.";
Virology 213:292-299(1995).
[7]
FUNCTION.
PubMed=9420286;
Werr M., Prange R.;
"Role for calnexin and N-linked glycosylation in the assembly and
secretion of hepatitis B virus middle envelope protein particles.";
J. Virol. 72:778-782(1998).
[8]
GLYCOSYLATION (ISOFORM M), AND ACETYLATION AT MET-1 (ISOFORM M).
STRAIN=Isolate clinical;
PubMed=10207016; DOI=10.1074/jbc.274.17.11945;
Schmitt S., Glebe D., Alving K., Tolle T.K., Linder M., Geyer H.,
Linder D., Peter-Katalinic J., Gerlich W.H., Geyer R.;
"Analysis of the pre-S2 N- and O-linked glycans of the M surface
protein from human hepatitis B virus.";
J. Biol. Chem. 274:11945-11957(1999).
[9]
GLYCOSYLATION AT THR-37 (ISOFORM M).
PubMed=15218190; DOI=10.1099/vir.0.79932-0;
Schmitt S., Glebe D., Tolle T.K., Lochnit G., Linder D., Geyer R.,
Gerlich W.H.;
"Structure of pre-S2 N- and O-linked glycans in surface proteins from
different genotypes of hepatitis B virus.";
J. Gen. Virol. 85:2045-2053(2004).
[10]
FUNCTION.
PubMed=17020942; DOI=10.1128/JVI.00621-06;
Blanchet M., Sureau C.;
"Analysis of the cytosolic domains of the hepatitis B virus envelope
proteins for their function in viral particle assembly and
infectivity.";
J. Virol. 80:11935-11945(2006).
[11]
MUTAGENESIS OF LEU-11; GLY-12 AND 13-PHE-PHE-14.
PubMed=16557545; DOI=10.1002/hep.21112;
Engelke M., Mills K., Seitz S., Simon P., Gripon P., Schnolzer M.,
Urban S.;
"Characterization of a hepatitis B and hepatitis delta virus receptor
binding site.";
Hepatology 43:750-760(2006).
[12]
MUTAGENESIS OF 11-LEU--PRO-15; 16-ASP--ASP-20; 21-PRO--ALA-25;
26-ASN--PRO-30; 31-ASP--ASN-35; 36-PRO--THR-40; 41-TRP--ASN-45;
46-LYS--GLY-50; 51-ALA--GLY-55; 56-PHE--HIS-60; 61-GLY--GLY-65;
66-TRP--ALA-70; 71-GLN--GLN-75; 76-THR--ASN-80; 81-PRO--SER-85;
86-THR--SER-90; 91-GLY--THR-95; 96-PRO--PRO-100; 101-LEU--HIS-105 AND
106-PRO--GLN-110.
PubMed=17376925; DOI=10.1128/JVI.00096-07;
Blanchet M., Sureau C.;
"Infectivity determinants of the hepatitis B virus pre-S domain are
confined to the N-terminal 75 amino acid residues.";
J. Virol. 81:5841-5849(2007).
[13]
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).
[14]
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).
[15]
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).
[16]
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=P03138-1; Sequence=Displayed;
Name=M; Synonyms=Middle envelope protein, MHB, M-HBsAg;
IsoId=P03138-2; Sequence=VSP_031405;
Note=Contains a N-acetylmethionine at position 1. Contains a
O-linked (GalNAc...) threonine at position 37.
{ECO:0000269|PubMed:10207016, ECO:0000269|PubMed:15218190};
Name=S; Synonyms=Small envelope protein, SHB, S-HBsAg;
IsoId=P03138-3; Sequence=VSP_031404;
-!- 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:0000255|HAMAP-Rule:MF_04075, ECO:0000269|PubMed:10207016,
ECO:0000269|PubMed:15218190}.
-!- 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=AAA45496.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAA26324.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; V01460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X02496; CAA26324.1; ALT_INIT; Genomic_DNA.
EMBL; M12393; AAA45496.1; ALT_INIT; Genomic_DNA.
PIR; A03703; SAVLAH.
SMR; P03138; -.
ELM; P03138; -.
OrthoDB; VOG090000AH; -.
EvolutionaryTrace; P03138; -.
Proteomes; UP000007930; 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;
Reference proteome; 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 2 389 Large envelope protein.
{ECO:0000255|HAMAP-Rule:MF_04075}.
/FTId=PRO_0000038107.
TOPO_DOM 2 242 Intravirion; in internal conformation.
{ECO:0000255|HAMAP-Rule:MF_04075}.
TOPO_DOM 2 170 Virion surface; in external conformation.
{ECO:0000255|HAMAP-Rule:MF_04075}.
TRANSMEM 171 191 Helical; Name=TM1; Note=In external
conformation. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TOPO_DOM 192 242 Intravirion; in external conformation.
{ECO:0000255|HAMAP-Rule:MF_04075}.
TRANSMEM 243 263 Helical; Name=TM2. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TOPO_DOM 264 337 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TRANSMEM 338 358 Helical. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TOPO_DOM 359 364 Intravirion. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TRANSMEM 365 387 Helical; Name=TM3. {ECO:0000255|HAMAP-
Rule:MF_04075}.
TOPO_DOM 388 389 Virion surface. {ECO:0000255|HAMAP-
Rule:MF_04075}.
REGION 2 163 Pre-S. {ECO:0000255|HAMAP-Rule:MF_04075}.
REGION 2 108 Pre-S1. {ECO:0000255|HAMAP-
Rule:MF_04075}.
REGION 109 163 Pre-S2. {ECO:0000255|HAMAP-
Rule:MF_04075}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000255|HAMAP-Rule:MF_04075}.
CARBOHYD 309 309 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255|HAMAP-Rule:MF_04075}.
VAR_SEQ 1 163 Missing (in isoform S). {ECO:0000305}.
/FTId=VSP_031404.
VAR_SEQ 1 108 Missing (in isoform M). {ECO:0000305}.
/FTId=VSP_031405.
VARIANT 75 75 Q -> E (in strain: Latvia).
VARIANT 147 147 A -> S (in strain: Latvia).
VARIANT 150 150 L -> I (in strain: Latvia).
VARIANT 288 290 MTT -> TTP (in strain: Latvia).
MUTAGEN 2 2 G->A: Complete loss of myristoylation.
Complete loss of infectivity.
{ECO:0000269|PubMed:7491754}.
MUTAGEN 11 15 LGFFP->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 11 11 L->R: Complete loss of infectivity.
{ECO:0000269|PubMed:16557545}.
MUTAGEN 12 12 G->E: Complete loss of infectivity.
{ECO:0000269|PubMed:16557545}.
MUTAGEN 13 14 FF->SS: Complete loss of infectivity.
{ECO:0000269|PubMed:16557545}.
MUTAGEN 13 13 F->S: Complete loss of infectivity.
MUTAGEN 16 20 DHQLD->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 21 25 PAFRA->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 26 30 NTANP->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 31 35 DWDFN->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 36 40 PNKDT->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 41 45 WPDAN->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 47 50 VGAG->L: Complete loss of infectivity.
MUTAGEN 51 55 AFGLG->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 56 60 FTPPH->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 61 65 GGLLG->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 66 70 WSPQA->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 71 75 QGILQ->KL: Complete loss of infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 76 80 TLPAN->KL: No effect on infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 81 85 PPPAS->KL: No effect on infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 86 90 TNRQS->KL: No effect on infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 91 95 GRQPT->KL: No effect on infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 96 100 PLSPP->KL: No effect on infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 101 105 LRNTH->KL: No effect on infectivity.
{ECO:0000269|PubMed:17376925}.
MUTAGEN 106 110 PQAMQ->KL: No effect on infectivity.
{ECO:0000269|PubMed:17376925}.
SEQUENCE 389 AA; 42766 MW; 6DC9E682DA694F63 CRC64;
MGQNLSTSNP LGFFPDHQLD PAFRANTANP DWDFNPNKDT WPDANKVGAG AFGLGFTPPH
GGLLGWSPQA QGILQTLPAN PPPASTNRQS GRQPTPLSPP LRNTHPQAMQ WNSTTFHQTL
QDPRVRGLYF PAGGSSSGTV NPVLTTASPL SSIFSRIGDP ALNMENITSG FLGPLLVLQA
GFFLLTRILT IPQSLDSWWT SLNFLGGTTV CLGQNSQSPT SNHSPTSCPP TCPGYRWMCL
RRFIIFLFIL LLCLIFLLVL LDYQGMLPVC PLIPGSSTTS TGPCRTCMTT AQGTSMYPSC
CCTKPSDGNC TCIPIPSSWA FGKFLWEWAS ARFSWLSLLV PFVQWFVGLS PTVWLSVIWM
MWYWGPSLYS ILSPFLPLLP IFFCLWVYI


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