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

 Q67886_HBV              Unreviewed;       382 AA.
Q67886;
01-NOV-1996, integrated into UniProtKB/TrEMBL.
01-NOV-1996, sequence version 1.
28-MAR-2018, entry version 78.
RecName: Full=Large envelope protein {ECO:0000256|HAMAP-Rule:MF_04075};
AltName: Full=L glycoprotein {ECO:0000256|HAMAP-Rule:MF_04075};
AltName: Full=L-HBsAg {ECO:0000256|HAMAP-Rule:MF_04075};
Short=LHB {ECO:0000256|HAMAP-Rule:MF_04075};
AltName: Full=Large S protein {ECO:0000256|HAMAP-Rule:MF_04075};
AltName: Full=Large surface protein {ECO:0000256|HAMAP-Rule:MF_04075};
AltName: Full=Major surface antigen {ECO:0000256|HAMAP-Rule:MF_04075};
Name=PreS1 {ECO:0000313|EMBL:CAA42467.1};
Synonyms=PreS2 {ECO:0000313|EMBL:CAA42467.1},
S {ECO:0000256|HAMAP-Rule:MF_04075},
S open reading frame {ECO:0000313|EMBL:CAA42467.1};
Hepatitis B virus (HBV).
Viruses; Retro-transcribing viruses; Hepadnaviridae;
Orthohepadnavirus.
NCBI_TaxID=10407 {ECO:0000313|EMBL:CAA42467.1, ECO:0000313|Proteomes:UP000122765};
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
[1] {ECO:0000313|EMBL:CAA42467.1, ECO:0000313|Proteomes:UP000122765}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HBsAg subtype ayw {ECO:0000313|EMBL:CAA42467.1};
TISSUE=HBsAg positive human serum {ECO:0000313|EMBL:CAA42467.1};
PubMed=1923778; DOI=10.1093/nar/19.18.5078;
Lai M.E., Melis A., Mazzoleni A.P., Uccheddu P., Balestrieri A.;
"Sequence analysis of hepatitis B virus genome of a new mutant of ayw
subtype isolated in Sardinia.";
Nucleic Acids Res. 19:5078-5078(1991).
-!- 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:0000256|HAMAP-Rule:MF_04075, ECO:0000256|SAAS:SAAS00968829}.
-!- 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:0000256|HAMAP-Rule:MF_04075, ECO:0000256|SAAS:SAAS00968840}.
-!- 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:0000256|HAMAP-Rule:MF_04075,
ECO:0000256|SAAS:SAAS00968834}.
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000256|HAMAP-
Rule:MF_04075, ECO:0000256|SAAS:SAAS00968828}.
-!- 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:0000256|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:0000256|HAMAP-Rule:MF_04075}.
-!- PTM: Myristoylated. {ECO:0000256|HAMAP-Rule:MF_04075}.
-!- SIMILARITY: Belongs to the orthohepadnavirus major surface antigen
family. {ECO:0000256|HAMAP-Rule:MF_04075,
ECO:0000256|SAAS:SAAS00968839}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_04075}.
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EMBL; X59795; CAA42467.1; -; Genomic_DNA.
PIR; JQ1572; JQ1572.
PIR; JQ2063; JQ2063.
PIR; JQ2066; JQ2066.
PIR; JQ2067; JQ2067.
PIR; JQ2068; JQ2068.
PIR; JQ2069; JQ2069.
PIR; JQ2070; JQ2070.
PIR; JQ2072; JQ2072.
PIR; JQ2076; JQ2076.
PIR; JQ2077; JQ2077.
PIR; JQ2078; JQ2078.
PIR; JQ2079; JQ2079.
PIR; JQ2081; JQ2081.
PIR; JQ2083; JQ2083.
Proteomes; UP000122765; 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.
3: Inferred from homology;
Acetylation {ECO:0000256|HAMAP-Rule:MF_04075};
Caveolin-mediated endocytosis of virus by host {ECO:0000256|HAMAP-
Rule:MF_04075, ECO:0000256|SAAS:SAAS00968835};
Complete proteome {ECO:0000313|Proteomes:UP000122765};
Fusion of virus membrane with host endosomal membrane
{ECO:0000256|HAMAP-Rule:MF_04075, ECO:0000256|SAAS:SAAS00968831};
Fusion of virus membrane with host membrane {ECO:0000256|HAMAP-
Rule:MF_04075, ECO:0000256|SAAS:SAAS00968831};
Glycoprotein {ECO:0000256|HAMAP-Rule:MF_04075};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04075,
ECO:0000256|SAAS:SAAS00968842};
Lipoprotein {ECO:0000256|HAMAP-Rule:MF_04075};
Membrane {ECO:0000256|HAMAP-Rule:MF_04075,
ECO:0000256|SAAS:SAAS00968833, ECO:0000256|SAM:Phobius};
Myristate {ECO:0000256|HAMAP-Rule:MF_04075};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_04075,
ECO:0000256|SAAS:SAAS00968833, ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_04075,
ECO:0000256|SAAS:SAAS00968833, ECO:0000256|SAM:Phobius};
Viral attachment to host cell {ECO:0000256|HAMAP-Rule:MF_04075,
ECO:0000256|SAAS:SAAS00968842};
Viral penetration into host cytoplasm {ECO:0000256|HAMAP-
Rule:MF_04075, ECO:0000256|SAAS:SAAS00968831,
ECO:0000256|SAAS:SAAS00968835};
Virion {ECO:0000256|HAMAP-Rule:MF_04075,
ECO:0000256|SAAS:SAAS00968842};
Virus endocytosis by host {ECO:0000256|HAMAP-Rule:MF_04075,
ECO:0000256|SAAS:SAAS00968835};
Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04075,
ECO:0000256|SAAS:SAAS00968831, ECO:0000256|SAAS:SAAS00968835,
ECO:0000256|SAAS:SAAS00968842}.
INIT_MET 1 1 Removed; by host. {ECO:0000256|HAMAP-
Rule:MF_04075}.
TOPO_DOM 2 235 Intravirion; in internal conformation.
{ECO:0000256|HAMAP-Rule:MF_04075}.
TOPO_DOM 2 163 Virion surface; in external conformation.
{ECO:0000256|HAMAP-Rule:MF_04075}.
TRANSMEM 164 182 Helical. {ECO:0000256|SAM:Phobius}.
TOPO_DOM 185 235 Intravirion; in external conformation.
{ECO:0000256|HAMAP-Rule:MF_04075}.
TRANSMEM 236 254 Helical. {ECO:0000256|SAM:Phobius}.
TOPO_DOM 257 330 Virion surface. {ECO:0000256|HAMAP-
Rule:MF_04075}.
TRANSMEM 326 355 Helical. {ECO:0000256|SAM:Phobius}.
TOPO_DOM 352 357 Intravirion. {ECO:0000256|HAMAP-
Rule:MF_04075}.
TRANSMEM 361 381 Helical. {ECO:0000256|SAM:Phobius}.
TOPO_DOM 381 382 Virion surface. {ECO:0000256|HAMAP-
Rule:MF_04075}.
REGION 2 156 Pre-S. {ECO:0000256|HAMAP-Rule:MF_04075}.
REGION 2 108 Pre-S1. {ECO:0000256|HAMAP-
Rule:MF_04075}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000256|HAMAP-Rule:MF_04075}.
SEQUENCE 382 AA; 41858 MW; B2489CAA25A52815 CRC64;
MGQNLSTSNP LGFFPDHQLD PAFRANTANP DWDFNPNKDT WPDANKVGAG AFGLGLTPPH
GGLLGWSPQA QGILQTVPAN PPPASTNRQT GRQPTPLSPP LRDTHPQAMQ WNSTTFHQTL
QDPPAGGSSS GTVNPVPTTV SHISSIFTRI GDPALNMENI TSGFLGPLLV LQAGFFLLTR
ILTIPQSLDS WWTSLNFLGG TTVCLGQNSQ SPTSNHSPTS CPPTCPGYRW MCLRRFIIFL
FILLLCLIFL LVLLDYQGML PVCPLIPGSS TTSTGPCRTC TTPAQGNSMY PSCCCTKPSD
GNCTCIPIPS SWAFGKFLWE WASARFSWLS LLVPFVQWFV GLSPTVWLSV IWMMWYWGPS
LYSILSPFLP LLPIFFCLWA YI


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