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Large envelope protein

 Q9IR29_HBV              Unreviewed;       388 AA.
Q9IR29;
01-OCT-2000, integrated into UniProtKB/TrEMBL.
01-OCT-2000, sequence version 1.
28-MAR-2018, entry version 68.
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=env {ECO:0000313|EMBL:BAA98022.1};
Synonyms=S {ECO:0000256|HAMAP-Rule:MF_04075};
Hepatitis B virus (HBV).
Viruses; Retro-transcribing viruses; Hepadnaviridae;
Orthohepadnavirus.
NCBI_TaxID=10407 {ECO:0000313|EMBL:BAA98022.1};
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
[1] {ECO:0000313|EMBL:BAA98022.1}
NUCLEOTIDE SEQUENCE.
PubMed=10856755; DOI=10.1016/S0166-0934(00)00153-1;
Usuda S., Okamoto H., Tanaka T., Kidd-Ljunggren K., Holland P.V.,
Miyakawa Y., Mayumi M.;
"Differentiation of hepatitis B virus genotypes D and E by ELISA using
monoclonal antibodies to epitopes on the preS2-region product.";
J. Virol. Methods 87:81-89(2000).
-!- 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; AB033272; BAA98022.1; -; Genomic_DNA.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
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};
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 envelope protein {ECO:0000313|EMBL:BAA98022.1};
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, ECO:0000313|EMBL:BAA98022.1};
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 2 252 Intravirion; in internal conformation.
{ECO:0000256|HAMAP-Rule:MF_04075}.
TOPO_DOM 2 180 Virion surface; in external conformation.
{ECO:0000256|HAMAP-Rule:MF_04075}.
TOPO_DOM 202 252 Intravirion; in external conformation.
{ECO:0000256|HAMAP-Rule:MF_04075}.
TRANSMEM 253 271 Helical. {ECO:0000256|SAM:Phobius}.
TOPO_DOM 274 347 Virion surface. {ECO:0000256|HAMAP-
Rule:MF_04075}.
TRANSMEM 352 374 Helical. {ECO:0000256|SAM:Phobius}.
TOPO_DOM 369 374 Intravirion. {ECO:0000256|HAMAP-
Rule:MF_04075}.
REGION 2 173 Pre-S. {ECO:0000256|HAMAP-Rule:MF_04075}.
REGION 2 118 Pre-S1. {ECO:0000256|HAMAP-
Rule:MF_04075}.
REGION 119 173 Pre-S2. {ECO:0000256|HAMAP-
Rule:MF_04075}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000256|HAMAP-Rule:MF_04075}.
SEQUENCE 388 AA; 42650 MW; 834095CAB40338EB CRC64;
MGLSWTVPLE WGKNHSTTNP LGFFPDHQLD PAFRANTRNP DWDHNPNKDH WTEANKVGVG
AFGPGFTPPH GGLLGWSPQA QGMLKTLPAD PPPASTNRQL GRQPTPITPP LRDTHPQAMQ
WNSTTFHQAL QDPRVRGLYF PAGGSSSGTV NPVPTTASLI SSIFSRIGDP APNMESITSG
FLGPLLVLQA GFFLLTKILT IPQSLDSWWT SLNFLGGAPV CLGQNSQSPT SNHSPTSCPP
ICPGYRWMCL RRFIIFLFIL LLCLIFLLVL LDYQGMLPVC PLIPGSSTTS TGPCRTCTTL
AQGTSMFPSC CCSKPSDGNC TCIPIPSSWA FGKFLWEWAS ARFSWLSLLV PFVQWFAGLS
PTVWLSVIWM MWYWGPSLYN ILSPFIPR


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