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

 A0A144HXU4_HBV          Unreviewed;       400 AA.
A0A144HXU4;
08-JUN-2016, integrated into UniProtKB/TrEMBL.
08-JUN-2016, sequence version 1.
28-MAR-2018, entry version 11.
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=S {ECO:0000256|HAMAP-Rule:MF_04075, ECO:0000313|EMBL:AMS75085.1};
Hepatitis B virus (HBV).
Viruses; Retro-transcribing viruses; Hepadnaviridae;
Orthohepadnavirus.
NCBI_TaxID=10407 {ECO:0000313|EMBL:AMS75085.1, ECO:0000313|Proteomes:UP000159686};
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
[1] {ECO:0000313|EMBL:AMS75085.1, ECO:0000313|Proteomes:UP000159686}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IND-DIB-RMRC-2052 {ECO:0000313|EMBL:AMS75085.1};
Borkakoty B.;
"Circulation of genotype-I hepatitis B virus in Dibang Valley,
Arunachal Pradesh.";
Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
-!- 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}.
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EMBL; KU950741; AMS75085.1; -; Genomic_DNA.
Proteomes; UP000159686; 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:UP000159686};
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 2 253 Intravirion; in internal conformation.
{ECO:0000256|HAMAP-Rule:MF_04075}.
TOPO_DOM 2 181 Virion surface; in external conformation.
{ECO:0000256|HAMAP-Rule:MF_04075}.
TOPO_DOM 203 253 Intravirion; in external conformation.
{ECO:0000256|HAMAP-Rule:MF_04075}.
TRANSMEM 254 272 Helical. {ECO:0000256|SAM:Phobius}.
TOPO_DOM 275 348 Virion surface. {ECO:0000256|HAMAP-
Rule:MF_04075}.
TRANSMEM 349 373 Helical. {ECO:0000256|SAM:Phobius}.
TOPO_DOM 370 375 Intravirion. {ECO:0000256|HAMAP-
Rule:MF_04075}.
TRANSMEM 379 399 Helical. {ECO:0000256|SAM:Phobius}.
TOPO_DOM 399 400 Virion surface. {ECO:0000256|HAMAP-
Rule:MF_04075}.
REGION 2 174 Pre-S. {ECO:0000256|HAMAP-Rule:MF_04075}.
REGION 2 119 Pre-S1. {ECO:0000256|HAMAP-
Rule:MF_04075}.
REGION 120 174 Pre-S2. {ECO:0000256|HAMAP-
Rule:MF_04075}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000256|HAMAP-Rule:MF_04075}.
SEQUENCE 400 AA; 43859 MW; 0805ED9203CD7AB9 CRC64;
MGGWSSTPRK GMGTNLSVPN PLGFLPDHQL DPAFGANSNN PDWDFNPNKD HWPQAHQVGA
GAFGPGFTPS HGGLLGWSPQ AQGILTTVPA VPPPASTNRQ SGRQPTPISP PLRDSHPQAM
QWNSTTFHQT LQDPRVRGLY FPAGGSSSGT VNPVPNIASH ISSIFARTGD PAPNMENITS
GFLGPLLVLQ AGFFLLTKIL TIPQSLDSWW TSLNFLGGST VCLGQNSQSP TSNHSPTSCP
PICPGYRWMF LRRFIIFLFI LLLCLIFLLV LLDYQGMLPV CPLIPGSSTT STGPCRTCTT
PAQGNSMYPS CCCTKPSDGN CTCIPIPSSW AFAKYLWEWA SARFSWLNLL VPFVQWFVGL
SPTVWLSVIW MMWFWGPNLY NILSPFIPLL PIFFCLWVYI


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