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Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen) [Cleaved into: Truncated S protein (St)]

 HBSAG_DHBV1             Reviewed;         328 AA.
P03145;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
20-DEC-2017, entry version 86.
RecName: Full=Large envelope protein;
AltName: Full=L glycoprotein;
AltName: Full=L-HBsAg;
Short=LHB;
AltName: Full=Large S protein;
AltName: Full=Large surface protein;
AltName: Full=Major surface antigen;
Contains:
RecName: Full=Truncated S protein;
Short=St;
Name=S;
Duck hepatitis B virus (strain United States/DHBV-16) (DHBV).
Viruses; Retro-transcribing viruses; Hepadnaviridae; Avihepadnavirus.
NCBI_TaxID=489543;
NCBI_TaxID=8835; Anas (ducks).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6699938;
Mandart E., Kay A., Galibert F.;
"Nucleotide sequence of a cloned duck hepatitis B virus genome:
comparison with woodchuck and human hepatitis B virus sequences.";
J. Virol. 49:782-792(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Isolate DHBV F1-6;
PubMed=2235507; DOI=10.1093/nar/18.20.6140;
Mattes F., Tong S., Teubner K., Blum H.E.;
"Complete nucleotide sequence of a German duck hepatitis B virus.";
Nucleic Acids Res. 18:6140-6140(1990).
[3]
MYRISTOYLATION AT GLY-2.
PubMed=1994583; DOI=10.1016/0042-6822(91)90503-4;
Macrae D.R., Bruss V., Ganem D.;
"Myristylation of a duck hepatitis B virus envelope protein is
essential for infectivity but not for virus assembly.";
Virology 181:359-363(1991).
[4]
PHOSPHORYLATION.
PubMed=7933117;
Grgacic E.V., Anderson D.A.;
"The large surface protein of duck hepatitis B virus is phosphorylated
in the pre-S domain.";
J. Virol. 68:7344-7350(1994).
[5]
PHOSPHORYLATION AT SER-118, AND MUTAGENESIS OF SER-118.
PubMed=9820150;
Grgacic E.V., Lin B., Gazina E.V., Snooks M.J., Anderson D.A.;
"Normal phosphorylation of duck hepatitis B virus L protein is
dispensable for infectivity.";
J. Gen. Virol. 79:2743-2751(1998).
[6]
MUTAGENESIS OF 185-LYS--GLU-188.
PubMed=12075081;
Grgacic E.V.;
"Identification of structural determinants of the first transmembrane
domain of the small envelope protein of duck hepatitis B virus
essential for particle morphogenesis.";
J. Gen. Virol. 83:1635-1644(2002).
[7]
CHARACTERIZATION OF TRUNCATED S PROTEIN.
PubMed=15827149; DOI=10.1128/JVI.79.9.5346-5352.2005;
Grgacic E.V., Anderson D.A.;
"St, a truncated envelope protein derived from the S protein of duck
hepatitis B virus, acts as a chaperone for the folding of the large
envelope protein.";
J. Virol. 79:5346-5352(2005).
-!- 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. The large envelope protein probably
also assumes fusion between virion and host membranes. In its
internal conformation the protein plays a role in virion
morphogenesis and mediates the contact with the nucleocapsid like
a matrix protein (By similarity). {ECO:0000250}.
-!- FUNCTION: Truncated S protein may be involved in translocation of
pre-S domain through the virion membrane.
-!- SUBUNIT: Large internal envelope protein interacts with capsid
protein. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Virion membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=L; Synonyms=Large envelope protein, LHB, L-HBsAg;
IsoId=P03145-1; Sequence=Displayed;
Name=S; Synonyms=Small envelope protein, SHB, S-HBsAg;
IsoId=P03145-2; Sequence=VSP_031887;
-!- 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.
-!- PTM: Myristoylation contributes importantly to DHBV infectivity.
It is most likely required for an early step of the life cycle
involving the entry or uncoating of virus particles.
{ECO:0000269|PubMed:1994583}.
-!- PTM: Phosphorylated on pre-S domain for about 50% of L proteins,
the L chains with internal pre-S region (Li-HBsAg).
{ECO:0000269|PubMed:7933117, ECO:0000269|PubMed:9820150}.
-!- PTM: Isoform S may be cleaved by a cellular protease to produce
truncated S protein.
-!- SIMILARITY: Belongs to the avihepadnavirus major surface antigen
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X12798; CAB57224.1; -; Genomic_DNA.
iPTMnet; P03145; -.
OrthoDB; VOG090000AH; -.
Proteomes; UP000007203; Genome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0039663; P:membrane fusion involved in viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
InterPro; IPR000349; HBV_HBSAG.
Pfam; PF00695; vMSA; 1.
1: Evidence at protein level;
Alternative initiation; Complete proteome;
Fusion of virus membrane with host membrane; Glycoprotein;
Host-virus interaction; Lipoprotein; Membrane; Myristate;
Phosphoprotein; Reference proteome; Transmembrane;
Transmembrane helix; Viral attachment to host cell;
Viral penetration into host cytoplasm; Virion;
Virus entry into host cell.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 328 Large envelope protein.
/FTId=PRO_0000038075.
CHAIN 162 ?238 Truncated S protein.
/FTId=PRO_0000322196.
TOPO_DOM 2 236 Cytoplasmic; in internal conformation.
{ECO:0000255}.
TOPO_DOM 2 163 Extracellular; in external conformation.
{ECO:0000255}.
TRANSMEM 164 184 Helical; Name=TM1; Note=In external
conformation. {ECO:0000255}.
TOPO_DOM 185 236 Cytoplasmic; in external conformation.
{ECO:0000255}.
TRANSMEM 237 257 Helical; Name=TM2. {ECO:0000255}.
TOPO_DOM 258 282 Extracellular. {ECO:0000255}.
TRANSMEM 283 303 Helical; Name=TM3. {ECO:0000255}.
TOPO_DOM 304 328 Cytoplasmic. {ECO:0000255}.
REGION 2 161 Pre-S.
SITE ?238 ?239 Cleavage; by host. {ECO:0000255}.
MOD_RES 118 118 Phosphoserine; by host.
{ECO:0000269|PubMed:9820150}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000269|PubMed:1994583}.
CARBOHYD 260 260 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
VAR_SEQ 1 161 Missing (in isoform S). {ECO:0000305}.
/FTId=VSP_031887.
MUTAGEN 118 118 S->A: 64% loss of phosphorylation.
{ECO:0000269|PubMed:9820150}.
MUTAGEN 185 188 KILE->AILA: Complete loss of pre-S domain
translocation.
{ECO:0000269|PubMed:12075081}.
SEQUENCE 328 AA; 36230 MW; B2D771241E407456 CRC64;
MGQHPAKSMD VRRIEGGEIL LNQLAGRMIP KGTLTWSGKF PTLDHVLDHV QTMEEINTLQ
NQGAWPAGAG RRVGLSNPTP QEIPQPQWTP EEDQKAREAF RRYQEERPPE TTTIPPSSPP
QWKLQPGDDP LLGNQSLLET HPLYQSEPAV PVIKTPPLKK KMSGTFGGIL AGLIGLLVSF
FLLIKILEIL RRLDWWWISL SSPKGKMQCA FQDTGAQISP HYVGSCPWGC PGFLWTYLRL
FIIFLLILLV AAGLLYLTDN GSTILGKLQW ASVSALFSSI SSLLPSDPKS LVALTFGLSL
IWMTSSSATQ TLVTLTQLAT LSALFYKS


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