HBSAG_WHV6
ID HBSAG_WHV6 Reviewed; 292 AA.
AC P11293;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Large envelope protein;
DE AltName: Full=L glycoprotein;
DE AltName: Full=L-HBsAg;
DE Short=LHB;
DE AltName: Full=Large S protein;
DE AltName: Full=Large surface protein;
DE AltName: Full=Major surface antigen;
DE Flags: Fragment;
GN Name=S;
OS Woodchuck hepatitis B virus (isolate w64/pWS23) (WHV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX NCBI_TaxID=10436;
OH NCBI_TaxID=9995; Marmota monax (Woodchuck).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3582979; DOI=10.1016/0378-1119(86)90325-2;
RA Etiemble J., Moeroey T., Trepo C., Tiollais P., Buendia M.-A.;
RT "Nucleotide sequence of the woodchuck hepatitis virus surface antigen mRNAs
RT and the variability of three overlapping viral genes.";
RL Gene 50:207-214(1986).
RN [2]
RP REVIEW.
RX PubMed=8957666; DOI=10.1159/000150471;
RA Bruss V., Gerhardt E., Vieluf K., Wunderlich G.;
RT "Functions of the large hepatitis B virus surface protein in viral particle
RT morphogenesis.";
RL Intervirology 39:23-31(1996).
RN [3]
RP REVIEW.
RX PubMed=9498079; DOI=10.1007/978-1-4615-5383-0_20;
RA Block T.M., Lu X., Mehta A., Park J., Blumberg B.S., Dwek R.;
RT "Role of glycan processing in hepatitis B virus envelope protein
RT trafficking.";
RL Adv. Exp. Med. Biol. 435:207-216(1998).
RN [4]
RP REVIEW.
RX PubMed=15567498; DOI=10.1016/j.virusres.2004.08.016;
RA Bruss V.;
RT "Envelopment of the hepatitis B virus nucleocapsid.";
RL Virus Res. 106:199-209(2004).
RN [5]
RP REVIEW.
RX PubMed=16863502; DOI=10.1111/j.1349-7006.2006.00235.x;
RA Wang H.C., Huang W., Lai M.D., Su I.J.;
RT "Hepatitis B virus pre-S mutants, endoplasmic reticulum stress and
RT hepatocarcinogenesis.";
RL Cancer Sci. 97:683-688(2006).
CC -!- FUNCTION: The large envelope protein exists in two topological
CC conformations, one which is termed 'external' or Le-HBsAg and the other
CC 'internal' or Li-HBsAg. In its external conformation the protein
CC attaches the virus to cell receptors and thereby initiating infection.
CC This interaction determines the species specificity and liver tropism.
CC The large envelope protein probably also assumes fusion between virion
CC and host membranes. In its internal conformation the protein plays a
CC role in virion morphogenesis and mediates the contact with the
CC nucleocapsid like a matrix protein (By similarity). {ECO:0000250}.
CC -!- FUNCTION: The middle envelope protein plays an important role in the
CC budding of the virion. It is involved in the induction of budding in a
CC nucleocapsid independent way. In this process the majority of envelope
CC proteins bud to form subviral lipoprotein particles of 22 nm of
CC diameter that do not contain a nucleocapsid (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: [Isoform L]: In its internal form (Li-HBsAg), interacts with
CC the capsid protein and with the isoform S. Interacts with host
CC chaperone CANX. {ECO:0000250|UniProtKB:P03141}.
CC -!- SUBUNIT: [Isoform M]: Associates with host chaperone CANX through its
CC pre-S2 N glycan; this association may be essential for isoform M proper
CC secretion. {ECO:0000250|UniProtKB:P03141}.
CC -!- SUBUNIT: [Isoform S]: Interacts with isoform L. Interacts with the
CC antigens of satellite virus HDV (HDVAgs); this interaction is required
CC for encapsidation of HDV genomic RNA. {ECO:0000250|UniProtKB:P03141}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=L; Synonyms=Large envelope protein, LHB, L-HBsAg;
CC IsoId=P11293-1; Sequence=Displayed;
CC Name=M; Synonyms=Middle envelope protein, MHB, M-HBsAg;
CC IsoId=P11293-2; Sequence=VSP_031463;
CC Name=S; Synonyms=Small envelope protein, SHB, S-HBsAg;
CC IsoId=P11293-3; Sequence=VSP_031462;
CC -!- DOMAIN: The large envelope protein is synthesized with the pre-S region
CC at the cytosolic side of the endoplasmic reticulum and, hence will be
CC within the virion after budding. Therefore the pre-S region is not N-
CC glycosylated. Later a post-translational translocation of N-terminal
CC pre-S and TM1 domains occur in about 50% of proteins at the virion
CC surface. These molecules change their topology by an unknown mechanism,
CC resulting in exposure of pre-S region at virion surface. For isoform M
CC in contrast, the pre-S2 region is translocated cotranslationally to the
CC endoplasmic reticulum lumen and is N-glycosylated.
CC -!- PTM: Isoform M is N-glycosylated by host at the pre-S2 region.
CC {ECO:0000250|UniProtKB:P03138}.
CC -!- PTM: Myristoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the orthohepadnavirus major surface antigen
CC family. {ECO:0000305}.
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DR EMBL; M15954; AAA69574.1; -; mRNA.
DR PIR; B29498; SAVL64.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0039663; P:membrane fusion involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR000349; HBV_HBSAG.
DR Pfam; PF00695; vMSA; 1.
PE 2: Evidence at transcript level;
KW Alternative initiation; Alternative splicing;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host-virus interaction; Lipoprotein; Membrane; Myristate; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT CHAIN <1..292
FT /note="Large envelope protein"
FT /id="PRO_0000038125"
FT TOPO_DOM <1..147
FT /note="Intravirion; in internal conformation"
FT /evidence="ECO:0000255"
FT TOPO_DOM <1..75
FT /note="Virion surface; in external conformation"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical; Note=In external conformation"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..147
FT /note="Intravirion; in external conformation"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..240
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..267
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 268..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..292
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT REGION <1..70
FT /note="Pre-S"
FT /evidence="ECO:0000250"
FT REGION <1..10
FT /note="Pre-S1"
FT /evidence="ECO:0000250"
FT REGION 11..70
FT /note="Pre-S2"
FT /evidence="ECO:0000250"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
FT VAR_SEQ <1..70
FT /note="Missing (in isoform S)"
FT /evidence="ECO:0000305"
FT /id="VSP_031462"
FT VAR_SEQ <1..10
FT /note="Missing (in isoform M)"
FT /evidence="ECO:0000305"
FT /id="VSP_031463"
FT NON_TER 1
FT CARBOHYD P11293-2:3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:P03138"
SQ SEQUENCE 292 AA; 33221 MW; 1D39E1312BBC6AC3 CRC64;
PLRDTHPHLT MKNQTFHLQG FVDGLRDLTT TERHHNAYGD PFTTLSPVVP TVSTTLSPPS
TTGDPALSPE MSPSSLLGLL AGLQVVYFLW TKIPTIAQNL DWWWTSLSFP GGIPECTGQN
SQFQTCKHLP TSCPPTCNGF RWMYLRRFII YLLVLLLCLI FLLVLLDWKG LLPVCPLQPT
TETTVNCRQC TLSVQDTYTP PYCCCLKPTA GNCTCWPIPS SWALGNYLWE WALARFSWLN
LLVPLLQWLG GISLIAWFLL IWMIWFWGPA LLSILPPFIP IFVLFFLIWV YI
