HBSAG_HPBDC
ID HBSAG_HPBDC Reviewed; 329 AA.
AC P30029;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 25-MAY-2022, entry version 66.
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 Contains:
DE RecName: Full=Truncated S protein;
DE Short=St;
GN Name=S;
OS Duck hepatitis B virus (strain China) (DHBV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Avihepadnavirus.
OX NCBI_TaxID=31510;
OH NCBI_TaxID=8835; Anas (ducks).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2235506; DOI=10.1093/nar/18.20.6139;
RA Tong S., Mattes F., Teubner K., Blum H.E.;
RT "Complete nucleotide sequence of a Chinese duck hepatitis B virus.";
RL Nucleic Acids Res. 18:6139-6139(1990).
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: Truncated S protein may be involved in translocation of pre-S
CC domain through the virion membrane. {ECO:0000250}.
CC -!- SUBUNIT: Large internal envelope protein interacts with capsid protein.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=L; Synonyms=Large envelope protein, LHB, L-HBsAg;
CC IsoId=P30029-1; Sequence=Displayed;
CC Name=S; Synonyms=Small envelope protein, SHB, S-HBsAg;
CC IsoId=P30029-2; Sequence=VSP_031888;
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.
CC -!- PTM: Myristoylation contributes importantly to DHBV infectivity. It is
CC most likely required for an early step of the life cycle involving the
CC entry or uncoating of virus particles.
CC -!- PTM: Phosphorylated on pre-S domain for about 50% of L proteins, the L
CC chains with internal pre-S region (Li-HBsAg).
CC -!- SIMILARITY: Belongs to the avihepadnavirus major surface antigen
CC family. {ECO:0000305}.
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DR EMBL; M21953; AAA45746.1; -; Genomic_DNA.
DR PIR; S12842; SAVLWE.
DR Proteomes; UP000008119; Genome.
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; 2.
PE 3: Inferred from homology;
KW Alternative initiation; Fusion of virus membrane with host membrane;
KW Glycoprotein; Host-virus interaction; Lipoprotein; Membrane; Myristate;
KW Phosphoprotein; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral penetration into host cytoplasm;
KW Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..329
FT /note="Large envelope protein"
FT /id="PRO_0000038077"
FT CHAIN 163..?239
FT /note="Truncated S protein"
FT /id="PRO_0000322197"
FT TOPO_DOM 2..237
FT /note="Cytoplasmic; in internal conformation"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2..164
FT /note="Extracellular; in external conformation"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical; Name=TM1; Note=In external conformation"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..237
FT /note="Cytoplasmic; in external conformation"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=TM2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Name=TM3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 2..162
FT /note="Pre-S"
FT /evidence="ECO:0000250"
FT REGION 61..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE ?239..?240
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..162
FT /note="Missing (in isoform S)"
FT /evidence="ECO:0000305"
FT /id="VSP_031888"
SQ SEQUENCE 329 AA; 36419 MW; 4449E8B9C082EDD1 CRC64;
MGQQPAKSMD VRRIEGGEIL LNQLAGRMIP KGAVTWSGKY PTIDHLLDHV QTMEEINTLQ
QQGAWPAGAG RRVGLTNPTP QEIPQPQWTP EEDQKAREAF RRYQEERPPE TTTIPPSSTP
PWKLQPGDDP LLESKSLLET HPLYQNPEPA VPVIKTPPLK KKMSGTFGGI LAGLIGLLVS
FFLLIKILEI LRKLDWWWIS LSSPKGKMQC AFQDTGAQIS PHYAGSCPWG CPGFLWTYLR
LFIIFLLILL VAAGLLYLTD NGSTILGKLQ WASVSALFSS ISSLLPSDQK SLVALMFGLL
LIWMTSSSAT QTLVTLTQLA TLSALFFKN
