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P17195 (HBSAG_HPBDW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Large envelope protein
Alternative name(s):
L glycoprotein
L-HBsAg
Short name=LHB
Large S protein
Large surface protein
Major surface antigen

Cleaved into the following chain:

  1. Truncated S protein
    Short name=St
Gene names
Name:S
OrganismDuck hepatitis B virus (isolate white Shanghai duck S31) (DHBV) [Complete proteome]
Taxonomic identifier10440 [NCBI]
Taxonomic lineageViruses › Retro-transcribing viruses › Hepadnaviridae › Avihepadnavirus
Virus hostAnas (ducks) [TaxID: 8835]

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

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.

Truncated S protein may be involved in translocation of pre-S domain through the virion membrane By similarity.

Subunit structure

Large internal envelope protein interacts with capsid protein By similarity.

Subcellular location

Virion membrane.

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.

Post-translational modification

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.

Phosphorylated on pre-S domain for about 50% of L proteins, the L chains with internal pre-S region (Li-HBsAg).

Sequence similarities

Belongs to the avihepadnavirus major surface antigen family.

Sequence caution

The sequence AAA45752.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform L (identifier: P17195-1)

Also known as: Large envelope protein; LHB; L-HBsAg;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform S (identifier: P17195-2)

Also known as: Small envelope protein; SHB; S-HBsAg;

The sequence of this isoform differs from the canonical sequence as follows:
     1-163: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 330329Large envelope protein
PRO_0000038081
Chain164 – ?24077Truncated S protein
PRO_0000322199

Regions

Topological domain2 – 238237Cytoplasmic; in internal conformation Potential
Topological domain2 – 165164Extracellular; in external conformation Potential
Transmembrane166 – 18621Helical; Name=TM1; Note=In external conformation; Potential
Topological domain187 – 23852Cytoplasmic; in external conformation Potential
Transmembrane239 – 25921Helical; Name=TM2; Potential
Topological domain260 – 29233Extracellular Potential
Transmembrane293 – 31321Helical; Name=TM3; Potential
Topological domain314 – 33017Cytoplasmic Potential
Region2 – 163162Pre-S

Sites

Site?240 – ?2412Cleavage; by host Potential

Amino acid modifications

Lipidation21N-myristoyl glycine; by host By similarity
Glycosylation2621N-linked (GlcNAc...); by host Potential

Natural variations

Alternative sequence1 – 163163Missing in isoform S.
VSP_031890

Sequences

Sequence LengthMass (Da)Tools
Isoform L (Large envelope protein) (LHB) (L-HBsAg) [UniParc].

Last modified February 26, 2008. Version 3.
Checksum: E56A456853C00775

FASTA33036,787
        10         20         30         40         50         60 
MGQQPAKSMD VRRIEGGELL LNQLAGRMIP KGTVTWSGKF PTIDHLLDHV QTMEEVNTLQ 

        70         80         90        100        110        120 
QQGAWPAGAG RRLGLTNPAP QEPPQPQWTP EEDQKAREAF RRYQEERPPE TTTIPPTSPT 

       130        140        150        160        170        180 
PWKLQPGDDP LLENKSLLET HPLYQNPEPA VPVIKTPPLR KKKMAGTFGG ILAGLIGLLV 

       190        200        210        220        230        240 
GFFLLIKILE ILRRLDWWWI SLSSPKGKMQ CAFQDTGAQI SPHYAGFCPW GCPGFLWTYL 

       250        260        270        280        290        300 
RLFIIFLLIL LVAAGLLYLT DNMSIILGKL QWESVSALFS SISSLLPSDQ KSLVALMFGL 

       310        320        330 
LLIWMTSSSA TQTLVTLTQL ATLSALFYKN

« Hide

Isoform S (Small envelope protein) (SHB) (S-HBsAg) [UniParc].

Checksum: A9B4916005C19F0C
Show »

FASTA16718,446

References

[1]"Molecular cloning and sequence analysis of duck hepatitis B virus genomes of a new variant isolated from Shanghai ducks."
Uchida M., Esumi M., Shikata T.
Virology 173:600-606(1989) [PubMed: 2596031] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M32991 Genomic DNA. Translation: AAA45752.1. Different initiation.
PIRSAVLWD. D33746.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000349. Hepvir_surfAg.
[Graphical view]
PfamPF00695. vMSA. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHBSAG_HPBDW
AccessionPrimary (citable) accession number: P17195
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 26, 2008
Last modified: May 31, 2011
This is version 51 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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