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P30029 (HBSAG_HPBDC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 45. 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 (strain China) (DHBV) [Complete proteome]
Taxonomic identifier31510 [NCBI]
Taxonomic lineageViruses › Retro-transcribing viruses › Hepadnaviridae › Avihepadnavirus
Virus hostAnas (ducks) [TaxID: 8835]

Protein attributes

Sequence length329 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.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform L (identifier: P30029-1)

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: P30029-2)

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

The sequence of this isoform differs from the canonical sequence as follows:
     1-162: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed; by host By similarity
Chain2 – 329328Large envelope protein
PRO_0000038077
Chain163 – ?23977Truncated S protein
PRO_0000322197

Regions

Topological domain2 – 237236Cytoplasmic; in internal conformation Potential
Topological domain2 – 164163Extracellular; in external conformation Potential
Transmembrane165 – 18521Helical; Name=TM1; Note=In external conformation; Potential
Topological domain186 – 23752Cytoplasmic; in external conformation Potential
Transmembrane238 – 25821Helical; Name=TM2; Potential
Topological domain259 – 29133Extracellular Potential
Transmembrane292 – 31221Helical; Name=TM3; Potential
Topological domain313 – 32917Cytoplasmic Potential
Region2 – 162161Pre-S By similarity

Sites

Site?239 – ?2402Cleavage; by host Potential

Amino acid modifications

Lipidation21N-myristoyl glycine; by host By similarity
Glycosylation2611N-linked (GlcNAc...); by host Potential

Natural variations

Alternative sequence1 – 162162Missing in isoform S.
VSP_031888

Sequences

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

Last modified February 26, 2008. Version 2.
Checksum: 4449E8B9C082EDD1

FASTA32936,419
        10         20         30         40         50         60 
MGQQPAKSMD VRRIEGGEIL LNQLAGRMIP KGAVTWSGKY PTIDHLLDHV QTMEEINTLQ 

        70         80         90        100        110        120 
QQGAWPAGAG RRVGLTNPTP QEIPQPQWTP EEDQKAREAF RRYQEERPPE TTTIPPSSTP 

       130        140        150        160        170        180 
PWKLQPGDDP LLESKSLLET HPLYQNPEPA VPVIKTPPLK KKMSGTFGGI LAGLIGLLVS 

       190        200        210        220        230        240 
FFLLIKILEI LRKLDWWWIS LSSPKGKMQC AFQDTGAQIS PHYAGSCPWG CPGFLWTYLR 

       250        260        270        280        290        300 
LFIIFLLILL VAAGLLYLTD NGSTILGKLQ WASVSALFSS ISSLLPSDQK SLVALMFGLL 

       310        320 
LIWMTSSSAT QTLVTLTQLA TLSALFFKN

« Hide

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

Checksum: F544F331095BDF10
Show »

FASTA16718,244

References

[1]"Complete nucleotide sequence of a Chinese duck hepatitis B virus."
Tong S., Mattes F., Teubner K., Blum H.E.
Nucleic Acids Res. 18:6139-6139(1990) [PubMed: 2235506] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M21953 Genomic DNA. Translation: AAA45746.1.
PIRSAVLWE. S12842.

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_HPBDC
AccessionPrimary (citable) accession number: P30029
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 26, 2008
Last modified: May 31, 2011
This is version 45 of the entry and version 2 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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