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Protein

Large envelope protein

Gene

S

Organism
Duck hepatitis B virus (isolate Shanghai/DHBVQCA34) (DHBV)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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

GO - Biological processi

Keywordsi

Biological processFusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended 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:
Truncated S protein
Short name:
St
Gene namesi
Name:S
OrganismiDuck hepatitis B virus (isolate Shanghai/DHBVQCA34) (DHBV)
Taxonomic identifieri644639 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesHepadnaviridaeAvihepadnavirus
Virus hostiAnas (ducks) [TaxID: 8835]
Proteomesi
  • UP000009098 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 238Cytoplasmic; in internal conformationSequence analysisAdd BLAST237
Topological domaini2 – 165Extracellular; in external conformationSequence analysisAdd BLAST164
Transmembranei166 – 186HelicalSequence analysisAdd BLAST21
Topological domaini187 – 238Cytoplasmic; in external conformationSequence analysisAdd BLAST52
Transmembranei239 – 259HelicalSequence analysisAdd BLAST21
Topological domaini260 – 292ExtracellularSequence analysisAdd BLAST33
Transmembranei293 – 313HelicalSequence analysisAdd BLAST21
Topological domaini314 – 330CytoplasmicSequence analysisAdd BLAST17

GO - Cellular componenti

Keywords - Cellular componenti

Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00003976812 – 330Large envelope proteinAdd BLAST329
ChainiPRO_0000397682164 – ?240Truncated S proteinAdd BLAST77

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1
Glycosylationi262N-linked (GlcNAc...) asparagine; by hostSequence analysis1

Post-translational modificationi

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).

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei?240 – ?241Cleavage; by hostSequence analysis2

Keywords - PTMi

Glycoprotein, Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

Large internal envelope protein interacts with capsid protein.By similarity

Structurei

3D structure databases

SMRiQ66405
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 163Pre-SBy similarityAdd BLAST162
Regioni166 – 186TM1By similarityAdd BLAST21
Regioni239 – 259TM2By similarityAdd BLAST21
Regioni293 – 313TM3By similarityAdd BLAST21

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi160 – 163Poly-Lys4

Domaini

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.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

OrthoDBiVOG090000AH

Family and domain databases

InterProiView protein in InterPro
IPR000349 HBV_HBSAG
PfamiView protein in Pfam
PF00695 vMSA, 1 hit

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform L (identifier: Q66405-1) [UniParc]FASTAAdd to basket
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.

« Hide

        10         20         30         40         50
MGQQPAKSMD VRRIEGGELL LNQLAGRMIP KGTVTWSGKF PTIDHLLDHV
60 70 80 90 100
QTMEEVNTLQ QQGAWPAGAG RRLGLTNPTP HETPQPQWTP EEDQKAREAF
110 120 130 140 150
RRYQEERPPE TTTIAPTSPT PWKLQPGDDP LLENKSLLET HPLYQNPEPA
160 170 180 190 200
VPVIKTPPLK KKKMPGTFGG ILAGLIGLLV SFFLLIKILE ILRRLDWWWI
210 220 230 240 250
SLSSPKGKMQ CAFQDTGAQI SQHYVGSCPW GCPGFLWTYL RLFIIFLLIL
260 270 280 290 300
LVAAGLLYLT DNMSIILEKL QWESVSVLFS SISSLLPSDQ KSLVALMFGL
310 320 330
LLIWMTSSSA TQTLVTLTQL ATLSVLFYKN
Length:330
Mass (Da):36,959
Last modified:November 1, 1996 - v1
Checksum:i7CE142013BB8D9F4
GO
Isoform S (identifier: Q66405-2) [UniParc]FASTAAdd to basket
Also known as: Small envelope protein, SHB, S-HBsAg

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

Show »
Length:167
Mass (Da):18,629
Checksum:i9CBEB135D24C1C75
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0396911 – 163Missing in isoform S. CuratedAdd BLAST163

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60213 Genomic DNA Translation: CAA42770.1 Sequence problems.
X60213 Genomic DNA Translation: CAA42771.1
X60213 Genomic DNA Translation: CAA42772.1 Sequence problems.
RefSeqiNP_039823.1, NC_001344.1
NP_039824.1, NC_001344.1
NP_039826.1, NC_001344.1

Genome annotation databases

GeneIDi2546411
2546412
2546415
KEGGivg:2546411
vg:2546412
vg:2546415

Keywords - Coding sequence diversityi

Alternative initiation

Similar proteinsi

Entry informationi

Entry nameiHBSAG_DHBVQ
AccessioniPrimary (citable) accession number: Q66405
Secondary accession number(s): Q66404, Q89748
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: November 1, 1996
Last modified: December 20, 2017
This is version 66 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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