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Protein

Large envelope protein

Gene

S

Organism
Duck hepatitis B virus (strain Germany/DHBV-3) (DHBV)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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
Gene namesi
Name:S
OrganismiDuck hepatitis B virus (strain Germany/DHBV-3) (DHBV)
Taxonomic identifieri489542 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesHepadnaviridaeAvihepadnavirus
Virus hostiAnas (ducks) [TaxID: 8835]
Proteomesi
  • UP000007204 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 236Intravirion; in internal conformationSequence analysisAdd BLAST235
Topological domaini2 – 163Virion surface; in external conformationSequence analysisAdd BLAST162
Transmembranei164 – 184Helical; Name=TM1; Note=In external conformationSequence analysisAdd BLAST21
Topological domaini185 – 236Intravirion; in external conformationSequence analysisAdd BLAST52
Transmembranei237 – 257Helical; Name=TM2Sequence analysisAdd BLAST21
Topological domaini258 – 282Virion surfaceSequence analysisAdd BLAST25
Transmembranei283 – 303Helical; Name=TM3Sequence analysisAdd BLAST21
Topological domaini304 – 328IntravirionSequence analysisAdd BLAST25

GO - Cellular componenti

Keywords - Cellular componenti

Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00003223762 – 328Large envelope proteinAdd BLAST327

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1
Glycosylationi260N-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?238 – ?239Cleavage; by hostSequence analysis2

Keywords - PTMi

Glycoprotein, Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PRIDEiP0C684

Interactioni

Subunit structurei

Large internal envelope protein interacts with capsid protein.By similarity

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 161Pre-SBy similarityAdd BLAST160

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: P0C684-1) [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
MGQHPAKSMD VRRIEGGELL LNQLAGRMIP KGTLTWSGKF PTIDHVLDHV
60 70 80 90 100
QTMEEINTLQ QQGAWPAGAG RRVGLSNPAP QEIPQPQWTP EEDQKAREAF
110 120 130 140 150
RRYQEERPPE TTTIPPTSPT QWKLQPGDDP LLGNQSLLET HPLYQTEPAV
160 170 180 190 200
PVIKTPPLKK KMSGTFGGIL AGLIGLLVSF FLLIKILEIL RRLDWWWISL
210 220 230 240 250
SSPKGKMQCA FQDTGAQISP HYAGSCPWGC PGFLWTYLRL FIIFLLILLV
260 270 280 290 300
AAGLLYLTDN GSTILGKLQW ASVSALFSSI SSLLPSDPKS LVALTFGLSL
310 320
IWMTSSSATQ TLVTLTQLAT LSALFYKS
Length:328
Mass (Da):36,218
Last modified:February 26, 2008 - v1
Checksum:iB26768D718127EE9
GO
Isoform S (identifier: P0C684-2) [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:
     1-161: Missing.

Show »
Length:167
Mass (Da):18,174
Checksum:iE87909ED394531C2
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0318971 – 161Missing in isoform S. CuratedAdd BLAST161

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ195079 Genomic DNA No translation available.

Keywords - Coding sequence diversityi

Alternative initiation

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ195079 Genomic DNA No translation available.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP0C684

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OrthoDBiVOG090000AH

Family and domain databases

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

Entry informationi

Entry nameiHBSAG_DHBV3
AccessioniPrimary (citable) accession number: P0C684
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: February 26, 2008
Last modified: December 20, 2017
This is version 35 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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Main funding by: National Institutes of Health

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