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Q67875

- HBSAG_HBVD6

UniProt

Q67875 - HBSAG_HBVD6

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Protein

Large envelope protein

Gene

S

Organism
Hepatitis B virus genotype D subtype ayw (isolate Italy/CI/1992) (HBV-D)
Status
Reviewed - Annotation score: 4 out of 5- 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. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assumes fusion between virion membrane and endosomal membrane (Probable). 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 similarityCurated
The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid (By similarity).By similarity

GO - Biological processi

  1. caveolin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  2. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
  3. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Caveolin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virus endocytosis by host, 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
OrganismiHepatitis B virus genotype D subtype ayw (isolate Italy/CI/1992) (HBV-D)
Taxonomic identifieri489489 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesHepadnaviridaeOrthohepadnavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Pan troglodytes (Chimpanzee) [TaxID: 9598]
ProteomesiUP000008282: Genome

Subcellular locationi

Virion membrane By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 242241Intravirion; in internal conformationSequence AnalysisAdd
BLAST
Topological domaini2 – 170169Virion surface; in external conformationSequence AnalysisAdd
BLAST
Transmembranei171 – 19121Helical; Note=In external conformationSequence AnalysisAdd
BLAST
Topological domaini192 – 24251Intravirion; in external conformationSequence AnalysisAdd
BLAST
Transmembranei243 – 26321HelicalSequence AnalysisAdd
BLAST
Topological domaini264 – 33774Virion surfaceSequence AnalysisAdd
BLAST
Transmembranei338 – 35821HelicalSequence AnalysisAdd
BLAST
Topological domaini359 – 3646IntravirionSequence Analysis
Transmembranei365 – 38723HelicalSequence AnalysisAdd
BLAST
Topological domaini388 – 3892Virion surfaceSequence Analysis

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. virion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Virion

Pathology & Biotechi

Biotechnological usei

Systematic vaccination of individuals at risk of exposure to the virus has been the main method of controlling the morbidity and mortality associated with hepatitis B. The first hepatitis B vaccine was manufactured by the purification and inactivation of HBsAg obtained from the plasma of chronic hepatitis B virus carriers. The vaccine is now produced by recombinant DNA techniques and expression of the S isoform in yeast cells. The pre-S region do not seem to induce strong enough antigenic response.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by hostBy similarity
Chaini2 – 389388Large envelope proteinPRO_0000319087Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
Glycosylationi309 – 3091N-linked (GlcNAc...); by hostBy similarity

Post-translational modificationi

Myristoylated.By similarity

Keywords - PTMi

Glycoprotein, Lipoprotein, Myristate

Interactioni

Subunit structurei

Li-HBsAg interacts with capsid protein and with HDV Large delta antigen. Isoform M associates with host chaperone CANX through its pre-S2 N glycan. This association may be essential for M proper secretion (By similarity).By similarity

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 163162Pre-SAdd
BLAST
Regioni2 – 108107Pre-S1Add
BLAST
Regioni109 – 16355Pre-S2Add
BLAST

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

Family and domain databases

InterProiIPR000349. Hepvir_surfAg.
[Graphical view]
PfamiPF00695. vMSA. 1 hit.
[Graphical view]

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 splicing and alternative initiation. Align

Isoform L (identifier: Q67875-1) [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
MGQNLSTSNP LGFFPDHQLD PASRANTANP DWDFNPNKDT WPDANKDGAG
60 70 80 90 100
AFGLGLTPPH GGLLGWSPQA QGILHTVPAN PPPASTNRQT GRQPTPLSPP
110 120 130 140 150
LRDTHPQAVQ WNSTTFHQTL QDPRVRGLYF PAGGSSSGTV NPVPTTASPL
160 170 180 190 200
SSIFSRIGDP VTNMENITSG FLGPLLVLQA GFFLLTRILT IPQSLDSWWT
210 220 230 240 250
SLNFRGGTTV CLGQNSQSPT SNHSPTSCPP TCPGYRWMCL RGFIIFLFIL
260 270 280 290 300
LLCLIFLLVL LEYQGMLHVC PLIPGTTTTS TGPCKTCTTP AQGNSMFPSC
310 320 330 340 350
CCTKTSDGNC TCIPIPSSWA FAKYLWEWAS VRFSWLSLLV PFVQWFVGLS
360 370 380
PTVWLSAIWM MWYWGPSLYS ILSPFLPLLP IFFCLWVYI
Length:389
Mass (Da):42,661
Last modified:November 1, 1996 - v1
Checksum:iA39542B416E48F24
GO
Isoform S (identifier: Q67875-2) [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:226
Mass (Da):25,416
Checksum:i12A0B859465C37CE
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 163163Missing in isoform S. CuratedVSP_031410Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65258 Genomic DNA. Translation: CAA46353.1.
PIRiJQ2054.
S20749.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Web resourcesi

HepSEQ

Hepatitis virus B database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65258 Genomic DNA. Translation: CAA46353.1 .
PIRi JQ2054.
S20749.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR000349. Hepvir_surfAg.
[Graphical view ]
Pfami PF00695. vMSA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Sequence analysis of HBV genomes isolated from patients with HBsAg negative chronic liver disease."
    Lai M.E., Mazzoleni A.P., Balestrieri A., Melis A., Porru A.
    Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Functions of the large hepatitis B virus surface protein in viral particle morphogenesis."
    Bruss V., Gerhardt E., Vieluf K., Wunderlich G.
    Intervirology 39:23-31(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  3. "Role of glycan processing in hepatitis B virus envelope protein trafficking."
    Block T.M., Lu X., Mehta A., Park J., Blumberg B.S., Dwek R.
    Adv. Exp. Med. Biol. 435:207-216(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  4. "Envelopment of the hepatitis B virus nucleocapsid."
    Bruss V.
    Virus Res. 106:199-209(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  5. "Hepatitis B virus pre-S mutants, endoplasmic reticulum stress and hepatocarcinogenesis."
    Wang H.C., Huang W., Lai M.D., Su I.J.
    Cancer Sci. 97:683-688(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiHBSAG_HBVD6
AccessioniPrimary (citable) accession number: Q67875
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 59 of the entry and version 1 of the sequence. [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

External Data

Dasty 3