Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q67875

- HBSAG_HBVD6

UniProt

Q67875 - HBSAG_HBVD6

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 58 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. virion membrane Source: UniProtKB-SubCell

    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

    Structurei

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 242241Intravirion; in internal conformationSequence AnalysisAdd
    BLAST
    Topological domaini2 – 170169Virion surface; in external conformationSequence AnalysisAdd
    BLAST
    Topological domaini192 – 24251Intravirion; in external conformationSequence AnalysisAdd
    BLAST
    Topological domaini264 – 33774Virion surfaceSequence AnalysisAdd
    BLAST
    Topological domaini359 – 3646IntravirionSequence Analysis
    Topological domaini388 – 3892Virion surfaceSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei171 – 19121Helical; Note=In external conformationSequence AnalysisAdd
    BLAST
    Transmembranei243 – 26321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei338 – 35821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei365 – 38723HelicalSequence AnalysisAdd
    BLAST

    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

    MGQNLSTSNP LGFFPDHQLD PASRANTANP DWDFNPNKDT WPDANKDGAG    50
    AFGLGLTPPH GGLLGWSPQA QGILHTVPAN PPPASTNRQT GRQPTPLSPP 100
    LRDTHPQAVQ WNSTTFHQTL QDPRVRGLYF PAGGSSSGTV NPVPTTASPL 150
    SSIFSRIGDP VTNMENITSG FLGPLLVLQA GFFLLTRILT IPQSLDSWWT 200
    SLNFRGGTTV CLGQNSQSPT SNHSPTSCPP TCPGYRWMCL RGFIIFLFIL 250
    LLCLIFLLVL LEYQGMLHVC PLIPGTTTTS TGPCKTCTTP AQGNSMFPSC 300
    CCTKTSDGNC TCIPIPSSWA FAKYLWEWAS VRFSWLSLLV PFVQWFVGLS 350
    PTVWLSAIWM MWYWGPSLYS ILSPFLPLLP IFFCLWVYI 389
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 1, 2014
    This is version 58 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