HBSAG_HBVC6
ID HBSAG_HBVC6 Reviewed; 226 AA.
AC P30019;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 23-FEB-2022, entry version 68.
DE RecName: Full=Small envelope protein;
DE AltName: Full=S glycoprotein;
DE AltName: Full=S-HBsAg;
DE Short=SHB;
DE AltName: Full=Small S protein;
DE AltName: Full=Small surface protein;
GN Name=S;
OS Hepatitis B virus genotype C subtype adr (isolate China/NC-1/1988) (HBV-C).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX NCBI_TaxID=31513;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Qi Z.H., Yan J., Xiong W.J., Cai L.W.;
RT "Determination of the nucleotide sequence and studies on the structure of
RT hepatitis B virus (HBV) adr NC-1 surface antigen (HBsAg) gene.";
RL Sheng Wu Hua Hsueh Tsa Chih 4:201-209(1988).
RN [2]
RP REVIEW.
RX PubMed=8957666; DOI=10.1159/000150471;
RA Bruss V., Gerhardt E., Vieluf K., Wunderlich G.;
RT "Functions of the large hepatitis B virus surface protein in viral particle
RT morphogenesis.";
RL Intervirology 39:23-31(1996).
RN [3]
RP REVIEW.
RX PubMed=9498079; DOI=10.1007/978-1-4615-5383-0_20;
RA Block T.M., Lu X., Mehta A., Park J., Blumberg B.S., Dwek R.;
RT "Role of glycan processing in hepatitis B virus envelope protein
RT trafficking.";
RL Adv. Exp. Med. Biol. 435:207-216(1998).
RN [4]
RP REVIEW.
RX PubMed=15567498; DOI=10.1016/j.virusres.2004.08.016;
RA Bruss V.;
RT "Envelopment of the hepatitis B virus nucleocapsid.";
RL Virus Res. 106:199-209(2004).
RN [5]
RP REVIEW.
RX PubMed=16863502; DOI=10.1111/j.1349-7006.2006.00235.x;
RA Wang H.C., Huang W., Lai M.D., Su I.J.;
RT "Hepatitis B virus pre-S mutants, endoplasmic reticulum stress and
RT hepatocarcinogenesis.";
RL Cancer Sci. 97:683-688(2006).
CC -!- FUNCTION: The large envelope protein exists in two topological
CC conformations, one which is termed 'external' or Le-HBsAg and the other
CC 'internal' or Li-HBsAg. In its external conformation the protein
CC attaches the virus to cell receptors and thereby initiating infection.
CC This interaction determines the species specificity and liver tropism.
CC This attachment induces virion internalization predominantly through
CC caveolin-mediated endocytosis. The large envelope protein also assumes
CC fusion between virion membrane and endosomal membrane (Probable). In
CC its internal conformation the protein plays a role in virion
CC morphogenesis and mediates the contact with the nucleocapsid like a
CC matrix protein (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- FUNCTION: The middle envelope protein plays an important role in the
CC budding of the virion. It is involved in the induction of budding in a
CC nucleocapsid independent way. In this process the majority of envelope
CC proteins bud to form subviral lipoprotein particles of 22 nm of
CC diameter that do not contain a nucleocapsid (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}.
CC -!- BIOTECHNOLOGY: Systematic vaccination of individuals at risk of
CC exposure to the virus has been the main method of controlling the
CC morbidity and mortality associated with hepatitis B. The first
CC hepatitis B vaccine was manufactured by the purification and
CC inactivation of HBsAg obtained from the plasma of chronic hepatitis B
CC virus carriers. The vaccine is now produced by recombinant DNA
CC techniques and expression of the S isoform in yeast cells. The pre-S
CC region do not seem to induce strong enough antigenic response.
CC -!- SIMILARITY: Belongs to the orthohepadnavirus major surface antigen
CC family. {ECO:0000305}.
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DR PIR; JC1002; SAVLN1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0075513; P:caveolin-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR000349; HBV_HBSAG.
DR Pfam; PF00695; vMSA; 1.
PE 1: Evidence at protein level;
KW Caveolin-mediated endocytosis of virus by host;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host-virus interaction; Lipoprotein; Membrane; Myristate; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Virion; Virus endocytosis by host;
KW Virus entry into host cell.
FT CHAIN 1..226
FT /note="Small envelope protein"
FT /id="PRO_0000222356"
FT TOPO_DOM 1..7
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..79
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..174
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..201
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..226
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000250"
SQ SEQUENCE 226 AA; 25397 MW; 90FC24FA074B66AF CRC64;
MENTASGFLG PLLVLQAGFF LLTRILTIPQ SLDSWWTSLN FLGGAPTCPG QNSQSPTSNH
SPTSCPPICP GYRWMCLRRF IIFLFILLLC LIFLLVLLDY HGMLPVCPLL PGTSTTSTGP
CKTCTIPAQG TSMFPSCCCT KPSDGNCTCI PIPSSWAFAR FLWEWASVRF SWLSLLVPFV
QWFVGLSPTV WLSVIWMMWY WGPSLYNILS PFLPLLPIFF CLWVYI
