位置:首页 > 蛋白库 > HBSAG_HBVA5
HBSAG_HBVA5
ID   HBSAG_HBVA5             Reviewed;         400 AA.
AC   Q02317;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   23-FEB-2022, entry version 77.
DE   RecName: Full=Large envelope protein {ECO:0000255|HAMAP-Rule:MF_04075};
DE   AltName: Full=L glycoprotein {ECO:0000255|HAMAP-Rule:MF_04075};
DE   AltName: Full=L-HBsAg {ECO:0000255|HAMAP-Rule:MF_04075};
DE            Short=LHB {ECO:0000255|HAMAP-Rule:MF_04075};
DE   AltName: Full=Large S protein {ECO:0000255|HAMAP-Rule:MF_04075};
DE   AltName: Full=Large surface protein {ECO:0000255|HAMAP-Rule:MF_04075};
DE   AltName: Full=Major surface antigen {ECO:0000255|HAMAP-Rule:MF_04075};
GN   Name=S {ECO:0000255|HAMAP-Rule:MF_04075};
OS   Hepatitis B virus genotype A1 subtype adw (isolate
OS   Philippines/pFDW294/1988) (HBV-A).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Blubervirales; Hepadnaviridae; Orthohepadnavirus.
OX   NCBI_TaxID=31514;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Estacio R.C., Chavez C.C., Okamoto H., Lingao A.L., Reyes M.T., Domingo E.,
RA   Mayumi M.;
RT   "Nucleotide sequence of a hepatitis B virus genome of subtype adw isolated
RT   from a Philippino: comparison with the reported three genomes of the same
RT   subtype.";
RL   J. Gastroenterol. Hepatol. 3:215-222(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 assures
CC       fusion between virion membrane and endosomal membrane. In its internal
CC       conformation the protein plays a role in virion morphogenesis and
CC       mediates the contact with the nucleocapsid like a matrix protein.
CC       {ECO:0000255|HAMAP-Rule:MF_04075}.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_04075}.
CC   -!- SUBUNIT: [Isoform L]: In its internal form (Li-HBsAg), interacts with
CC       the capsid protein and with the isoform S. Interacts with host
CC       chaperone CANX. {ECO:0000250|UniProtKB:P03141}.
CC   -!- SUBUNIT: [Isoform M]: Associates with host chaperone CANX through its
CC       pre-S2 N glycan; this association may be essential for isoform M proper
CC       secretion. {ECO:0000250|UniProtKB:P03141}.
CC   -!- SUBUNIT: [Isoform S]: Interacts with isoform L. Interacts with the
CC       antigens of satellite virus HDV (HDVAgs); this interaction is required
CC       for encapsidation of HDV genomic RNA. {ECO:0000250|UniProtKB:P03141}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04075}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC       Name=L; Synonyms=Large envelope protein, LHB, L-HBsAg;
CC         IsoId=Q02317-1; Sequence=Displayed;
CC       Name=M; Synonyms=Middle envelope protein, MHB, M-HBsAg;
CC         IsoId=Q02317-2; Sequence=VSP_031359;
CC       Name=S; Synonyms=Small envelope protein, SHB, S-HBsAg;
CC         IsoId=Q02317-3; Sequence=VSP_031358;
CC   -!- DOMAIN: The large envelope protein is synthesized with the pre-S region
CC       at the cytosolic side of the endoplasmic reticulum and, hence will be
CC       within the virion after budding. Therefore the pre-S region is not N-
CC       glycosylated. Later a post-translational translocation of N-terminal
CC       pre-S and TM1 domains occur in about 50% of proteins at the virion
CC       surface. These molecules change their topology by an unknown mechanism,
CC       resulting in exposure of pre-S region at virion surface. For isoform M
CC       in contrast, the pre-S2 region is translocated cotranslationally to the
CC       endoplasmic reticulum lumen and is N-glycosylated. {ECO:0000255|HAMAP-
CC       Rule:MF_04075}.
CC   -!- PTM: Isoform M is N-terminally acetylated by host at a ratio of 90%,
CC       and N-glycosylated by host at the pre-S2 region.
CC       {ECO:0000250|UniProtKB:P03138, ECO:0000255|HAMAP-Rule:MF_04075}.
CC   -!- PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04075}.
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:0000255|HAMAP-Rule:MF_04075}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M57663; AAA69680.1; -; Genomic_DNA.
DR   Proteomes; UP000007908; Genome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
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-UniRule.
DR   HAMAP; MF_04075; HBV_HBSAG; 1.
DR   InterPro; IPR000349; HBV_HBSAG.
DR   Pfam; PF00695; vMSA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative initiation; Alternative splicing;
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   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT   CHAIN           2..400
FT                   /note="Large envelope protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT                   /id="PRO_0000038105"
FT   TOPO_DOM        2..253
FT                   /note="Intravirion; in internal conformation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT   TOPO_DOM        2..181
FT                   /note="Virion surface; in external conformation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT   TRANSMEM        182..202
FT                   /note="Helical; Name=TM1; Note=In external conformation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT   TOPO_DOM        203..253
FT                   /note="Intravirion; in external conformation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT   TRANSMEM        254..274
FT                   /note="Helical; Name=TM2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT   TOPO_DOM        275..348
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT   TOPO_DOM        370..375
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT   TRANSMEM        376..398
FT                   /note="Helical; Name=TM3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT   TOPO_DOM        399..400
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..174
FT                   /note="Pre-S"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT   REGION          2..119
FT                   /note="Pre-S1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT   REGION          89..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..174
FT                   /note="Pre-S2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT   COMPBIAS        93..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04075"
FT   VAR_SEQ         1..174
FT                   /note="Missing (in isoform S)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_031358"
FT   VAR_SEQ         1..119
FT                   /note="Missing (in isoform M)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_031359"
FT   MOD_RES         Q02317-2:1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        Q02317-2:4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   400 AA;  43741 MW;  7EBD53A004136BD2 CRC64;
     MGGWSSKPRK GMGTNLSVPN PLGFFPDHQL DPAFGANSNN PDWDFNPIKD HWPQANQVGV
     GAFGPGFTPP HGGVLGWSPQ AQGILATVPA MPPPASTNRQ SGRQPTPISP PLRDSHPQAM
     QWNSTAFHQA LQDPRVRGLY FPAGGSSSGT LNPVPTIASH ISSISSRIGD PAPNMENITS
     GFLGPLLVLQ AGFFLLTRIL TIPQSLDSWW TSLNFLGGAP VCLGQNSQSP TSNHSPTSCP
     PICPGYRWMC LRRFIIFLFI LLLCLIFLLV LLDYQGMLPV CPLIPGSTTT STGPCKTCTT
     PAQGNSMFPS CCCTKPTDGN CTCIPIPSSW AFAKYLWEWA SVRFSWLSLL VPFVQWFVGL
     SPTVWLSAIW MMWYWGPSLY NILSPFIPLL PIFFCLWVYI
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024