| Tag |
Content |
LipidDB ID |
LipidDB-490133-00791 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
8.4 |
Molecular Weight |
42766.45 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
Large envelope protein |
Protein Synonyms/Alias |
L glycoprotein; L-HBsAg; LHB; Large S protein; Large surface protein; Major surface antigen; |
Gene Name |
S |
Gene Synonyms/Alias |
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Created Date |
21-JUL-1986 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGQNLSTSN | [1] | N-Myristoylation |
|
Organism |
Hepatitis B virus genotype D subtype ayw (isolat France/Tiollais/1979) (HBV-D) |
NCBI Taxa ID |
490133 |
Reference |
[1] Meier A, Mehrle S, Weiss TS, Mier W, Urban S. Myristoylated PreS1-domain ofthe hepatitis B virus L-protein mediates specific binding to differentiatedhepatocytes. Hepatology. 2013 Jul;58(1):31-42. doi: 10.1002/hep.26181. Epub 2013 Mar 14.[ PMID:23213046]
|
Functional Description |
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). |
Sequence Annotation |
Topological domain: 2 242 Intravirion; in internal conformation.
Topological domain: 2 170 Virion surface; in external conformation.
Transmembrane: 171 191 Helical; Note=In external conformation.
Topological domain: 192 242 Intravirion; in external conformation.
Transmembrane: 243 263 Helical.
Topological domain: 264 337 Virion surface.
Transmembrane: 338 358 Helical.
Topological domain: 359 364 Intravirion.
Transmembrane: 365 387 Helical.
Topological domain: 388 389 Virion surface.
Region: 2 163 Pre-S.
Region: 2 108 Pre-S1.
Region: 109 163 Pre-S2.
Modified residue: 109 109 N-acetylmethionine; by host; in isoformM; partial.
|
Protein Length |
389 AA. |
Protein Sequence
(Canonical) |
MGQNLSTSNP LGFFPDHQLD PAFRANTANP DWDFNPNKDT WPDANKVGAG AFGLGFTPPH 60
GGLLGWSPQA QGILQTLPAN PPPASTNRQS GRQPTPLSPP LRNTHPQAMQ WNSTTFHQTL 120
QDPRVRGLYF PAGGSSSGTV NPVLTTASPL SSIFSRIGDP ALNMENITSG FLGPLLVLQA 180
GFFLLTRILT IPQSLDSWWT SLNFLGGTTV CLGQNSQSPT SNHSPTSCPP TCPGYRWMCL 240
RRFIIFLFIL LLCLIFLLVL LDYQGMLPVC PLIPGSSTTS TGPCRTCMTT AQGTSMYPSC 300
CCTKPSDGNC TCIPIPSSWA FGKFLWEWAS ARFSWLSLLV PFVQWFVGLS PTVWLSVIWM 360
MWYWGPSLYS ILSPFLPLLP IFFCLWVYI 389
|
FASTA
(Canonical) |
>LipidDB-490133-00791|P03138
MGQNLSTSNPLGFFPDHQLDPAFRANTANPDWDFNPNKDTWPDANKVGAGAFGLGFTPPH
GGLLGWSPQAQGILQTLPANPPPASTNRQSGRQPTPLSPPLRNTHPQAMQWNSTTFHQTL
QDPRVRGLYFPAGGSSSGTVNPVLTTASPLSSIFSRIGDPALNMENITSGFLGPLLVLQA
GFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQSPTSNHSPTSCPPTCPGYRWMCL
RRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCRTCMTTAQGTSMYPSC
CCTKPSDGNCTCIPIPSSWAFGKFLWEWASARFSWLSLLVPFVQWFVGLSPTVWLSVIWM
MWYWGPSLYSILSPFLPLLPIFFCLWVYI
|
Gene Ontology |
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW GO:0019012; C:virion; IEA:UniProtKB-KW GO:0075513; P:caveolin-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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