| Tag |
Content |
LipidDB ID |
LipidDB-489543-00815 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
8.71 |
Molecular Weight |
36230.1 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
Truncated S protein |
Protein Synonyms/Alias |
L glycoprotein; L-HBsAg; LHB; Large S protein; Large surface protein; Major surface antigen; St; |
Gene Name |
S |
Gene Synonyms/Alias |
|
Created Date |
21-JUL-1986 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGQHPAKSM | [1] | N-Myristoylation |
|
Organism |
Duck hepatitis B virus (strain United States/DHBV-16) (DHBV) |
NCBI Taxa ID |
489543 |
Reference |
[1] Macrae DR, Bruss V, Ganem D. Myristylation of a duck hepatitis B virusenvelope protein is essential for infectivity but not for virus assembly.Virology. 1991 Mar;181(1):359-63.[ PMID:1994583]
|
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. The large envelope protein probably also assumes fusion between virion and host membranes. 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: 2 236 Cytoplasmic; in internal conformation.
Topological domain: 2 163 Extracellular; in external conformation.
Transmembrane: 164 184 Helical; Name=TM1; Note=In externalconformation.
Topological domain: 185 236 Cytoplasmic; in external conformation.
Transmembrane: 237 257 Helical; Name=TM2.
Topological domain: 258 282 Extracellular.
Transmembrane: 283 303 Helical; Name=TM3.
Topological domain: 304 328 Cytoplasmic.
Region: 2 161 Pre-S.
Functional site: ?238 ?239 Cleavage; by host.
Modified residue: 118 118 Phosphoserine; by host.
|
Protein Length |
328 AA. |
Protein Sequence
(Canonical) |
MGQHPAKSMD VRRIEGGEIL LNQLAGRMIP KGTLTWSGKF PTLDHVLDHV QTMEEINTLQ 60
NQGAWPAGAG RRVGLSNPTP QEIPQPQWTP EEDQKAREAF RRYQEERPPE TTTIPPSSPP 120
QWKLQPGDDP LLGNQSLLET HPLYQSEPAV PVIKTPPLKK KMSGTFGGIL AGLIGLLVSF 180
FLLIKILEIL RRLDWWWISL SSPKGKMQCA FQDTGAQISP HYVGSCPWGC PGFLWTYLRL 240
FIIFLLILLV AAGLLYLTDN GSTILGKLQW ASVSALFSSI SSLLPSDPKS LVALTFGLSL 300
IWMTSSSATQ TLVTLTQLAT LSALFYKS 328
|
FASTA
(Canonical) |
>LipidDB-489543-00815|P03145
MGQHPAKSMDVRRIEGGEILLNQLAGRMIPKGTLTWSGKFPTLDHVLDHVQTMEEINTLQ
NQGAWPAGAGRRVGLSNPTPQEIPQPQWTPEEDQKAREAFRRYQEERPPETTTIPPSSPP
QWKLQPGDDPLLGNQSLLETHPLYQSEPAVPVIKTPPLKKKMSGTFGGILAGLIGLLVSF
FLLIKILEILRRLDWWWISLSSPKGKMQCAFQDTGAQISPHYVGSCPWGCPGFLWTYLRL
FIIFLLILLVAAGLLYLTDNGSTILGKLQWASVSALFSSISSLLPSDPKSLVALTFGLSL
IWMTSSSATQTLVTLTQLATLSALFYKS
|
Gene Ontology |
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW GO:0019012; C:virion; IEA:UniProtKB-KW GO:0039663; P:membrane fusion involved in viral entry into host cell; 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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