Detail Information for IndEnz0002006805
IED ID IndEnz0002006805
Enzyme Type ID protease006805
Protein Name Large envelope protein
L glycoprotein
L-HBsAg
LHB
Large S protein
Large surface protein
Major surface antigen

Cleaved into: Truncated S protein
St
Gene Name S
Organism Duck hepatitis B virus (strain United States/DHBV-16) (DHBV)
Taxonomic Lineage Viruses Riboviria Pararnavirae Artverviricota Revtraviricetes Blubervirales Hepadnaviridae Avihepadnavirus (avian hepatitis B-type viruses) Duck hepatitis B virus Duck hepatitis B virus (strain United States/DHBV-16) (DHBV)
Enzyme Sequence MGQHPAKSMDVRRIEGGEILLNQLAGRMIPKGTLTWSGKFPTLDHVLDHVQTMEEINTLQNQGAWPAGAGRRVGLSNPTPQEIPQPQWTPEEDQKAREAFRRYQEERPPETTTIPPSSPPQWKLQPGDDPLLGNQSLLETHPLYQSEPAVPVIKTPPLKKKMSGTFGGILAGLIGLLVSFFLLIKILEILRRLDWWWISLSSPKGKMQCAFQDTGAQISPHYVGSCPWGCPGFLWTYLRLFIIFLLILLVAAGLLYLTDNGSTILGKLQWASVSALFSSISSLLPSDPKSLVALTFGLSLIWMTSSSATQTLVTLTQLATLSALFYKS
Enzyme Length 328
Uniprot Accession Number P03145
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: 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). {ECO:0000250}.; FUNCTION: Truncated S protein may be involved in translocation of pre-S domain through the virion membrane.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (1); Chain (2); Compositional bias (1); Glycosylation (1); Initiator methionine (1); Lipidation (1); Modified residue (1); Mutagenesis (2); Region (2); Site (1); Topological domain (5); Transmembrane (3)
Keywords Alternative initiation;Fusion of virus membrane with host membrane;Glycoprotein;Host-virus interaction;Lipoprotein;Membrane;Myristate;Phosphoprotein;Reference proteome;Transmembrane;Transmembrane helix;Viral attachment to host cell;Viral penetration into host cytoplasm;Virion;Virus entry into host cell
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Virion membrane.
Modified Residue MOD_RES 118; /note=Phosphoserine; by host; /evidence=ECO:0000269|PubMed:9820150
Post Translational Modification PTM: Myristoylation contributes importantly to DHBV infectivity. It is most likely required for an early step of the life cycle involving the entry or uncoating of virus particles. {ECO:0000269|PubMed:1994583}.; PTM: Phosphorylated on pre-S domain for about 50% of L proteins, the L chains with internal pre-S region (Li-HBsAg). {ECO:0000269|PubMed:7933117, ECO:0000269|PubMed:9820150}.; PTM: Isoform S may be cleaved by a cellular protease to produce truncated S protein.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 36,230
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda