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 |