A0A067YTT7 · A0A067YTT7_HBV
- ProteinLarge envelope protein
- GeneP
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids400 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein.
The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | virion membrane | |
Biological Process | caveolin-mediated endocytosis of virus by host cell | |
Biological Process | fusion of virus membrane with host endosome membrane | |
Biological Process | virion attachment to host cell |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameLarge envelope protein
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Riboviria > Pararnavirae > Artverviricota > Revtraviricetes > Blubervirales > Hepadnaviridae > Orthohepadnavirus
- Virus hosts
Accessions
- Primary accessionA0A067YTT7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 2-181 | Virion surface; in external conformation | ||||
Sequence: GGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPAFKANSENPDWDLNPHKDNWPDANKVGVGAFGPGFTPPHGGLLGWSPQAQSIFTTVPAAPPPASTNRQSGRQPTPLSPPLRDTHPQAMQWNSTTFHQTLQDPRVRALYFPAGGSSSGTVSPAQNTVSTISSILSKTGDPVPNMENIASG | ||||||
Topological domain | 2-253 | Intravirion; in internal conformation | ||||
Sequence: GGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPAFKANSENPDWDLNPHKDNWPDANKVGVGAFGPGFTPPHGGLLGWSPQAQSIFTTVPAAPPPASTNRQSGRQPTPLSPPLRDTHPQAMQWNSTTFHQTLQDPRVRALYFPAGGSSSGTVSPAQNTVSTISSILSKTGDPVPNMENIASGLLGPLLVLQAGFFLLTKILTIPQSLDSWWTSLNFLGGTPVCLGQNSQSQISSHSPTCCPPICPGYRWMCLRR | ||||||
Topological domain | 203-253 | Intravirion; in external conformation | ||||
Sequence: PQSLDSWWTSLNFLGGTPVCLGQNSQSQISSHSPTCCPPICPGYRWMCLRR | ||||||
Transmembrane | 254-272 | Helical | ||||
Sequence: FIIFLCILLLCLIFLLVLL | ||||||
Topological domain | 275-348 | Virion surface | ||||
Sequence: QGMLPVCPLIPGSSTTSTGPCKTCTTPAHGTSMFPSCCCTKPTDGNCTCIPIPSSWAFAKYLWEWASVRFSWLS | ||||||
Transmembrane | 344-373 | Helical | ||||
Sequence: FSWLSLLVPFVQWFVGLSPTVWLSVIWMMW | ||||||
Topological domain | 370-375 | Intravirion | ||||
Sequence: WMMWYW | ||||||
Transmembrane | 379-399 | Helical | ||||
Sequence: LYNILSPFMPLLPIFFCLWVY | ||||||
Topological domain | 399-400 | Virion surface | ||||
Sequence: YI |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed; by host | ||||
Sequence: M | ||||||
Lipidation | 2 | N-myristoyl glycine; by host | ||||
Sequence: G | ||||||
Chain | PRO_5023575527 | 2-400 | Large envelope protein | |||
Sequence: GGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPAFKANSENPDWDLNPHKDNWPDANKVGVGAFGPGFTPPHGGLLGWSPQAQSIFTTVPAAPPPASTNRQSGRQPTPLSPPLRDTHPQAMQWNSTTFHQTLQDPRVRALYFPAGGSSSGTVSPAQNTVSTISSILSKTGDPVPNMENIASGLLGPLLVLQAGFFLLTKILTIPQSLDSWWTSLNFLGGTPVCLGQNSQSQISSHSPTCCPPICPGYRWMCLRRFIIFLCILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCKTCTTPAHGTSMFPSCCCTKPTDGNCTCIPIPSSWAFAKYLWEWASVRFSWLSLLVPFVQWFVGLSPTVWLSVIWMMWYWGPSLYNILSPFMPLLPIFFCLWVYI |
Post-translational modification
Isoform M is N-terminally acetylated by host at a ratio of 90%, and N-glycosylated by host at the pre-S2 region.
Myristoylated.
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-24 | Disordered | ||||
Sequence: MGGWSSKPRKGMGTNLSVPNPLGF | ||||||
Region | 2-119 | Pre-S1 | ||||
Sequence: GGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPAFKANSENPDWDLNPHKDNWPDANKVGVGAFGPGFTPPHGGLLGWSPQAQSIFTTVPAAPPPASTNRQSGRQPTPLSPPLRDTHPQA | ||||||
Region | 2-174 | Pre-S | ||||
Sequence: GGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPAFKANSENPDWDLNPHKDNWPDANKVGVGAFGPGFTPPHGGLLGWSPQAQSIFTTVPAAPPPASTNRQSGRQPTPLSPPLRDTHPQAMQWNSTTFHQTLQDPRVRALYFPAGGSSSGTVSPAQNTVSTISSILSKTGDPVPN | ||||||
Compositional bias | 87-108 | Polar residues | ||||
Sequence: TVPAAPPPASTNRQSGRQPTPL | ||||||
Region | 87-114 | Disordered | ||||
Sequence: TVPAAPPPASTNRQSGRQPTPLSPPLRD | ||||||
Region | 120-174 | Pre-S2 | ||||
Sequence: MQWNSTTFHQTLQDPRVRALYFPAGGSSSGTVSPAQNTVSTISSILSKTGDPVPN |
Domain
The large envelope protein is synthesized with the pre-S region at the cytosolic side of the endoplasmic reticulum and, hence will be within the virion after budding. Therefore the pre-S region is not N-glycosylated. Later a post-translational translocation of N-terminal pre-S and TM1 domains occur in about 50% of proteins at the virion surface. These molecules change their topology by an unknown mechanism, resulting in exposure of pre-S region at virion surface. For isoform M in contrast, the pre-S2 region is translocated cotranslationally to the endoplasmic reticulum lumen and is N-glycosylated.
Sequence similarities
Belongs to the orthohepadnavirus major surface antigen family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length400
- Mass (Da)43,840
- Last updated2014-10-01 v1
- ChecksumF91EE546F3BD23F6
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 87-108 | Polar residues | ||||
Sequence: TVPAAPPPASTNRQSGRQPTPL |