P68979 (E3GL_ADE06) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 9, 2013.
Version 43.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Early E3 18.5 kDa glycoprotein Alternative name(s): E3-19K E3gp 19 kDa Short name=E19 GP19K |
| Organism | Human adenovirus C serotype 6 (HAdV-6) (Human adenovirus 6) |
| Taxonomic identifier | 10534 [NCBI] |
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Adenoviridae › Mastadenovirus › ![]() |
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
Protein attributes
| Sequence length | 159 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Binds and retains class I heavy chains in the endoplasmic reticulum during the early period of virus infection, thereby impairing their transport to the cell surface. Also delays the expression of class I alleles that it cannot affect by direct retention. Binds transporters associated with antigen processing (TAP) and acts as a tapasin inhibitor, preventing class I/TAP association. In consequence, infected cells are masked for immune recognition by cytotoxic T-lymphocytes By similarity. |
| Subcellular location | Host endoplasmic reticulum membrane; Single-pass type I membrane protein. |
| Developmental stage | Expressed at early period of virus infection. |
| Domain | The lumenal domain binds directly to the peptide-binding domain of class I molecules. The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins By similarity. |
| Post-translational modification | Both disulfide bonds are absolutely critical for the interaction with MHC antigens By similarity. N-glycosylated; high-mannose By similarity. |
| Sequence similarities | Belongs to the adenoviridae E19 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Host-virus interaction Inhibition of host adaptive immune response by virus Inhibition of host tapasin by virus Viral immunoevasion |
| Cellular component | Host endoplasmic reticulum Host membrane Membrane |
| Developmental stage | Early protein |
| Domain | Signal Transmembrane Transmembrane helix |
| Ligand | Lectin Mannose-binding |
| PTM | Disulfide bond Glycoprotein |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological_process | suppression by virus of host tapasin activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | host cell endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | mannose binding Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 17 | 17 | By similarity | ||||||||||||||||||||||
| Chain | 18 – 159 | 142 | Early E3 18.5 kDa glycoprotein | PRO_0000036485 | |||||||||||||||||||||
Regions | |||||||||||||||||||||||||
| Topological domain | 18 – 123 | 106 | Lumenal Potential | ||||||||||||||||||||||
| Transmembrane | 124 – 144 | 21 | Helical; Potential | ||||||||||||||||||||||
| Topological domain | 145 – 159 | 15 | Cytoplasmic Potential | ||||||||||||||||||||||
| Motif | 156 – 159 | 4 | Di-lysine motif By similarity | ||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||
| Glycosylation | 29 | 1 | N-linked (GlcNAc...); by host Potential | ||||||||||||||||||||||
| Glycosylation | 78 | 1 | N-linked (GlcNAc...); by host Potential | ||||||||||||||||||||||
| Disulfide bond | 28 ↔ 45 | By similarity | |||||||||||||||||||||||
| Disulfide bond | 39 ↔ 100 | By similarity | |||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||
| Beta strand | 27 – 35 | 9 | |||||||||||||||||||||||
| Beta strand | 38 – 46 | 9 | |||||||||||||||||||||||
| Beta strand | 48 – 56 | 9 | |||||||||||||||||||||||
| Beta strand | 59 – 69 | 11 | |||||||||||||||||||||||
| Beta strand | 76 – 83 | 8 | |||||||||||||||||||||||
| Beta strand | 86 – 93 | 8 | |||||||||||||||||||||||
| Helix | 96 – 103 | 8 | |||||||||||||||||||||||
| Helix | 105 – 109 | 5 | |||||||||||||||||||||||
Sequences
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References
| [1] | "Sequence analysis of group C human adenoviruses type 1 and 6 for five genes of region E3." Reichmann H., Schaarschmidt E., Geisler B., Hausmann J., Ortmann D., Bauer U., Flunker G., Seidel W. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | Y16037 Genomic DNA. Translation: CAA75990.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR006965. Adenovirus_Gp19K. [Graphical view] | ||||||||||||
| Pfam | PF04881. Adeno_GP19K. 1 hit. [Graphical view] | ||||||||||||
| ProDom | PD006739. Adeno_GP19K. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | E3GL_ADE06 | ||||||||
| Accession | Primary (citable) accession number: P68979 Secondary accession number(s): P03251 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
