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P68979 (E3GL_ADE06) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Early E3 18.5 kDa glycoprotein
Alternative name(s):
E3-19K
E3gp 19 kDa
Short name=E19
GP19K
OrganismHuman adenovirus C serotype 6 (HAdV-6) (Human adenovirus 6)
Taxonomic identifier10534 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageAdenoviridaeMastadenovirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length159 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 By similarity
Chain18 – 159142Early E3 18.5 kDa glycoprotein
PRO_0000036485

Regions

Topological domain18 – 123106Lumenal Potential
Transmembrane124 – 14421Helical; Potential
Topological domain145 – 15915Cytoplasmic Potential
Motif156 – 1594Di-lysine motif By similarity

Amino acid modifications

Glycosylation291N-linked (GlcNAc...); by host Potential
Glycosylation781N-linked (GlcNAc...); by host Potential
Disulfide bond28 ↔ 45 By similarity
Disulfide bond39 ↔ 100 By similarity

Secondary structure

................. 159
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P68979 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: ED2519547E18AEB0

FASTA15918,438
        10         20         30         40         50         60 
MRYMILGLLA LAAVCSAAKK VEFKEPACNV TFKSEANECT TLIKCTTEHE KLIIRHKDKI 

        70         80         90        100        110        120 
GKYAVYAIWQ PGDTNDYNVT VFQGENRKTF MYKFPFYEMC DITMYMSKQY KLWPPQKCLE 

       130        140        150 
NTGTFCSTAL LITALALVCT LLYLKYKSRR SFIDEKKMP 

« Hide

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
EntryMethodResolution (Å)ChainPositionsPDBsum
4E5XX-ray1.95G/H18-117[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR006965. Adenovirus_Gp19K.
[Graphical view]
PfamPF04881. Adeno_GP19K. 1 hit.
[Graphical view]
ProDomPD006739. Adeno_GP19K. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameE3GL_ADE06
AccessionPrimary (citable) accession number: P68979
Secondary accession number(s): P03251
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: February 19, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references