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Protein

Early E3 18.5 kDa glycoprotein

Gene
N/A
Organism
Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processHost-virus interaction, Inhibition of host adaptive immune response by virus, Inhibition of host tapasin by virus, Viral immunoevasion
LigandLectin, Mannose-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Early E3 18.5 kDa glycoprotein
Alternative name(s):
E3-19K
E3gp 19 kDa
Short name:
E19
GP19K
OrganismiHuman adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Taxonomic identifieri10515 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAdenoviridaeMastadenovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008167 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini18 – 123LumenalSequence analysisAdd BLAST106
Transmembranei124 – 144HelicalSequence analysisAdd BLAST21
Topological domaini145 – 159CytoplasmicSequence analysisAdd BLAST15

GO - Cellular componenti

Keywords - Cellular componenti

Host endoplasmic reticulum, Host membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi28C → S: Complete loss of binding to Tw1.3 epitope. 1 Publication1
Mutagenesisi39C → A or S: 60% loss of binding to Tw1.3 epitope. 1 Publication1
Mutagenesisi45C → S: Complete loss of binding to Tw1.3 epitope. 1 Publication1
Mutagenesisi100C → S: 60% loss of binding to Tw1.3 epitope. 1 Publication1
Mutagenesisi118C → S: No effect. 1 Publication1
Mutagenesisi126C → S: No effect. 1 Publication1
Mutagenesisi139C → S: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 171 PublicationAdd BLAST17
ChainiPRO_000003648218 – 159Early E3 18.5 kDa glycoproteinAdd BLAST142

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi28 ↔ 451 Publication
Glycosylationi29N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi39 ↔ 1001 Publication
Glycosylationi78N-linked (GlcNAc...); by hostSequence analysis1

Post-translational modificationi

Both disulfide bonds are absolutely critical for the interaction with MHC antigens.
N-glycosylated; high-mannose.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP68978.

Expressioni

Developmental stagei

Expressed at early period of virus infection.

Keywords - Developmental stagei

Early protein

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SPBPJ4664.04Q96WV52EBI-4407041,EBI-8503699From Schizosaccharomyces pombe (strain 972 / ATCC 24843).

Protein-protein interaction databases

IntActiP68978. 8 interactors.

Structurei

3D structure databases

SMRiP68978.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi156 – 159Di-lysine motif4

Domaini

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.

Sequence similaritiesi

Belongs to the adenoviridae E19 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

OrthoDBiVOG0900012T.

Family and domain databases

InterProiView protein in InterPro
IPR006965. Adenovirus_Gp19K.
PfamiView protein in Pfam
PF04881. Adeno_GP19K. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD006739. Adeno_GP19K. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P68978-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYMILGLLA LAAVCSAAKK VEFKEPACNV TFKSEANECT TLIKCTTEHE
60 70 80 90 100
KLIIRHKDKI GKYAVYAIWQ PGDTNDYNVT VFQGENRKTF MYKFPFYEMC
110 120 130 140 150
DITMYMSKQY KLWPPQKCLE NTGTFCSTAL LITALALVCT LLYLKYKSRR

SFIDEKKMP
Length:159
Mass (Da):18,438
Last modified:July 21, 1986 - v1
Checksum:iED2519547E18AEB0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01917 Genomic DNA. Translation: AAA92221.1.
PIRiA03821. Q6ADE.
RefSeqiAP_000184.1. AC_000007.1.
NP_040531.1. NC_001405.1.

Genome annotation databases

GeneIDi2652987.
KEGGivg:2652987.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01917 Genomic DNA. Translation: AAA92221.1.
PIRiA03821. Q6ADE.
RefSeqiAP_000184.1. AC_000007.1.
NP_040531.1. NC_001405.1.

3D structure databases

SMRiP68978.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP68978. 8 interactors.

Proteomic databases

PRIDEiP68978.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2652987.
KEGGivg:2652987.

Phylogenomic databases

OrthoDBiVOG0900012T.

Family and domain databases

InterProiView protein in InterPro
IPR006965. Adenovirus_Gp19K.
PfamiView protein in Pfam
PF04881. Adeno_GP19K. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD006739. Adeno_GP19K. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiE3GL_ADE02
AccessioniPrimary (citable) accession number: P68978
Secondary accession number(s): P03251
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: March 15, 2017
This is version 61 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.